2024-03-28T23:06:04Zhttp://repository.helmholtz-hzi.de/oai/requestoai:repository.helmholtz-hzi.de:10033/84062019-08-30T11:32:37Zcom_10033_6815com_10033_6814col_10033_6886
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http://hdl.handle.net/10033/8406
88729
en_US
American Society for Microbiology
Copyright © 2000, American Society for Microbiology
Distribution and Antigenicity of Fibronectin Binding Proteins (SfbI and SfbII) of Streptococcus pyogenes Clinical Isolates from the Northern Territory, Australia
YES
2018-06-12T17:21:01Z
ORIGINAL
Godfellow et al_final.pdf
Godfellow et al_final.pdf
allowed publisher's PDF
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165374
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MD5
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CC-LICENSE
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49
https://hzi.openrepository.com/bitstream/10033/8406/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
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false
license_text
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MD5
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https://hzi.openrepository.com/bitstream/10033/8406/4/license_rdf
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MD5
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Godfellow et al_final.pdf.txt
Godfellow et al_final.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/8406/7/Godfellow%20et%20al_final.pdf.txt
24b78191d93b17cf68727d7174f37c45
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THUMBNAIL
Godfellow et al_final.pdf.jpg
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Generated Thumbnail
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https://hzi.openrepository.com/bitstream/10033/8406/8/Godfellow%20et%20al_final.pdf.jpg
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10033/8406
oai:hzi.openrepository.com:10033/8406
2019-08-30 11:32:37.965
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85072019-08-30T11:32:38Zcom_10033_6815com_10033_6814col_10033_6886
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Applied and Environmental Microbiology 2002 68(7):3606-3613
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10.1128/AEM.68.7.3606-3613.2002
http://hdl.handle.net/10033/8507
126806
en_US
American Society for Microbiology
Copyright © 2002, American Society for Microbiology
Changes in Bacterioplankton Community Structure and Activity with Depth in a Eutrophic Lake as Revealed by 5S rRNA Analysis
YES
2018-06-13T01:29:53Z
ORIGINAL
Dominik and Höfle_final.pdf
Dominik and Höfle_final.pdf
allowed publisher's PDF
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MD5
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CC-LICENSE
license_url
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https://hzi.openrepository.com/bitstream/10033/8507/2/license_url
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MD5
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MD5
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TEXT
Dominik and Höfle_final.pdf.txt
Dominik and Höfle_final.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/8507/7/Dominik%20and%20H%c3%b6fle_final.pdf.txt
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THUMBNAIL
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Generated Thumbnail
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https://hzi.openrepository.com/bitstream/10033/8507/8/Dominik%20and%20H%c3%b6fle_final.pdf.jpg
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10033/8507
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85092019-08-30T11:32:38Zcom_10033_6815com_10033_6814col_10033_6886
Jansen, W. T. M.
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2007-02-19T09:20:40Z
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Infection and Immunity 2002 70(9):5202-5207
0019-9567
1098-5522
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10.1128/IAI.70.9.5202-5207.2002
http://hdl.handle.net/10033/8509
128270
en_US
American Society for Microbiology
Copyright © 2002, American Society for Microbiology
Hydrogen Peroxide-Mediated Killing of Caenorhabditis elegans by Streptococcus pyogenes
YES
2018-06-13T21:26:42Z
ORIGINAL
Jansen et al_final.pdf
Jansen et al_final.pdf
free text from BioMed's repository PubMedCentral
application/pdf
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https://hzi.openrepository.com/bitstream/10033/8509/1/Jansen%20et%20al_final.pdf
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MD5
1
true
CC-LICENSE
license_url
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49
https://hzi.openrepository.com/bitstream/10033/8509/2/license_url
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MD5
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false
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MD5
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TEXT
Jansen et al_final.pdf.txt
Jansen et al_final.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/8509/7/Jansen%20et%20al_final.pdf.txt
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MD5
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THUMBNAIL
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Generated Thumbnail
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10033/8509
oai:hzi.openrepository.com:10033/8509
2019-08-30 11:32:38.624
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85002019-08-30T11:32:38Zcom_10033_6815com_10033_6814col_10033_6886
Erdogan, Sezgin
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Talay, Susanne R.
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Rohde, Manfred
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Flores, Aurea E.
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Guzmán, Carlos A.
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Chhatwal, Gursharan S.
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2007-02-19T08:48:58Z
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2007-02-19T08:48:58Z
2002-02
Infection and Immunity 2002 70(2):803-811
0019-9567
1098-5522
11796614
http://hdl.handle.net/10033/8500
127721
en_US
American Society for Microbiology
Copyright © 2002, American Society for Microbiology
Molecular Analysis of Group B Protective Surface Protein, a New Cell Surface Protective Antigen of Group B Streptococci
YES
2018-06-13T16:02:58Z
ORIGINAL
Erdogan et al_final.pdf
Erdogan et al_final.pdf
free text from BMC's repository PubMedCentral
application/pdf
1152098
https://hzi.openrepository.com/bitstream/10033/8500/1/Erdogan%20et%20al_final.pdf
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MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8500/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
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application/octet-stream
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https://hzi.openrepository.com/bitstream/10033/8500/3/license_text
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MD5
3
false
license_rdf
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application/octet-stream
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https://hzi.openrepository.com/bitstream/10033/8500/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Erdogan et al_final.pdf.txt
Erdogan et al_final.pdf.txt
Extracted Text
text/plain
48721
https://hzi.openrepository.com/bitstream/10033/8500/7/Erdogan%20et%20al_final.pdf.txt
a97c7b54cb5ead0c907f8c8799712aa5
MD5
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false
THUMBNAIL
Erdogan et al_final.pdf.jpg
Erdogan et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
38381
https://hzi.openrepository.com/bitstream/10033/8500/8/Erdogan%20et%20al_final.pdf.jpg
3ec70ce9097084d3e3277df744f2ae6d
MD5
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10033/8500
oai:hzi.openrepository.com:10033/8500
2019-08-30 11:32:38.728
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86112019-08-30T11:32:39Zcom_10033_6815com_10033_6814col_10033_6886
Barthel, Manja
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500
Hapfelmeier, Siegfried
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500
Quintanilla-Martínez, Leticia
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Kremer, Marcus
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500
Rohde, Manfred
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500
Hogardt, Michael
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Pfeffer, Klaus
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Rüssmann, Holger
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Hardt, Wolf-Dietrich
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2007-02-20T13:07:06Z
2003-05
2007-02-20T13:07:06Z
2003-05
Infection and Immunity 2003 71(5):2839-2858
0019-9567
1098-5522
12704158
10.1128/IAI.71.5.2839-2858.2003
http://hdl.handle.net/10033/8611
153285
en_US
American Society for Microbiology
Copyright © 2003, American Society for Microbiology
Pretreatment of Mice with Streptomycin Provides a Salmonella enterica Serovar Typhimurium Colitis Model That Allows Analysis of Both Pathogen and Host
YES
2018-06-13T15:48:49Z
ORIGINAL
Barthel et al_final.pdf
Barthel et al_final.pdf
free copy from PubMed repository
application/pdf
5845425
https://hzi.openrepository.com/bitstream/10033/8611/1/Barthel%20et%20al_final.pdf
9170b2a54e56a5d71994a8da6a6ce6ff
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8611/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
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https://hzi.openrepository.com/bitstream/10033/8611/3/license_text
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MD5
3
false
license_rdf
license_rdf
application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8611/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Barthel et al_final.pdf.txt
Barthel et al_final.pdf.txt
Extracted Text
text/plain
98475
https://hzi.openrepository.com/bitstream/10033/8611/7/Barthel%20et%20al_final.pdf.txt
37c9ba647841b43d221580f3401060ad
MD5
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false
THUMBNAIL
Barthel et al_final.pdf.jpg
Barthel et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
39571
https://hzi.openrepository.com/bitstream/10033/8611/8/Barthel%20et%20al_final.pdf.jpg
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MD5
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10033/8611
oai:hzi.openrepository.com:10033/8611
2019-08-30 11:32:39.02
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85312019-08-30T11:32:39Zcom_10033_6815com_10033_6814col_10033_6886
Valenti-Weigand, P
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Rohde, Manfred
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Chhatwal, G S
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2007-02-19T10:37:07Z
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2007-02-19T10:37:07Z
1996-07
Infection and Immunity 1996 64(7):2467-2473
0019-9567
1098-5522
8698468
http://hdl.handle.net/10033/8531
174099
en_US
Entry and intracellular survival of group B streptococci in J774 macrophages.
YES
2018-06-12T18:09:48Z
ORIGINAL
Valenti-Weigand et al.final.pdf
Valenti-Weigand et al.final.pdf
free text from BMC's repository PubMed Central
application/pdf
1155039
https://hzi.openrepository.com/bitstream/10033/8531/1/Valenti-Weigand%20et%20al.final.pdf
431110eb9b8677978c80255d046c51be
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8531/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
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https://hzi.openrepository.com/bitstream/10033/8531/3/license_text
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MD5
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false
license_rdf
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application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8531/4/license_rdf
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MD5
4
false
TEXT
Valenti-Weigand et al.final.pdf.txt
Valenti-Weigand et al.final.pdf.txt
Extracted Text
text/plain
38524
https://hzi.openrepository.com/bitstream/10033/8531/7/Valenti-Weigand%20et%20al.final.pdf.txt
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MD5
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THUMBNAIL
Valenti-Weigand et al.final.pdf.jpg
Valenti-Weigand et al.final.pdf.jpg
Generated Thumbnail
image/jpeg
33465
https://hzi.openrepository.com/bitstream/10033/8531/8/Valenti-Weigand%20et%20al.final.pdf.jpg
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MD5
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10033/8531
oai:hzi.openrepository.com:10033/8531
2019-08-30 11:32:39.88
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85322019-08-30T11:32:15Zcom_10033_6815com_10033_6814col_10033_6886
Jerlström, P G
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Talay, S R
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Valentin-Weigand, P
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Timmis, K N
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Chhatwal, G S
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2007-02-19T10:37:53Z
1996-07
2007-02-19T10:37:53Z
1996-07
Infection and Immunity 1996 64(7):2787-2793
0019-9567
1098-5522
8698509
http://hdl.handle.net/10033/8532
174140
en_US
Identification of an immunoglobulin A binding motif located in the beta-antigen of the c protein complex of group B streptococci.
YES
2018-06-14T09:16:20Z
ORIGINAL
Jerlström et al_final.pdf
Jerlström et al_final.pdf
allowed publisher's PDF
application/pdf
520881
https://hzi.openrepository.com/bitstream/10033/8532/1/Jerlstr%c3%b6m%20et%20al_final.pdf
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MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8532/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
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false
license_text
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https://hzi.openrepository.com/bitstream/10033/8532/3/license_text
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MD5
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license_rdf
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https://hzi.openrepository.com/bitstream/10033/8532/4/license_rdf
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MD5
4
false
TEXT
Jerlström et al_final.pdf.txt
Jerlström et al_final.pdf.txt
Extracted Text
text/plain
39620
https://hzi.openrepository.com/bitstream/10033/8532/7/Jerlstr%c3%b6m%20et%20al_final.pdf.txt
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MD5
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THUMBNAIL
Jerlström et al_final.pdf.jpg
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Generated Thumbnail
image/jpeg
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https://hzi.openrepository.com/bitstream/10033/8532/8/Jerlstr%c3%b6m%20et%20al_final.pdf.jpg
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MD5
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10033/8532
oai:hzi.openrepository.com:10033/8532
2019-08-30 11:32:15.55
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85342019-08-30T11:24:30Zcom_10033_6815com_10033_6814col_10033_6886
Molinari, Gabriella
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Talay, S R
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Valentin-Weigand, P
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Rohde, Manfred
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500
Chhatwal, G S
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500
2007-02-19T10:39:27Z
1997-04
2007-02-19T10:39:27Z
1997-04
Infection and Immunity 1997 65(4):1357-1363
0019-9567
1098-5522
9119474
http://hdl.handle.net/10033/8534
175140
en_US
The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells.
YES
2018-06-12T23:18:45Z
ORIGINAL
Molinari et al_final.pdf
Molinari et al_final.pdf
free text from BMC's repository PubMedCentral
application/pdf
708961
https://hzi.openrepository.com/bitstream/10033/8534/1/Molinari%20et%20al_final.pdf
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MD5
1
true
CC-LICENSE
license_url
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text/plain
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https://hzi.openrepository.com/bitstream/10033/8534/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
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false
license_text
license_text
application/octet-stream
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MD5
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https://hzi.openrepository.com/bitstream/10033/8534/4/license_rdf
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MD5
4
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TEXT
Molinari et al_final.pdf.txt
Molinari et al_final.pdf.txt
Extracted Text
text/plain
36075
https://hzi.openrepository.com/bitstream/10033/8534/7/Molinari%20et%20al_final.pdf.txt
d9840ce5414aa55ea49452c4b3771f74
MD5
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THUMBNAIL
Molinari et al_final.pdf.jpg
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Generated Thumbnail
image/jpeg
37451
https://hzi.openrepository.com/bitstream/10033/8534/8/Molinari%20et%20al_final.pdf.jpg
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MD5
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10033/8534
oai:hzi.openrepository.com:10033/8534
2019-08-30 11:24:30.039
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/85362019-08-30T11:24:30Zcom_10033_6815com_10033_6814col_10033_6886
Dinkla, Katrin
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500
Rohde, Manfred
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Jansen, Wouter T.M.
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Kaplan, Edward L.
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Chhatwal, Gursharan S.
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Talay, Susanne R.
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2007-02-19T10:41:02Z
2003-06-15
2007-02-19T10:41:02Z
2003-06-15
Journal of Clinical Investigation 2003 111(12):1905-1912
0021-9738
12813026
10.1172/JCI200317247
http://hdl.handle.net/10033/8536
161421
en_US
American Society for Clinical Investigation
Copyright © 2003, American Society for Clinical Investigation
Rheumatic fever–associated Streptococcus pyogenes isolates aggregate collagen
YES
2018-06-12T21:30:39Z
ORIGINAL
Dinkla et al_final.pdf
Dinkla et al_final.pdf
allowed PDF
application/pdf
3094225
https://hzi.openrepository.com/bitstream/10033/8536/1/Dinkla%20et%20al_final.pdf
3e2cbc4f02c9692f14d8cdd199daeeb6
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8536/2/license_url
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MD5
2
false
license_text
license_text
application/octet-stream
0
https://hzi.openrepository.com/bitstream/10033/8536/4/license_text
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MD5
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false
license_rdf
license_rdf
application/octet-stream
24332
https://hzi.openrepository.com/bitstream/10033/8536/3/license_rdf
306824103cdab5a2460a7737d9c97e69
MD5
3
false
TEXT
Dinkla et al_final.pdf.txt
Dinkla et al_final.pdf.txt
Extracted Text
text/plain
45993
https://hzi.openrepository.com/bitstream/10033/8536/7/Dinkla%20et%20al_final.pdf.txt
cc582642d6032b3552ee92aa744d3719
MD5
7
false
THUMBNAIL
Dinkla et al_final.pdf.jpg
Dinkla et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
31476
https://hzi.openrepository.com/bitstream/10033/8536/8/Dinkla%20et%20al_final.pdf.jpg
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MD5
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10033/8536
oai:hzi.openrepository.com:10033/8536
2019-08-30 11:24:30.144
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86042019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Talay, S R
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500
Valentin-Weigand, P
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Jerlström, P G
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Timmis, K N
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Chhatwal, G S
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2007-02-20T12:56:42Z
1992-09
2007-02-20T12:56:42Z
1992-09
Infection and Immunity 1992 60(9):3837-3844
0019-9567
1098-5522
1386839
http://hdl.handle.net/10033/8604
257397
Images
en_US
Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells.
YES
2018-06-13T00:01:09Z
Images
ORIGINAL
Talay et al_final.pdf
Talay et al_final.pdf
free text from BMC's repository PubMed Central
application/pdf
1766389
https://hzi.openrepository.com/bitstream/10033/8604/1/Talay%20et%20al_final.pdf
4022ca2ca24123b3631d39864a1a9773
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8604/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
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application/octet-stream
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https://hzi.openrepository.com/bitstream/10033/8604/3/license_text
5583a4be1f6dbb777e1501f0e06a0664
MD5
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false
license_rdf
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23748
https://hzi.openrepository.com/bitstream/10033/8604/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Talay et al_final.pdf.txt
Talay et al_final.pdf.txt
Extracted Text
text/plain
45263
https://hzi.openrepository.com/bitstream/10033/8604/7/Talay%20et%20al_final.pdf.txt
705ec1d0db574ed2b38517b609de809e
MD5
7
false
THUMBNAIL
Talay et al_final.pdf.jpg
Talay et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
37612
https://hzi.openrepository.com/bitstream/10033/8604/8/Talay%20et%20al_final.pdf.jpg
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MD5
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10033/8604
oai:hzi.openrepository.com:10033/8604
2019-08-30 11:25:43.235
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86592019-08-30T11:24:26Zcom_10033_6815com_10033_6814col_10033_6886
Bolm, Maike
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Jansen, Wouter T. M.
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Schnabel, Ralf
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Chhatwal, Gursharan S.
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500
2007-02-20T14:32:48Z
2004-02
2007-02-20T14:32:48Z
2004-02
Infection and Immunity 2004 72(2):1192-1194
0019-9567
1098-5522
14742574
10.1128/IAI.72.2.1192-1194.2004
http://hdl.handle.net/10033/8659
321644
en_US
American Society for Microbiology
Copyright © 2004, American Society for Microbiology
Hydrogen Peroxide-Mediated Killing of Caenorhabditis elegans: a Common Feature of Different Streptococcal Species
YES
2018-06-12T17:48:04Z
ORIGINAL
Bolm et al_final.pdf
Bolm et al_final.pdf
free copy of text from PMC repository
application/pdf
154414
https://hzi.openrepository.com/bitstream/10033/8659/1/Bolm%20et%20al_final.pdf
cebcc279abb9f65505f5f6d079c011c2
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8659/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
22605
https://hzi.openrepository.com/bitstream/10033/8659/3/license_text
0d804ae578d831f4967f509ae1b0641e
MD5
3
false
license_rdf
license_rdf
application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8659/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Bolm et al_final.pdf.txt
Bolm et al_final.pdf.txt
Extracted Text
text/plain
13786
https://hzi.openrepository.com/bitstream/10033/8659/7/Bolm%20et%20al_final.pdf.txt
f5b353fac3dda66043d441cbcbaf2585
MD5
7
false
THUMBNAIL
Bolm et al_final.pdf.jpg
Bolm et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
34857
https://hzi.openrepository.com/bitstream/10033/8659/8/Bolm%20et%20al_final.pdf.jpg
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MD5
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10033/8659
oai:hzi.openrepository.com:10033/8659
2019-08-30 11:24:26.106
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86632019-08-30T11:24:26Zcom_10033_6815com_10033_6814col_10033_6886
Bergmann, Simone
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Rohde, Manfred
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500
Hammerschmidt, Sven
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500
2007-02-20T14:35:49Z
2004-04
2007-02-20T14:35:49Z
2004-04
Infection and Immunity 2004 72(4):2416-2419
0019-9567
1098-5522
15039372
10.1128/IAI.72.4.2416-2419.2004
http://hdl.handle.net/10033/8663
375162
en_US
American Society for Microbiology
Copyright © 2004, American Society for Microbiology
Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus pneumoniae Is a Surface-Displayed Plasminogen-Binding Protein
YES
2018-06-12T23:41:35Z
ORIGINAL
Bergmann et al_final.pdf
Bergmann et al_final.pdf
free text from PMC repository
application/pdf
433691
https://hzi.openrepository.com/bitstream/10033/8663/1/Bergmann%20et%20al_final.pdf
8ea73e12fc6053f804980872d7c09237
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8663/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
22605
https://hzi.openrepository.com/bitstream/10033/8663/3/license_text
0d804ae578d831f4967f509ae1b0641e
MD5
3
false
license_rdf
license_rdf
application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8663/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Bergmann et al_final.pdf.txt
Bergmann et al_final.pdf.txt
Extracted Text
text/plain
19631
https://hzi.openrepository.com/bitstream/10033/8663/7/Bergmann%20et%20al_final.pdf.txt
a540286fcb6167a13a507efef4c067b3
MD5
7
false
THUMBNAIL
Bergmann et al_final.pdf.jpg
Bergmann et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
35126
https://hzi.openrepository.com/bitstream/10033/8663/8/Bergmann%20et%20al_final.pdf.jpg
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MD5
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10033/8663
oai:hzi.openrepository.com:10033/8663
2019-08-30 11:24:26.262
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86642019-08-30T11:25:39Zcom_10033_6815com_10033_6814col_10033_6886
Goldmann, Oliver
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Rohde, Manfred
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Chhatwal, Gursharan Singh
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500
Medina, Eva
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600
http://orcid.org/0000-0001-9073-0223
2007-02-20T14:36:16Z
2004-05
2007-02-20T14:36:16Z
2004-05
Infection and Immunity 2004 72(5):2956-2963
0019-9567
1098-5522
15102808
10.1128/IAI.72.5.2956-2963.2004
http://hdl.handle.net/10033/8664
387899
en_US
American Society for Microbiology
Copyright © 2004, American Society for Microbiology
Role of Macrophages in Host Resistance to Group A Streptococci
YES
2018-06-13T01:23:58Z
ORIGINAL
Goldmann et al_final.pdf
Goldmann et al_final.pdf
free text from PMC repository
application/pdf
977582
https://hzi.openrepository.com/bitstream/10033/8664/1/Goldmann%20et%20al_final.pdf
e645228d1311cc6a8a1c8623a6fcc06e
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8664/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
22605
https://hzi.openrepository.com/bitstream/10033/8664/3/license_text
0d804ae578d831f4967f509ae1b0641e
MD5
3
false
license_rdf
license_rdf
application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8664/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Goldmann et al_final.pdf.txt
Goldmann et al_final.pdf.txt
Extracted Text
text/plain
42571
https://hzi.openrepository.com/bitstream/10033/8664/7/Goldmann%20et%20al_final.pdf.txt
36c86586c64b1ab3b64d77af0430bbc2
MD5
7
false
THUMBNAIL
Goldmann et al_final.pdf.jpg
Goldmann et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
32287
https://hzi.openrepository.com/bitstream/10033/8664/8/Goldmann%20et%20al_final.pdf.jpg
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MD5
8
false
10033/8664
oai:hzi.openrepository.com:10033/8664
2019-08-30 11:25:39.972
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86822019-08-30T11:33:26Zcom_10033_6815com_10033_6814col_10033_6886
McArthur, J.
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500
Medina, Eva
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600
http://orcid.org/0000-0001-9073-0223
Mueller, A.
5da74d3fef760ac28354bed19d1de6e1
500
Chin, J.
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500
Currie, B. J.
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500
Sriprakash, K. S.
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500
Talay, S. R.
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Chhatwal, G. S.
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500
Walker, M. J.
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500
2007-02-21T08:17:55Z
2004-12
2007-02-21T08:17:55Z
2004-12
Infection and Immunity 2004 72(12):7342-7345
0019-9567
1098-5522
15557665
10.1128/IAI.72.12.7342-7345.2004
http://hdl.handle.net/10033/8682
529117
en_US
American Society for Microbiology
Copyright © 2004, American Society for Microbiology
Intranasal Vaccination with Streptococcal Fibronectin Binding Protein Sfb1 Fails To Prevent Growth and Dissemination of Streptococcus pyogenes in a Murine Skin Infection Model
YES
2018-06-13T07:26:49Z
ORIGINAL
McArthur et al_final.pdf
McArthur et al_final.pdf
free text from PMC repository
application/pdf
238440
https://hzi.openrepository.com/bitstream/10033/8682/1/McArthur%20et%20al_final.pdf
65e2a04402e8335be4b70c41db329362
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8682/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
22605
https://hzi.openrepository.com/bitstream/10033/8682/3/license_text
0d804ae578d831f4967f509ae1b0641e
MD5
3
false
license_rdf
license_rdf
application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8682/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
McArthur et al_final.pdf.txt
McArthur et al_final.pdf.txt
Extracted Text
text/plain
24187
https://hzi.openrepository.com/bitstream/10033/8682/7/McArthur%20et%20al_final.pdf.txt
c6cd485289441f620f7a1b8690b5d2c4
MD5
7
false
THUMBNAIL
McArthur et al_final.pdf.jpg
McArthur et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
40685
https://hzi.openrepository.com/bitstream/10033/8682/8/McArthur%20et%20al_final.pdf.jpg
f6eaa6fa6e1e86a190e7a84373c583f5
MD5
8
false
10033/8682
oai:hzi.openrepository.com:10033/8682
2019-08-30 11:33:26.733
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/87002019-08-30T11:25:07Zcom_10033_6815com_10033_6814col_10033_6886
Pracht, Daniela
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500
Elm, Christine
3c559e634fcfda25756e255dac760439
500
Gerber, Joachim
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500
Bergmann, Simone
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500
Rohde, Manfred
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500
Seiler, Marleen
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500
Kim, Kwang S.
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500
Jenkinson, Howard F.
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500
Nau, Roland
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500
Hammerschmidt, Sven
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500
2007-02-21T08:39:54Z
2005-05
2007-02-21T08:39:54Z
2005-05
Infection and Immunity 2005 73(5):2680-2689
0019-9567
1098-5522
15845469
10.1128/IAI.73.5.2680-2689.2005
http://hdl.handle.net/10033/8700
1087317
en_US
American Society for Microbiology
Copyright © 2005, American Society for Microbiology
PavA of Streptococcus pneumoniae Modulates Adherence, Invasion, and Meningeal Inflammation
YES
2018-06-12T21:36:40Z
ORIGINAL
Pracht et al_final.pdf
Pracht et al_final.pdf
free copy from PMC repository
application/pdf
690336
https://hzi.openrepository.com/bitstream/10033/8700/1/Pracht%20et%20al_final.pdf
6de4ed0b99293ef2425cfb6feca2f8ed
MD5
1
true
CC-LICENSE
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/8700/2/license_url
924993ce0b3ba389f79f32a1b2735415
MD5
2
false
license_text
license_text
application/octet-stream
22605
https://hzi.openrepository.com/bitstream/10033/8700/3/license_text
0d804ae578d831f4967f509ae1b0641e
MD5
3
false
license_rdf
license_rdf
application/octet-stream
23748
https://hzi.openrepository.com/bitstream/10033/8700/4/license_rdf
b92763cfc0af52c7c868455edfaf3266
MD5
4
false
TEXT
Pracht et al_final.pdf.txt
Pracht et al_final.pdf.txt
Extracted Text
text/plain
58053
https://hzi.openrepository.com/bitstream/10033/8700/7/Pracht%20et%20al_final.pdf.txt
e36ae2cc82ed60fb9676ee386b679a9e
MD5
7
false
THUMBNAIL
Pracht et al_final.pdf.jpg
Pracht et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
36444
https://hzi.openrepository.com/bitstream/10033/8700/8/Pracht%20et%20al_final.pdf.jpg
25f6424c13750300376a4e1fad950094
MD5
8
false
10033/8700
oai:hzi.openrepository.com:10033/8700
2019-08-30 11:25:07.604
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/87472019-08-30T11:25:09Zcom_10033_6815com_10033_6814col_10033_6886
Machata, Silke
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500
Hain, Torsten
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500
Rohde, Manfred
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500
Chakraborty, Trinad
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500
2007-02-22T14:44:54Z
2005-12
2007-02-22T14:44:54Z
2005-12
Journal of Bacteriology 2005 187(24):8385-8394
0021-9193
1098-5530
16321943
10.1128/JB.187.24.8385-8394.2005
http://hdl.handle.net/10033/8747
1317001
en_US
American Society for Microbiology
Copyright © 2005, American Society for Microbiology
Simultaneous Deficiency of both MurA and p60 Proteins Generates a Rough Phenotype in Listeria monocytogenes
YES
2018-06-12T23:51:08Z
ORIGINAL
machata et al_final.pdf
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10033/8747
oai:hzi.openrepository.com:10033/8747
2019-08-30 11:25:09.13
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/123512019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Sugareva, Venelina
28f2aef006612ba18b1c18f7068d55b0
500
Härtl, Albert
0427230fedf55360864bc5514ec8955f
500
Brock, Matthias
30293dd7916d322c186e76483411dba7
500
Hübner, Katrin
4a4baa812bfb1a523f33025c9f76f2f8
500
Rohde, Manfred
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Heinekamp, Thorsten
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500
Brakhage, Axel A
54db12014a28ce5adc1f747d47eee56e
500
2007-06-19T07:43:43Z
2007-06-19T07:43:43Z
2006-11-01
Arch. Microbiol. 2006, 186(5):345-55
0302-8933
16988817
10.1007/s00203-006-0144-2
http://hdl.handle.net/10033/12351
Aspergillus fumigatus is an important pathogen of the immunocompromised host. Previously, it was shown that the polyketide synthase encoded by the pksP (alb1) gene represents a virulence determinant. pksP is part of a gene cluster involved in dihydroxynaphthalene (DHN)-like melanin biosynthesis. Because a putative laccase-encoding gene (abr2) is also part of the cluster and a laccase was found to represent a virulence factor in Cryptococcus neoformans, here, the Abr2 laccase was characterised. Deletion of the abr2 gene changed the gray-green conidial pigment to a brown color and the ornamentation of conidia was reduced compared with wild-type conidia. In contrast to the white pksP mutant, the susceptibility of the Deltaabr2 mutant against reactive oxygen species (ROS) was not increased, suggesting that the intermediate of DHN-like melanin produced up to the step catalysed by Abr2 already possesses ROS scavenging activity. In an intranasal mouse infection model, the Deltaabr2 mutant strain showed no reduction in virulence compared with the wild type. In the Deltaabr2 mutant, overall laccase activity was reduced only during sporulation, but not during vegetative growth. An abr2p-lacZ gene fusion was expressed during sporulation, but not during vegetative growth confirming the pattern of laccase activity due to Abr2.
592160 bytes
application/pdf
YES
en
Characterisation of the laccase-encoding gene abr2 of the dihydroxynaphthalene-like melanin gene cluster of Aspergillus fumigatus.
Article
2018-06-13T00:14:55Z
Aspergillus fumigatus is an important pathogen of the immunocompromised host. Previously, it was shown that the polyketide synthase encoded by the pksP (alb1) gene represents a virulence determinant. pksP is part of a gene cluster involved in dihydroxynaphthalene (DHN)-like melanin biosynthesis. Because a putative laccase-encoding gene (abr2) is also part of the cluster and a laccase was found to represent a virulence factor in Cryptococcus neoformans, here, the Abr2 laccase was characterised. Deletion of the abr2 gene changed the gray-green conidial pigment to a brown color and the ornamentation of conidia was reduced compared with wild-type conidia. In contrast to the white pksP mutant, the susceptibility of the Deltaabr2 mutant against reactive oxygen species (ROS) was not increased, suggesting that the intermediate of DHN-like melanin produced up to the step catalysed by Abr2 already possesses ROS scavenging activity. In an intranasal mouse infection model, the Deltaabr2 mutant strain showed no reduction in virulence compared with the wild type. In the Deltaabr2 mutant, overall laccase activity was reduced only during sporulation, but not during vegetative growth. An abr2p-lacZ gene fusion was expressed during sporulation, but not during vegetative growth confirming the pattern of laccase activity due to Abr2.
ORIGINAL
Sugareva_final.pdf
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main document
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LICENSE
license.txt
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text/plain
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5
false
TEXT
Sugareva_final.pdf.txt
Sugareva_final.pdf.txt
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10033/12351
oai:hzi.openrepository.com:10033/12351
2019-08-30 11:37:00.131
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/145502019-08-30T11:35:14Zcom_10033_6815com_10033_6814col_10033_6886
Burnett, Tracey A
b66efdb26c744b50d4a4eccca5bb8469
500
Dinkla, Katrin
81f17e1395e1a97fa5ca8ea2b6a3cdd4
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Uphoff, Cord
738414ffe94b25d2ff9ab2b30926d1a1
500
Srivastava, Mukesh
ff11438e77e38e1abe0e37a6d157e1a5
500
Cordwell, Stuart J
ef8f7856478a5bc16b514668f8825272
500
Geary, Steven
5fa783ad1d2b0fe513f1c2ac895c931e
500
Liao, Xiaofen
e9ef7f537605d034e4e9695932564df0
500
Minion, F Chris
948815b0169dc60ca1feeb28113d1884
500
Walker, Mark J
f0cadb1546aa7739cd666f11abfead8e
500
Djordjevic, Steven P
92b6e55574571a624e374ff8e9a361f3
500
2007-11-13T12:35:13Z
2007-11-13T12:35:13Z
2006-05-01
Mol. Microbiol. 2006, 60(3):669-86
0950-382X
16629669
10.1111/j.1365-2958.2006.05139.x
http://hdl.handle.net/10033/14550
Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparin-binding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages. Following purification of four recombinant proteins spanning P159 (F1P159, F2P159, F3P159 and F4P159), only F3P159 and F4P159 bound heparin in a dose-dependent manner (K(d) values 142.37 +/- 22.01 nM; 75.37 +/- 7.34 nM respectively). Scanning electron microscopic studies showed M. hyopneumoniae bound intimately to porcine kidney epithelial-like cells (PK15 cells) but these processes were inhibited by excess heparin and F4P159. Similarly, latex beads coated with F2P159 and F4P159 adhered to and entered PK15 cells, but heparin, F2P159 and F4P159 was inhibitory. These findings indicate that P159 is a post-translationally cleaved, glycosaminoglycan-binding adhesin of M. hyopneumoniae.
3565814 bytes
application/pdf
YES
en
P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells.
Article
2018-06-12T17:34:17Z
Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparin-binding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages. Following purification of four recombinant proteins spanning P159 (F1P159, F2P159, F3P159 and F4P159), only F3P159 and F4P159 bound heparin in a dose-dependent manner (K(d) values 142.37 +/- 22.01 nM; 75.37 +/- 7.34 nM respectively). Scanning electron microscopic studies showed M. hyopneumoniae bound intimately to porcine kidney epithelial-like cells (PK15 cells) but these processes were inhibited by excess heparin and F4P159. Similarly, latex beads coated with F2P159 and F4P159 adhered to and entered PK15 cells, but heparin, F2P159 and F4P159 was inhibitory. These findings indicate that P159 is a post-translationally cleaved, glycosaminoglycan-binding adhesin of M. hyopneumoniae.
ORIGINAL
Burnettfinal.pdf
Burnettfinal.pdf
original document
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true
LICENSE
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MD5
2
false
TEXT
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Burnettfinal.pdf.txt
Extracted Text
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10033/14550
oai:hzi.openrepository.com:10033/14550
2019-08-30 11:35:14.045
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/147322019-08-30T11:24:31Zcom_10033_6815com_10033_6814col_10033_6886
Nitsche, D Patric
d92d11ca383e7cc23c2c92a382da967a
500
Johansson, Helena M
d4b62131f82bfbd4e6161c92a35718c3
500
Frick, Inga-Maria
3b364729dd1a1682aaaa27652b08de47
500
Mörgelin, Matthias
3b24bbdfdbc2401bc3afa6678a7b152e
500
2007-11-26T10:18:16Z
2007-11-26T10:18:16Z
2006-01-20
J. Biol. Chem. 2006, 281(3):1670-9
0021-9258
16278217
10.1074/jbc.M506776200
http://hdl.handle.net/10033/14732
Group G streptococcus (GGS) is a human pathogen of emerging clinical significance. It causes skin and soft tissue infections, occasionally resulting in life-threatening conditions such as sepsis and necrotizing fasciitis. We recently identified FOG, a novel surface protein of GGS with fibrinogen binding and immune evasion properties. Here we investigated the role of FOG in streptococcal primary adhesion to host tissue. A FOG-expressing clinical isolate adhered more efficiently to human skin biopsies ex vivo and to the murine dermis in vivo than a FOG-deficient strain. Scanning and transmission electron microscopy of skin specimens exhibited that this property was assigned to the ability of FOG to interact with collagen I, a major interstitial component of the dermis. Overlay experiments with human skin extracts and radiolabeled FOG followed by matrix-assisted laser desorption/ionization time of flight mass spectrometry analysis identified both the alpha1- and alpha2-chains of collagen I as targets for FOG. Transmission electron microscopy of the molecular complexes revealed thread-like FOG molecules binding via their NH2 termini to distinct sites on collagen I monomers and fibrils. The results demonstrate that FOG is important for GGS adhesion in vivo, implying a pathogenic role for this surface protein.
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Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo.
Article
2018-06-13T07:37:16Z
Group G streptococcus (GGS) is a human pathogen of emerging clinical significance. It causes skin and soft tissue infections, occasionally resulting in life-threatening conditions such as sepsis and necrotizing fasciitis. We recently identified FOG, a novel surface protein of GGS with fibrinogen binding and immune evasion properties. Here we investigated the role of FOG in streptococcal primary adhesion to host tissue. A FOG-expressing clinical isolate adhered more efficiently to human skin biopsies ex vivo and to the murine dermis in vivo than a FOG-deficient strain. Scanning and transmission electron microscopy of skin specimens exhibited that this property was assigned to the ability of FOG to interact with collagen I, a major interstitial component of the dermis. Overlay experiments with human skin extracts and radiolabeled FOG followed by matrix-assisted laser desorption/ionization time of flight mass spectrometry analysis identified both the alpha1- and alpha2-chains of collagen I as targets for FOG. Transmission electron microscopy of the molecular complexes revealed thread-like FOG molecules binding via their NH2 termini to distinct sites on collagen I monomers and fibrils. The results demonstrate that FOG is important for GGS adhesion in vivo, implying a pathogenic role for this surface protein.
ORIGINAL
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oai:repository.helmholtz-hzi.de:10033/194322019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Mayer, H
59872ef1bcac558a9fb325c6ce288673
500
Department of Microbial Pathogenesis, Helmholtz Center for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany. manfred.rohde@helmholtz-hzi.de
2008-02-29T12:42:20Z
2008-02-29T12:42:20Z
2007-05
Exocytotic process as a novel model for mineralization by osteoblasts in vitro and in vivo determined by electron microscopic analysis. 2007, 80 (5):323-36 Calcif. Tissue Int.
0171-967X
17406769
10.1007/s00223-007-9013-5
http://hdl.handle.net/10033/19432
Calcified tissue international
The process of biomineralization has been examined during osteoblastic differentiation of bone marrow stroma cells (BMSCs) from embryonic chick in culture and in periosteum itself by a number of different techniques including transmission and scanning electron microscopy. In cell culture of BMSCs at days 20-25, crystals were accumulated extracellularly in the collagen matrix, resulting in large plate-like crystallites and noncollagen associated on the culture disk surface. In contrast, up to days 10-18, mainly intracellular mineralization was visible by numerous needle-like crystal structures in the cell cytoplasm and in vacuoles. After 20-30 days, the crystal content of these vacuoles is released, most probably by membrane fusion to the outside of the cells. Energy-dispersive X-ray analysis (EDX), electron spectroscopic imaging, and electron energy loss spectroscopy demonstrated that Ca, O, and P are located in the intra- and extracellular needle-like crystals. From EDX spectra a Ca/P ratio of 1.3 was estimated for the intracellular structures and a Ca/P ratio of 1.5, for the extracellular material (for comparison, the Ca/P ratio in tibiae is 1.6). X-ray diffraction and quantitative infrared spectral analyses also demonstrated an increase of crystalline bone apatite along the mineralization process. In addition to the finding in vitro, the presence of intracellular needle-like crystals in vacuoles could be demonstrated in vivo in osteoblastic cells of the periosteum in tibia of day 11. The results are in favor of a novel model for mineralization by osteoblasts, in which amorphous Ca/P material is directly secreted via an exocytotic process from vacuoles of the osteoblast, deposited extracellularly, propagated into the collagen fibril matrix, and matured to hydroxyapatite.
en
Animals
Calcification, Physiologic
Cell Differentiation
Cells, Cultured
Chick Embryo
Collagen
Durapatite
Exocytosis
Microscopy, Electron, Scanning
Microscopy, Electron, Transmission
Models, Biological
Osteoblasts
Stromal Cells
Exocytotic process as a novel model for mineralization by osteoblasts in vitro and in vivo determined by electron microscopic analysis.
Article
2018-06-13T09:23:09Z
The process of biomineralization has been examined during osteoblastic differentiation of bone marrow stroma cells (BMSCs) from embryonic chick in culture and in periosteum itself by a number of different techniques including transmission and scanning electron microscopy. In cell culture of BMSCs at days 20-25, crystals were accumulated extracellularly in the collagen matrix, resulting in large plate-like crystallites and noncollagen associated on the culture disk surface. In contrast, up to days 10-18, mainly intracellular mineralization was visible by numerous needle-like crystal structures in the cell cytoplasm and in vacuoles. After 20-30 days, the crystal content of these vacuoles is released, most probably by membrane fusion to the outside of the cells. Energy-dispersive X-ray analysis (EDX), electron spectroscopic imaging, and electron energy loss spectroscopy demonstrated that Ca, O, and P are located in the intra- and extracellular needle-like crystals. From EDX spectra a Ca/P ratio of 1.3 was estimated for the intracellular structures and a Ca/P ratio of 1.5, for the extracellular material (for comparison, the Ca/P ratio in tibiae is 1.6). X-ray diffraction and quantitative infrared spectral analyses also demonstrated an increase of crystalline bone apatite along the mineralization process. In addition to the finding in vitro, the presence of intracellular needle-like crystals in vacuoles could be demonstrated in vivo in osteoblastic cells of the periosteum in tibia of day 11. The results are in favor of a novel model for mineralization by osteoblasts, in which amorphous Ca/P material is directly secreted via an exocytotic process from vacuoles of the osteoblast, deposited extracellularly, propagated into the collagen fibril matrix, and matured to hydroxyapatite.
ORIGINAL
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2019-08-30 11:37:23.774
Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/195532019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
McMillan, David J
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Sriprakash, Kadaba S
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Chhatwal, Gursharan S
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Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
2008-03-03T14:20:49Z
2008-03-03T14:20:49Z
2007-11
Genetic variation in group A streptococci. 2007, 297 (7-8):525-32 Int. J. Med. Microbiol.
1438-4221
17459766
10.1016/j.ijmm.2007.02.007
http://hdl.handle.net/10033/19553
International journal of medical microbiology : IJMM
Group A streptococcus (GAS) is responsible for a range of human diseases that vary in their clinical manifestations and severity. While numerous virulence factors have been described, the way these factors interact to promote different streptococcal diseases is less clear. In order to identify multifactorial relationships between GAS and the human host, novel high-throughput techniques such as microarrays are necessary. We have performed comparative studies using custom-designed virulence arrays to enhance our understanding of the high degree of genotypic variation that occurs in streptococci. This study has pointed to mobile genetic elements as the major agents that promote variation. Our results show that multiple combinations of genes might bring about similar clinical pictures. This adds further complexity to the intricate relationship between pathogen and host.
en
Genotype
Humans
Streptococcal Infections
Streptococcus
Streptococcus pyogenes
Variation (Genetics)
Genetic variation in group A streptococci.
Article
2018-06-12T19:58:35Z
Group A streptococcus (GAS) is responsible for a range of human diseases that vary in their clinical manifestations and severity. While numerous virulence factors have been described, the way these factors interact to promote different streptococcal diseases is less clear. In order to identify multifactorial relationships between GAS and the human host, novel high-throughput techniques such as microarrays are necessary. We have performed comparative studies using custom-designed virulence arrays to enhance our understanding of the high degree of genotypic variation that occurs in streptococci. This study has pointed to mobile genetic elements as the major agents that promote variation. Our results show that multiple combinations of genes might bring about similar clinical pictures. This adds further complexity to the intricate relationship between pathogen and host.
ORIGINAL
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McMillan et al_final.pdf
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Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/196132019-08-30T11:37:24Zcom_10033_6815com_10033_6814col_10033_6886
Lee, Yong-Jin
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500
Prange, Alexander
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500
Lichtenberg, Henning
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Rohde, Manfred
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Dashti, Mona
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Wiegel, Juergen
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Department of Microbiology, The University of Georgia, Athens, GA 30602-2605, USA.
2008-03-04T10:26:33Z
2008-03-04T10:26:33Z
2007-10
In situ analysis of sulfur species in sulfur globules produced from thiosulfate by Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes. 2007, 189 (20):7525-9 J. Bacteriol.
0021-9193
17644590
10.1128/JB.00782-07
http://hdl.handle.net/10033/19613
Journal of bacteriology
The Firmicutes Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes convert thiosulfate, forming sulfur globules inside and outside cells. X-ray absorption near-edge structure analysis revealed that the sulfur consisted mainly of sulfur chains with organic end groups similar to sulfur formed in purple sulfur bacteria, suggesting the possibility that the process of sulfur globule formation by bacteria is an ancient feature.
en
Organic Chemicals
Spectrum Analysis
Sulfur Compounds
Thermoanaerobacter
Thermoanaerobacterium
Thiosulfates
In situ analysis of sulfur species in sulfur globules produced from thiosulfate by Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes.
Article
2018-06-12T22:48:35Z
The Firmicutes Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes convert thiosulfate, forming sulfur globules inside and outside cells. X-ray absorption near-edge structure analysis revealed that the sulfur consisted mainly of sulfur chains with organic end groups similar to sulfur formed in purple sulfur bacteria, suggesting the possibility that the process of sulfur globule formation by bacteria is an ancient feature.
ORIGINAL
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Helmholtz Zentrum für Infektionsforschung Repository
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Reissmann, Silvana
d3f934cc3ed8b9c1f2a39fa845189980
500
Johansson, Helena M
d4b62131f82bfbd4e6161c92a35718c3
500
Frick, Inga-Maria
3b364729dd1a1682aaaa27652b08de47
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
2008-03-04T13:25:29Z
2008-03-04T13:25:29Z
2007-06-29
Identification of a streptococcal octapeptide motif involved in acute rheumatic fever. 2007, 282 (26):18686-93 J. Biol. Chem.
0021-9258
17452321
10.1074/jbc.M701047200
http://hdl.handle.net/10033/19652
The Journal of biological chemistry
Acute rheumatic fever is a serious autoimmune sequela of pharyngitis caused by certain group A streptococci. One mechanism applied by streptococcal strains capable of causing acute rheumatic fever is formation of an autoantigenic complex with human collagen IV. In some geographic regions with a high incidence of acute rheumatic fever pharyngeal carriage of group C and group G streptococci prevails. Examination of such strains revealed the presence of M-like surface proteins that bind human collagen. Using a peptide array and recombinant proteins with targeted amino acid substitutions, we could demonstrate that formation of collagen complexes during streptococcal infections depends on an octapeptide motif, which is present in collagen binding M and M-like proteins of different beta-hemolytic streptococcal species. Mice immunized with streptococcal proteins that contain the collagen binding octapeptide motif developed high serum titers of anti-collagen antibodies. In sera of rheumatic fever patients such a collagen autoimmune response was accompanied by specific reactivity against the collagen-binding proteins, linking the observed effect to clinical cases. Taken together, the data demonstrate that the identified octapeptide motif through its action on collagen plays a crucial role in the pathogenesis of rheumatic fever. Eradication of streptococci that express proteins with the collagen binding motif appears advisable for controlling rheumatic fever.
en
Acute Disease
Amino Acid Sequence
Animals
Antibodies, Bacterial
Autoantibodies
Autoimmunity
Bacterial Proteins
Biological Markers
Collagen Type IV
Female
Humans
Mice
Mice, Inbred C3H
Microscopy, Electron, Scanning
Molecular Sequence Data
Peptide Fragments
Rheumatic Fever
Specific Pathogen-Free Organisms
Streptococcus
Surface Plasmon Resonance
Virulence
Identification of a streptococcal octapeptide motif involved in acute rheumatic fever.
Article
2018-06-13T03:44:59Z
Acute rheumatic fever is a serious autoimmune sequela of pharyngitis caused by certain group A streptococci. One mechanism applied by streptococcal strains capable of causing acute rheumatic fever is formation of an autoantigenic complex with human collagen IV. In some geographic regions with a high incidence of acute rheumatic fever pharyngeal carriage of group C and group G streptococci prevails. Examination of such strains revealed the presence of M-like surface proteins that bind human collagen. Using a peptide array and recombinant proteins with targeted amino acid substitutions, we could demonstrate that formation of collagen complexes during streptococcal infections depends on an octapeptide motif, which is present in collagen binding M and M-like proteins of different beta-hemolytic streptococcal species. Mice immunized with streptococcal proteins that contain the collagen binding octapeptide motif developed high serum titers of anti-collagen antibodies. In sera of rheumatic fever patients such a collagen autoimmune response was accompanied by specific reactivity against the collagen-binding proteins, linking the observed effect to clinical cases. Taken together, the data demonstrate that the identified octapeptide motif through its action on collagen plays a crucial role in the pathogenesis of rheumatic fever. Eradication of streptococci that express proteins with the collagen binding motif appears advisable for controlling rheumatic fever.
ORIGINAL
Dinkla et al_final.pdf
Dinkla et al_final.pdf
original manuscript
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2019-08-30 11:37:24.147
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/198332019-08-30T11:37:44Zcom_10033_6815com_10033_6814col_10033_6886
Walker, Mark J
f0cadb1546aa7739cd666f11abfead8e
500
Hollands, Andrew
fdb996bb26364f8e30146b25faff5ec1
500
Sanderson-Smith, Martina L
f988705f4e446c263f31eed6480bf32c
500
Cole, Jason N
0da4cff8dda2ba931b3f39a4af5f0030
500
Kirk, Joshua K
70831685dabd87531b0ced2e6472353e
500
Henningham, Anna
7a1597386a7b2ec248a34460db772026
500
McArthur, Jason D
2356302df6069f0a4451bf1419f10c43
500
Dinkla, Katrin
81f17e1395e1a97fa5ca8ea2b6a3cdd4
500
Aziz, Ramy K
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500
Kansal, Rita G
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500
Simpson, Amelia J
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500
Buchanan, John T
60a253ddf52fb418071181f60fdb53c2
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Kotb, Malak
b98c2bffdad9986e0b15a8d75edbb276
500
Nizet, Victor
dbd1742a4694623263b14b9c4abdbb1f
500
School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.
2008-03-05T13:49:43Z
2008-03-05T13:49:43Z
2007-08
DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection. 2007, 13 (8):981-5 Nat. Med.
1078-8956
17632528
10.1038/nm1612
http://hdl.handle.net/10033/19833
Nature medicine
Most invasive bacterial infections are caused by species that more commonly colonize the human host with minimal symptoms. Although phenotypic or genetic correlates underlying a bacterium's shift to enhanced virulence have been studied, the in vivo selection pressures governing such shifts are poorly understood. The globally disseminated M1T1 clone of group A Streptococcus (GAS) is linked with the rare but life-threatening syndromes of necrotizing fasciitis and toxic shock syndrome. Mutations in the GAS control of virulence regulatory sensor kinase (covRS) operon are associated with severe invasive disease, abolishing expression of a broad-spectrum cysteine protease (SpeB) and allowing the recruitment and activation of host plasminogen on the bacterial surface. Here we describe how bacteriophage-encoded GAS DNase (Sda1), which facilitates the pathogen's escape from neutrophil extracellular traps, serves as a selective force for covRS mutation. The results provide a paradigm whereby natural selection exerted by the innate immune system generates hypervirulent bacterial variants with increased risk of systemic dissemination.
en
Animals
Cell Survival
Deoxyribonuclease I
Humans
Immunity, Natural
Mice
Neutrophils
Phenotype
Selection (Genetics)
Streptococcal Infections
Streptococcus pyogenes
Virulence
DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection.
Article
2018-06-13T16:59:32Z
Most invasive bacterial infections are caused by species that more commonly colonize the human host with minimal symptoms. Although phenotypic or genetic correlates underlying a bacterium's shift to enhanced virulence have been studied, the in vivo selection pressures governing such shifts are poorly understood. The globally disseminated M1T1 clone of group A Streptococcus (GAS) is linked with the rare but life-threatening syndromes of necrotizing fasciitis and toxic shock syndrome. Mutations in the GAS control of virulence regulatory sensor kinase (covRS) operon are associated with severe invasive disease, abolishing expression of a broad-spectrum cysteine protease (SpeB) and allowing the recruitment and activation of host plasminogen on the bacterial surface. Here we describe how bacteriophage-encoded GAS DNase (Sda1), which facilitates the pathogen's escape from neutrophil extracellular traps, serves as a selective force for covRS mutation. The results provide a paradigm whereby natural selection exerted by the innate immune system generates hypervirulent bacterial variants with increased risk of systemic dissemination.
ORIGINAL
Walker et al_final.pdf
Walker et al_final.pdf
original manuscript
application/pdf
495226
https://hzi.openrepository.com/bitstream/10033/19833/1/Walker%20et%20al_final.pdf
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oai:hzi.openrepository.com:10033/19833
2019-08-30 11:37:44.762
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/243522019-08-30T11:26:42Zcom_10033_6815com_10033_6814col_10033_6886
Nitsche-Schmitz, D Patric
cb8c9f97bad4b6ed57d10ef22331a3f4
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Helmholtz Centre for Infection Research, Microbial Pathogenesis, Braunschweig, Germany.
2008-04-29T08:59:29Z
2008-04-29T08:59:29Z
2007-09
Invasion mechanisms of Gram-positive pathogenic cocci. 2007, 98 (3):488-96 Thromb. Haemost.
0340-6245
17849036
http://hdl.handle.net/10033/24352
Thrombosis and haemostasis
Gram-positive cocci are important human pathogens. Streptococci and staphylococci in particular are a major threat to human health, since they cause a variety of serious invasive infections. Their invasion into normally sterile sites of the host depends on elaborated bacterial mechanisms that involve adhesion to the host tissue, its degradation, internalisation by host cells, and passage through epithelia and endothelia. Interactions of bacterial surface proteins with proteins of the host's extracellular matrix as well as with cell surface receptors are crucial factors in these processes, and some of the key mechanisms are similar in many pathogenic Gram-positive cocci. Therapies that interfere with these mechanisms may become efficient alternatives to today's antibiotic treatments.
en
Adhesins, Bacterial
Animals
Anti-Bacterial Agents
Antigens, Bacterial
Bacterial Adhesion
Bacterial Outer Membrane Proteins
Bacterial Proteins
Bacterial Translocation
Carrier Proteins
Caveolae
Endocytosis
Extracellular Matrix Proteins
Humans
Hydrolases
Phagocytes
Phagocytosis
Staphylococcal Infections
Staphylococcus
Streptococcal Infections
Streptococcus
Invasion mechanisms of Gram-positive pathogenic cocci.
Article
2018-06-13T00:24:56Z
Gram-positive cocci are important human pathogens. Streptococci and staphylococci in particular are a major threat to human health, since they cause a variety of serious invasive infections. Their invasion into normally sterile sites of the host depends on elaborated bacterial mechanisms that involve adhesion to the host tissue, its degradation, internalisation by host cells, and passage through epithelia and endothelia. Interactions of bacterial surface proteins with proteins of the host's extracellular matrix as well as with cell surface receptors are crucial factors in these processes, and some of the key mechanisms are similar in many pathogenic Gram-positive cocci. Therapies that interfere with these mechanisms may become efficient alternatives to today's antibiotic treatments.
ORIGINAL
Nitsche-Schimtz_final.pdf
Nitsche-Schimtz_final.pdf
original manuscript
application/pdf
1063556
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oai:repository.helmholtz-hzi.de:10033/246522019-08-30T11:34:48Zcom_10033_6815com_10033_6814col_10033_6886
Friedrichs, C
843ac8efccea8b9c66c5263a784c960a
500
Rodloff, A C
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500
Chhatwal, G S
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Schellenberger, W
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Eschrich, K
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Institute for Medical Microbiology and Epidemiology of Infectious Diseases, University of Leipzig, Liebigstr. 24, D-04105 Leipzig, Germany. claudia.friedrichs@medizin.uni-leipzig.de
2008-05-02T08:26:18Z
2008-05-02T08:26:18Z
2007-08
Rapid identification of viridans streptococci by mass spectrometric discrimination. 2007, 45 (8):2392-7 J. Clin. Microbiol.
0095-1137
17553974
10.1128/JCM.00556-07
http://hdl.handle.net/10033/24652
Journal of clinical microbiology
Viridans streptococci (VS) are responsible for several systemic diseases, such as endocarditis, abscesses, and septicemia. Unfortunately, species identification by conventional methods seems to be more difficult than species identification of other groups of bacteria. The aim of the present study was to evaluate the use of cell matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) for the rapid identification of 10 different species of VS. A total of 99 VS clinical isolates, 10 reference strains, and 20 strains from our in-house culture collection were analyzed by MALDI-TOF-MS. To evaluate the mass-spectrometric discrimination results, all strains were identified in parallel by phenotypic and genotypic methods. MALDI-TOF-MS identified 71 isolates as the mitis group, 23 as the anginosus group, and 5 as Streptococcus salivarius. Comparison of the species identification results obtained by the MALDI-TOF-MS analyses and with the phenotypic/genotypic identification systems showed 100% consistency at the species level. Thus, MALDI-TOF-MS seems to be a rapid and reliable method for the identification of species of VS from clinical samples.
en
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=17553974
Bacterial Typing Techniques
Humans
Polymerase Chain Reaction
Sensitivity and Specificity
Sequence Analysis, DNA
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Streptococcal Infections
Viridans Streptococci
Rapid identification of viridans streptococci by mass spectrometric discrimination.
article
2018-06-12T22:38:22Z
Viridans streptococci (VS) are responsible for several systemic diseases, such as endocarditis, abscesses, and septicemia. Unfortunately, species identification by conventional methods seems to be more difficult than species identification of other groups of bacteria. The aim of the present study was to evaluate the use of cell matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) for the rapid identification of 10 different species of VS. A total of 99 VS clinical isolates, 10 reference strains, and 20 strains from our in-house culture collection were analyzed by MALDI-TOF-MS. To evaluate the mass-spectrometric discrimination results, all strains were identified in parallel by phenotypic and genotypic methods. MALDI-TOF-MS identified 71 isolates as the mitis group, 23 as the anginosus group, and 5 as Streptococcus salivarius. Comparison of the species identification results obtained by the MALDI-TOF-MS analyses and with the phenotypic/genotypic identification systems showed 100% consistency at the species level. Thus, MALDI-TOF-MS seems to be a rapid and reliable method for the identification of species of VS from clinical samples.
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Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/290122019-08-30T11:27:16Zcom_10033_6815com_10033_6814col_10033_6886
Vary, Patricia S
8fd4511a1003ea8ef74d2297e3093274
500
Biedendieck, Rebekka
99f9888d56ae72e5e76f2181e6338d9b
500
Fuerch, Tobias
72d91c61e801c7620a7818f38931a5f3
500
Meinhardt, Friedhelm
766083529d4ff98039ab2f1be2dbe3b7
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Deckwer, Wolf-Dieter
81387c59fd4ed6919870311cf5e4984f
500
Jahn, Dieter
d201967c749f1274e18a5379802a90b2
500
Department of Biological Sciences, Northern Illinois University, DeKalb, IL 60115, USA.
2008-05-30T08:37:12Z
2008-05-30T08:37:12Z
2007-10
Bacillus megaterium--from simple soil bacterium to industrial protein production host. 2007, 76 (5):957-67 Appl. Microbiol. Biotechnol.
0175-7598
17657486
10.1007/s00253-007-1089-3
http://hdl.handle.net/10033/29012
Applied microbiology and biotechnology
Bacillus megaterium has been industrially employed for more than 50 years, as it possesses some very useful and unusual enzymes and a high capacity for the production of exoenzymes. It is also a desirable cloning host for the production of intact proteins, as it does not possess external alkaline proteases and can stably maintain a variety of plasmid vectors. Genetic tools for this species include transducing phages and several hundred mutants covering the processes of biosynthesis, catabolism, division, sporulation, germination, antibiotic resistance, and recombination. The seven plasmids of B. megaterium strain QM B1551 contain several unusual metabolic genes that may be useful in bioremediation. Recently, several recombinant shuttle vectors carrying different strong inducible promoters and various combinations of affinity tags for simple protein purification have been constructed. Leader sequences-mediated export of affinity-tagged proteins into the growth medium was made possible. These plasmids are commercially available. For a broader application of B. megaterium in industry, sporulation and protease-deficient as well as UV-sensitive mutants were constructed. The genome sequence of two different strains, plasmidless DSM319 and QM B1551 carrying seven natural plasmids, is now available. These sequences allow for a systems biotechnology optimization of the production host B. megaterium. Altogether, a "toolbox" of hundreds of genetically characterized strains, genetic methods, vectors, hosts, and genomic sequences make B. megaterium an ideal organism for industrial, environmental, and experimental applications.
en
Bacillus megaterium
Genetic Engineering
Industrial Microbiology
Plasmids
Recombinant Proteins
Soil Microbiology
Bacillus megaterium--from simple soil bacterium to industrial protein production host.
Article
2008-10-05T00:00:00Z
Bacillus megaterium has been industrially employed for more than 50 years, as it possesses some very useful and unusual enzymes and a high capacity for the production of exoenzymes. It is also a desirable cloning host for the production of intact proteins, as it does not possess external alkaline proteases and can stably maintain a variety of plasmid vectors. Genetic tools for this species include transducing phages and several hundred mutants covering the processes of biosynthesis, catabolism, division, sporulation, germination, antibiotic resistance, and recombination. The seven plasmids of B. megaterium strain QM B1551 contain several unusual metabolic genes that may be useful in bioremediation. Recently, several recombinant shuttle vectors carrying different strong inducible promoters and various combinations of affinity tags for simple protein purification have been constructed. Leader sequences-mediated export of affinity-tagged proteins into the growth medium was made possible. These plasmids are commercially available. For a broader application of B. megaterium in industry, sporulation and protease-deficient as well as UV-sensitive mutants were constructed. The genome sequence of two different strains, plasmidless DSM319 and QM B1551 carrying seven natural plasmids, is now available. These sequences allow for a systems biotechnology optimization of the production host B. megaterium. Altogether, a "toolbox" of hundreds of genetically characterized strains, genetic methods, vectors, hosts, and genomic sequences make B. megaterium an ideal organism for industrial, environmental, and experimental applications.
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oai:hzi.openrepository.com:10033/29012
2019-08-30 11:27:16.113
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/303972019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Heroven, Ann Kathrin
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500
Böhme, Katja
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Rohde, Manfred
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Dersch, Petra
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Institut für Mikrobiologie, Technische Universität Braunschweig, 38106 Braunschweig, Germany.
2008-06-24T13:53:53Z
2008-06-24T13:53:53Z
2008-06
A Csr-type regulatory system, including small non-coding RNAs, regulates the global virulence regulator RovA of Yersinia pseudotuberculosis through RovM. 2008, 68 (5):1179-95 Mol. Microbiol.
1365-2958
18430141
10.1111/j.1365-2958.2008.06218.x
http://hdl.handle.net/10033/30397
Molecular microbiology
The MarR-type regulator RovA controls expression of virulence genes of Yersinia pseudotuberculosis in response to environmental signals. Using a genetic strategy to discover components that influence rovA expression, we identified new regulatory factors with homology to components of the carbon storage regulator system (Csr). We showed that overexpression of a CsrB- or a CsrC-type RNA activates rovA, whereas a CsrA-like protein represses RovA synthesis. We further demonstrate that influence of the Csr system on rovA is indirect and occurs through control of the LysR regulator RovM, which inhibits rovA transcription. The CsrA protein had also a major influence on the motility of Yersinia, which was independent of RovM. The CsrB and CsrC RNAs are differentially expressed in Yersinia. CsrC is highly induced in complex but not in minimal media, indicating that medium-dependent rovM expression is mediated through CsrC. CsrB synthesis is generally very low. However, overexpression of the response regulator UvrY was found to activate CsrB production, which in turn represses CsrC synthesis independent of the growth medium. In summary, the post-transcriptional Csr-type components were shown to be key regulators in the co-ordinated environmental control of physiological processes and virulence factors, which are crucial for the initiation of Yersinia infections.
en
A Csr-type regulatory system, including small non-coding RNAs, regulates the global virulence regulator RovA of Yersinia pseudotuberculosis through RovM.
Article
2016-12-05T00:00:00Z
The MarR-type regulator RovA controls expression of virulence genes of Yersinia pseudotuberculosis in response to environmental signals. Using a genetic strategy to discover components that influence rovA expression, we identified new regulatory factors with homology to components of the carbon storage regulator system (Csr). We showed that overexpression of a CsrB- or a CsrC-type RNA activates rovA, whereas a CsrA-like protein represses RovA synthesis. We further demonstrate that influence of the Csr system on rovA is indirect and occurs through control of the LysR regulator RovM, which inhibits rovA transcription. The CsrA protein had also a major influence on the motility of Yersinia, which was independent of RovM. The CsrB and CsrC RNAs are differentially expressed in Yersinia. CsrC is highly induced in complex but not in minimal media, indicating that medium-dependent rovM expression is mediated through CsrC. CsrB synthesis is generally very low. However, overexpression of the response regulator UvrY was found to activate CsrB production, which in turn represses CsrC synthesis independent of the growth medium. In summary, the post-transcriptional Csr-type components were shown to be key regulators in the co-ordinated environmental control of physiological processes and virulence factors, which are crucial for the initiation of Yersinia infections.
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2019-08-30 11:25:11.271
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/472372019-08-30T11:32:16Zcom_10033_6815com_10033_6814col_10033_6886
Dinkla, K
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500
Cole, J N
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Cork, A J
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Maamary, P G
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McArthur, J D
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Chhatwal, G S
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Walker, M J
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School of Biological Sciences, University of Wollongong, Wollongong, NSW, 2522, Australia.
2009-01-09T13:41:47Z
2009-01-09T13:41:47Z
2008-08
M protein-mediated plasminogen binding is essential for the virulence of an invasive Streptococcus pyogenes isolate. 2008, 22 (8):2715-22 FASEB J.
1530-6860
18467595
10.1096/fj.07-105643
http://hdl.handle.net/10033/47237
The FASEB journal : official publication of the Federation of American Societies for Experimental Biology
The human protease plasmin plays a crucial role in the capacity of the group A streptococcus (GAS; Streptococcus pyogenes) to initiate invasive disease. The GAS strain NS88.2 was isolated from a case of bacteremia from the Northern Territory of Australia, a region with high rates of GAS invasive disease. Mutagenesis of the NS88.2 plasminogen binding M protein Prp was undertaken to examine the contribution of plasminogen binding and cell surface plasmin acquisition to virulence. The isogenic mutant NS88.2prp was engineered whereby four amino acid residues critical for plasminogen binding were converted to alanine codons in the GAS genome sequence. The mutated residues were reverse complemented to the wild-type sequence to construct GAS strain NS88.2prpRC. In comparison to NS88.2 and NS88.2prpRC, the NS88.2prp mutant exhibited significantly reduced ability to bind human plasminogen and accumulate cell surface plasmin activity during growth in human plasma. Utilizing a humanized plasminogen mouse model of invasive infection, we demonstrate that the capacity to bind plasminogen and accumulate surface plasmin activity plays an essential role in GAS virulence.
en
http://www.fasebj.org/cgi/reprint/22/8/2715
Animals
Antigens, Bacterial
Bacterial Outer Membrane Proteins
Base Sequence
Carrier Proteins
DNA Primers
DNA, Bacterial
Disease Models, Animal
Fibrinogen
Genes, Bacterial
Humans
Immunity, Innate
Mice
Mice, Inbred C57BL
Mice, Transgenic
Mutation
Phagocytosis
Plasminogen
Protein Binding
Recombinant Proteins
Streptococcal Infections
Streptococcus pyogenes
Virulence
M protein-mediated plasminogen binding is essential for the virulence of an invasive Streptococcus pyogenes isolate.
Article
2019-02-18T09:58:45Z
The human protease plasmin plays a crucial role in the capacity of the group A streptococcus (GAS; Streptococcus pyogenes) to initiate invasive disease. The GAS strain NS88.2 was isolated from a case of bacteremia from the Northern Territory of Australia, a region with high rates of GAS invasive disease. Mutagenesis of the NS88.2 plasminogen binding M protein Prp was undertaken to examine the contribution of plasminogen binding and cell surface plasmin acquisition to virulence. The isogenic mutant NS88.2prp was engineered whereby four amino acid residues critical for plasminogen binding were converted to alanine codons in the GAS genome sequence. The mutated residues were reverse complemented to the wild-type sequence to construct GAS strain NS88.2prpRC. In comparison to NS88.2 and NS88.2prpRC, the NS88.2prp mutant exhibited significantly reduced ability to bind human plasminogen and accumulate cell surface plasmin activity during growth in human plasma. Utilizing a humanized plasminogen mouse model of invasive infection, we demonstrate that the capacity to bind plasminogen and accumulate surface plasmin activity plays an essential role in GAS virulence.
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/485372019-08-30T11:32:17Zcom_10033_6815com_10033_6814col_10033_6886
Molinari, Gabriella
5d176297d3b6b36d5771fd16366e808d
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Wilde, Christian
fd05841fa9276d15d0b7ca6339fd44ce
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Just, Ingo
6fb02e3e2f57167d8d1c3db75fedaaf0
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Aktories, Klaus
486715084ea6926d55867b2479e4cfcc
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Department of Microbial Pathogenesis, GBF-German Research Centre for Biotechnology, Mascheroder Weg 1, 38124 Braunschweig, Germany.
2009-02-05T11:44:31Z
2009-02-05T11:44:31Z
2006-06
Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells. 2006, 74 (6):3673-7 Infect. Immun.
0019-9567
16714601
10.1128/IAI.02013-05
http://hdl.handle.net/10033/48537
Infection and immunity
The C3stau2 exoenzyme from Staphylococcus aureus is a C3-like ADP-ribosyltransferase which possesses no specific receptor-binding domain or translocation unit required for entry in target cells where its substrate is located. Here we show that C3stau2 can reach its target after invasion of staphylococci in eukaryotic cells without needing translocation.
en
ADP Ribose Transferases
Animals
Hela Cells
Humans
Mice
Microscopy, Immunoelectron
Protein Transport
Staphylococcus aureus
Virulence
Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells.
Article
2018-06-13T00:23:57Z
The C3stau2 exoenzyme from Staphylococcus aureus is a C3-like ADP-ribosyltransferase which possesses no specific receptor-binding domain or translocation unit required for entry in target cells where its substrate is located. Here we show that C3stau2 can reach its target after invasion of staphylococci in eukaryotic cells without needing translocation.
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oai:hzi.openrepository.com:10033/48537
2019-08-30 11:32:17.011
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/650542019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Dinkla, Katrin
81f17e1395e1a97fa5ca8ea2b6a3cdd4
500
Talay, Susanne R
5a6000962c21b07f4c6cda30597c0701
500
Mörgelin, Matthias
3b24bbdfdbc2401bc3afa6678a7b152e
500
Graham, Rikki M A
8c56d7dc1bc487990743d42a159c1c45
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Nitsche-Schmitz, D Patric
cb8c9f97bad4b6ed57d10ef22331a3f4
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Braunschweig, Germany.
2009-04-16T10:35:51Z
2009-04-16T10:35:51Z
2009
Crucial role of the CB3-region of collagen IV in PARF-induced acute rheumatic fever. 2009, 4 (3):e4666 PLoS ONE
1932-6203
19252743
10.1371/journal.pone.0004666
http://hdl.handle.net/10033/65054
PLoS ONE
Acute rheumatic fever (ARF) and rheumatic heart disease are serious autoimmune sequelae to infections with Streptococcus pyogenes. Streptococcal M-proteins have been implicated in ARF pathogenesis. Their interaction with collagen type IV (CIV) is a triggering step that induces generation of collagen-specific auto-antibodies. Electron microscopy of the protein complex between M-protein type 3 (M3-protein) and CIV identified two prominent binding sites of which one is situated in the CB3-region of CIV. In a radioactive binding assay, M3-protein expressing S. pyogenes and S. gordonii bound the CB3-fragment. Detailed analysis of the interactions by surface plasmon resonance measurements and site directed mutagenesis revealed high affinity interactions with dissociation constants in the nanomolar range that depend on the recently described collagen binding motif of streptococcal M-proteins. Because of its role in the induction of disease-related collagen autoimmunity the motif is referred to as "peptide associated with rheumatic fever" (PARF). Both, sera of mice immunized with M3-protein as well as sera from patients with ARF contained anti-CB3 auto-antibodies, indicating their contribution to ARF pathogenesis. The identification of the CB3-region as a binding partner for PARF directs the further approaches to understand the unusual autoimmune pathogenesis of PARF-dependent ARF and forms a molecular basis for a diagnostic test that detects rheumatogenic streptococci.
en
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=19252743
Crucial role of the CB3-region of collagen IV in PARF-induced acute rheumatic fever.
Article
2018-06-12T21:25:59Z
Acute rheumatic fever (ARF) and rheumatic heart disease are serious autoimmune sequelae to infections with Streptococcus pyogenes. Streptococcal M-proteins have been implicated in ARF pathogenesis. Their interaction with collagen type IV (CIV) is a triggering step that induces generation of collagen-specific auto-antibodies. Electron microscopy of the protein complex between M-protein type 3 (M3-protein) and CIV identified two prominent binding sites of which one is situated in the CB3-region of CIV. In a radioactive binding assay, M3-protein expressing S. pyogenes and S. gordonii bound the CB3-fragment. Detailed analysis of the interactions by surface plasmon resonance measurements and site directed mutagenesis revealed high affinity interactions with dissociation constants in the nanomolar range that depend on the recently described collagen binding motif of streptococcal M-proteins. Because of its role in the induction of disease-related collagen autoimmunity the motif is referred to as "peptide associated with rheumatic fever" (PARF). Both, sera of mice immunized with M3-protein as well as sera from patients with ARF contained anti-CB3 auto-antibodies, indicating their contribution to ARF pathogenesis. The identification of the CB3-region as a binding partner for PARF directs the further approaches to understand the unusual autoimmune pathogenesis of PARF-dependent ARF and forms a molecular basis for a diagnostic test that detects rheumatogenic streptococci.
ORIGINAL
Dinkla et al_final.pdf
Dinkla et al_final.pdf
Open Access publication
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TEXT
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10033/65054
oai:hzi.openrepository.com:10033/65054
2019-08-30 11:25:43.408
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/847332019-08-30T11:34:48Zcom_10033_6815com_10033_6814col_10033_6886
Mehboob, Farrakh
470bac0721cb9bcd99ac392f76966733
500
Junca, Howard
5673a883ce8a86c487dd3415d9743d9c
500
Schraa, Gosse
cae7e38614fb2ce836ac4e51eb99c902
500
Stams, Alfons J M
b1e4dd58526bac4a46cfb0fdd80e2843
500
Wageningen University, The Netherlands.
2009-10-23T07:38:19Z
2009-10-23T07:38:19Z
2009-06
Growth of Pseudomonas chloritidismutans AW-1(T) on n-alkanes with chlorate as electron acceptor. 2009, 83 (4):739-47 Appl. Microbiol. Biotechnol.
1432-0614
19352644
10.1007/s00253-009-1985-9
http://hdl.handle.net/10033/84733
Applied microbiology and biotechnology
Microbial (per)chlorate reduction is a unique process in which molecular oxygen is formed during the dismutation of chlorite. The oxygen thus formed may be used to degrade hydrocarbons by means of oxygenases under seemingly anoxic conditions. Up to now, no bacterium has been described that grows on aliphatic hydrocarbons with chlorate. Here, we report that Pseudomonas chloritidismutans AW-1(T) grows on n-alkanes (ranging from C7 until C12) with chlorate as electron acceptor. Strain AW-1(T) also grows on the intermediates of the presumed n-alkane degradation pathway. The specific growth rates on n-decane and chlorate and n-decane and oxygen were 0.5 +/- 0.1 and 0.4 +/- 0.02 day(-1), respectively. The key enzymes chlorate reductase and chlorite dismutase were assayed and found to be present. The oxygen-dependent alkane oxidation was demonstrated in whole-cell suspensions. The strain degrades n-alkanes with oxygen and chlorate but not with nitrate, thus suggesting that the strain employs oxygenase-dependent pathways for the breakdown of n-alkanes.
en
Alkanes
Chlorates
Molecular Sequence Data
Nitrates
Oxidoreductases
Oxygen
Pseudomonas
Growth of Pseudomonas chloritidismutans AW-1(T) on n-alkanes with chlorate as electron acceptor.
Article
2018-06-13T00:57:35Z
Microbial (per)chlorate reduction is a unique process in which molecular oxygen is formed during the dismutation of chlorite. The oxygen thus formed may be used to degrade hydrocarbons by means of oxygenases under seemingly anoxic conditions. Up to now, no bacterium has been described that grows on aliphatic hydrocarbons with chlorate. Here, we report that Pseudomonas chloritidismutans AW-1(T) grows on n-alkanes (ranging from C7 until C12) with chlorate as electron acceptor. Strain AW-1(T) also grows on the intermediates of the presumed n-alkane degradation pathway. The specific growth rates on n-decane and chlorate and n-decane and oxygen were 0.5 +/- 0.1 and 0.4 +/- 0.02 day(-1), respectively. The key enzymes chlorate reductase and chlorite dismutase were assayed and found to be present. The oxygen-dependent alkane oxidation was demonstrated in whole-cell suspensions. The strain degrades n-alkanes with oxygen and chlorate but not with nitrate, thus suggesting that the strain employs oxygenase-dependent pathways for the breakdown of n-alkanes.
ORIGINAL
Mehboob et al_final.pdf
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final manuscript
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LICENSE
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TEXT
Mehboob et al_final.pdf.txt
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10033/84733
oai:hzi.openrepository.com:10033/84733
2019-08-30 11:34:48.358
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/929422019-08-30T11:35:13Zcom_10033_6815com_10033_6814col_10033_6886
Candela, Marco
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Biagi, Elena
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Centanni, Manuela
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Turroni, Silvia
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Vici, Manuela
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Musiani, Francesco
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Vitali, Beatrice
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Bergmann, Simone
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Hammerschmidt, Sven
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Brigidi, Patrizia
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Department of Pharmaceutical Sciences, CIRB-centre for Biotechnology, University of Bologna, Italy.
2010-02-24T14:25:06Z
2010-02-24T14:25:06Z
2009-10
Bifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the host. 2009, 155 (Pt 10):3294-303 Microbiology (Reading, Engl.)
1350-0872
19574304
10.1099/mic.0.028795-0
http://hdl.handle.net/10033/92942
Microbiology (Reading, England)
The interaction with the host plasminogen/plasmin system represents a novel component in the molecular cross-talk between bifidobacteria and human host. Here, we demonstrated that the plasminogen-binding bifidobacterial species B. longum, B. bifidum, B. breve and B. lactis share the key glycolytic enzyme enolase as a surface receptor for human plasminogen. Enolase was visualized on the cell surface of the model strain B. lactis BI07. The His-tagged recombinant protein showed a high affinity for human plasminogen, with an equilibrium dissociation constant in the nanomolar range. By site-directed mutagenesis we demonstrated that the interaction between the B. lactis BI07 enolase and human plasminogen involves an internal plasminogen-binding site homologous to that of pneumococcal enolase. According to our data, the positively charged residues Lys-251 and Lys-255, as well as the negatively charged Glu-252, of the B. lactis BI07 enolase are crucial for plasminogen binding. Acting as a human plasminogen receptor, the bifidobacterial surface enolase is suggested to play an important role in the interaction process with the host.
en
Bifidobacterium
Binding Sites
DNA, Bacterial
Host-Pathogen Interactions
Humans
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Phosphopyruvate Hydratase
Plasminogen
Protein Binding
Protein Interaction Mapping
Sequence Analysis, DNA
Bifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the host.
Article
2010-10-15T00:00:00Z
The interaction with the host plasminogen/plasmin system represents a novel component in the molecular cross-talk between bifidobacteria and human host. Here, we demonstrated that the plasminogen-binding bifidobacterial species B. longum, B. bifidum, B. breve and B. lactis share the key glycolytic enzyme enolase as a surface receptor for human plasminogen. Enolase was visualized on the cell surface of the model strain B. lactis BI07. The His-tagged recombinant protein showed a high affinity for human plasminogen, with an equilibrium dissociation constant in the nanomolar range. By site-directed mutagenesis we demonstrated that the interaction between the B. lactis BI07 enolase and human plasminogen involves an internal plasminogen-binding site homologous to that of pneumococcal enolase. According to our data, the positively charged residues Lys-251 and Lys-255, as well as the negatively charged Glu-252, of the B. lactis BI07 enolase are crucial for plasminogen binding. Acting as a human plasminogen receptor, the bifidobacterial surface enolase is suggested to play an important role in the interaction process with the host.
ORIGINAL
Candela et al_final.pdf
Candela et al_final.pdf
allowed publishers pdf after embargo period
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THUMBNAIL
Candela et al_final.pdf.jpg
Candela et al_final.pdf.jpg
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TEXT
Candela et al_final.pdf.txt
Candela et al_final.pdf.txt
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oai:hzi.openrepository.com:10033/92942
2019-08-30 11:35:13.87
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/980532019-08-30T11:26:07Zcom_10033_6815com_10033_6814col_10033_6886
Moeller, Ralf
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Rohde, Manfred
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Reitz, Günther
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Department of Medical Microbiology, Helmholtz Centre for Infection Research, Inhoffenstr. 7, D-38124 Braunschweig, Germany
2010-05-06T13:18:28Z
2010-05-06T13:18:28Z
2010-04
Moeller, R., Rohde, M., Reitz, G. Effects of ionizing radiation on the survival of bacterial spores in artificial martian regolith (2010) Icarus, 206 (2), pp. 783-786.
DOI: 10.1016/j.icarus.2009.11.014
http://hdl.handle.net/10033/98053
Icarus
Science Direct
Effects of ionizing radiation on the survival of bacterial spares in artificial martia regolith
Article
2018-06-12T20:05:38Z
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ORIGINAL
Moeller et al_final.pdf
Moeller et al_final.pdf
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TEXT
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2019-08-30 11:26:07.767
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1067782019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Reissmann, Silvana
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Rodloff, Arne C
fbc333f987c5873f18f41fcc0ab5daa5
500
Brahmadathan, Kootallur N
5a726c3fce0db03c60b85e46c5d063c0
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Nitsche-Schmitz, D Patric
cb8c9f97bad4b6ed57d10ef22331a3f4
500
Helmholtz Centre for Infection Research, Braunschweig, Germany.
2010-06-24T09:36:11Z
2010-06-24T09:36:11Z
2010-04
Contribution of Streptococcus anginosus to infections caused by groups C and G streptococci, southern India. 2010, 16 (4):656-63 Emerging Infect. Dis.
1080-6059
20350380
http://hdl.handle.net/10033/106778
Emerging infectious diseases
Vellore, a region in southern India, has a high incidence of severe human infections with Beta-hemolytic group C and G streptococci (GCGS). To determine the causative species in these infections, we conducted 16S rRNA gene sequencing: Streptococcus dysgalactiae subsp. equisimilis (81%) and S. anginosus (19%) were the causative organisms in the 2-year study period (2006-2007). We used PCR to detect the virulence-related emm gene; results showed that it was restricted to S. dysgalactieae subsp. equisimilis isolates of 99.2% tested positive. Due to a novel marker, S. anginosus and S. constellatus can be quickly and accurately distinguished from other members of the genus. The notable contribution of the anginosus group to human infections suggests that this group of obligate pathogens deserves more attention in healthcare and research.
en
DNA, Bacterial
Genes, Bacterial
Genetic Markers
Humans
India
Open Reading Frames
Polymerase Chain Reaction
RNA, Ribosomal, 16S
Sequence Analysis, DNA
Streptococcal Infections
Streptococcus
Streptococcus anginosus
Streptococcus constellatus
Virulence Factors
Contribution of Streptococcus anginosus to infections caused by groups C and G streptococci, southern India.
Article
2018-06-13T00:56:20Z
Vellore, a region in southern India, has a high incidence of severe human infections with Beta-hemolytic group C and G streptococci (GCGS). To determine the causative species in these infections, we conducted 16S rRNA gene sequencing: Streptococcus dysgalactiae subsp. equisimilis (81%) and S. anginosus (19%) were the causative organisms in the 2-year study period (2006-2007). We used PCR to detect the virulence-related emm gene; results showed that it was restricted to S. dysgalactieae subsp. equisimilis isolates of 99.2% tested positive. Due to a novel marker, S. anginosus and S. constellatus can be quickly and accurately distinguished from other members of the genus. The notable contribution of the anginosus group to human infections suggests that this group of obligate pathogens deserves more attention in healthcare and research.
ORIGINAL
Reißmann et al_final.pdf
Reißmann et al_final.pdf
Open Access document
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oai:hzi.openrepository.com:10033/106778
2019-08-30 11:35:39.466
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1111482019-08-30T11:31:49Zcom_10033_6815com_10033_6814col_10033_6886
Candela, Marco
8d222d25d482ebaf1a5dc9a1e65f3436
500
Centanni, Manuela
169beec34868d34aae9d2965a8027e58
500
Fiori, Jessica
2d0f16e3a36ce987e9eae70289de303c
500
Biagi, Elena
0e988c15573f01ca8ad44455865e9cfb
500
Turroni, Silvia
f931c3a35612723f5382506e79c23278
500
Orrico, Catia
146cbe231c4a683e005881783eb40b18
500
Bergmann, Simone
f37a40ca97e3a301c072bcf4cbbb91ea
500
Hammerschmidt, Sven
721efda1f965cd4be1552565a54d8b5b
500
Brigidi, Patrizia
22cfd509db32566ee736e166d95d4fc9
500
Department of Pharmaceutical Sciences, University of Bologna, Italy.
2010-09-14T10:50:07Z
2010-09-14T10:50:07Z
2010-06
DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts. 2010, 156 (Pt 6):1609-18 Microbiology (Reading, Engl.)
1465-2080
20167618
10.1099/mic.0.038307-0
http://hdl.handle.net/10033/111148
Microbiology (Reading, England)
Bifidobacterium animalis subsp. lactis lives in the gastrointestinal tract of most mammals, including humans. Recently, for the probiotic strain B. animalis subsp. lactis BI07, a dose-dependent plasminogen-binding activity was demonstrated and five putative plasminogen-binding proteins were identified. Here we investigated the role of surface DnaK as a B. animalis subsp. lactis BI07 plasminogen receptor. DnaK was visualized on the bacterial cell surface by transmission electron microscopy. The His-tagged recombinant DnaK protein showed a high affinity for human plasminogen, with an equilibrium dissociation constant in the nanomolar range. The capability to tolerate physiological concentrations of bile salts is a crucial feature for an intestinal symbiont micro-organism. By proteome analysis we demonstrated that the long-term exposure of B. animalis subsp. lactis BI07 to bile salts results in the upregulation of important surface plasminogen receptors such as DnaK and enolase. Moreover, adaptation of B. animalis subsp. lactis BI07 to physiological concentrations of bile salts significantly increased its capacity to interact with the host plasminogen system. By enhancing the bacterial capacity to interact with the host plasminogen, the gut bile environment may facilitate the colonization of the human host by B. animalis subsp. lactis BI07.
en
Bacterial Proteins
Bifidobacterium
Bile Acids and Salts
Gastrointestinal Tract
HSP70 Heat-Shock Proteins
Humans
Microscopy, Electron, Transmission
Phosphopyruvate Hydratase
Plasminogen
Proteome
Recombinant Proteins
Up-Regulation
DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts.
Article
2012-06-15T00:00:00Z
Bifidobacterium animalis subsp. lactis lives in the gastrointestinal tract of most mammals, including humans. Recently, for the probiotic strain B. animalis subsp. lactis BI07, a dose-dependent plasminogen-binding activity was demonstrated and five putative plasminogen-binding proteins were identified. Here we investigated the role of surface DnaK as a B. animalis subsp. lactis BI07 plasminogen receptor. DnaK was visualized on the bacterial cell surface by transmission electron microscopy. The His-tagged recombinant DnaK protein showed a high affinity for human plasminogen, with an equilibrium dissociation constant in the nanomolar range. The capability to tolerate physiological concentrations of bile salts is a crucial feature for an intestinal symbiont micro-organism. By proteome analysis we demonstrated that the long-term exposure of B. animalis subsp. lactis BI07 to bile salts results in the upregulation of important surface plasminogen receptors such as DnaK and enolase. Moreover, adaptation of B. animalis subsp. lactis BI07 to physiological concentrations of bile salts significantly increased its capacity to interact with the host plasminogen system. By enhancing the bacterial capacity to interact with the host plasminogen, the gut bile environment may facilitate the colonization of the human host by B. animalis subsp. lactis BI07.
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oai:hzi.openrepository.com:10033/111148
2019-08-30 11:31:49.536
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1171652019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Itzek, Andreas
5742f09a19452ec7163791e1323aedb2
500
Gillen, Christine M
50af3bbc78783e699669dea49de1eb9e
500
Fulde, Marcus
8e6c69232f5183b89bc38e4c9811ef00
500
Friedrichs, Claudia
5760a5dbed5f687479b1bb0bb4fb8adc
500
Rodloff, Arne C
fbc333f987c5873f18f41fcc0ab5daa5
500
Chhatwal, Gursharan S
5f2bb8ec30d6711867f55a23959f3c98
500
Nitsche-Schmitz, Daniel Patric
7579ab19b7f34fc0c9cbf6080a689eef
500
Department of Medical Microbiology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
2010-12-03T15:41:05Z
2010-12-03T15:41:05Z
2010
Contribution of plasminogen activation towards the pathogenic potential of oral streptococci. 2010, 5 (11):e13826 PLoS ONE
1932-6203
21072208
10.1371/journal.pone.0013826
http://hdl.handle.net/10033/117165
PloS one
Oral streptococci are a heterogeneous group of human commensals, with a potential to cause serious infections. Activation of plasminogen has been shown to increase the virulence of typical human pathogenic streptococci such as S. pneumoniae. One important factor for plasminogen activation is the streptococcal α-enolase. Here we report that plasminogen activation is also common in oral streptococci species involved in clinical infection and that it depends on the action of human plasminogen activators. The ability to activate plasminogen did not require full conservation of the internal plasminogen binding sequence motif FYDKERKVY of α-enolase that was previously described as crucial for increased plasminogen binding, activation and virulence. Instead, experiments with recombinant α-enolase variants indicate that the naturally occurring variations do not impair plasminogen binding. In spite of these variations in the internal plasminogen binding motif oral streptococci showed similar activation of plasminogen. We conclude that the pathomechanism of plasminogen activation is conserved in oral streptococci that cause infections in human. This may contribute to their opportunistic pathogenic character that is unfurled in certain niches.
en
Contribution of plasminogen activation towards the pathogenic potential of oral streptococci.
Article
2018-06-12T21:26:37Z
Oral streptococci are a heterogeneous group of human commensals, with a potential to cause serious infections. Activation of plasminogen has been shown to increase the virulence of typical human pathogenic streptococci such as S. pneumoniae. One important factor for plasminogen activation is the streptococcal α-enolase. Here we report that plasminogen activation is also common in oral streptococci species involved in clinical infection and that it depends on the action of human plasminogen activators. The ability to activate plasminogen did not require full conservation of the internal plasminogen binding sequence motif FYDKERKVY of α-enolase that was previously described as crucial for increased plasminogen binding, activation and virulence. Instead, experiments with recombinant α-enolase variants indicate that the naturally occurring variations do not impair plasminogen binding. In spite of these variations in the internal plasminogen binding motif oral streptococci showed similar activation of plasminogen. We conclude that the pathomechanism of plasminogen activation is conserved in oral streptococci that cause infections in human. This may contribute to their opportunistic pathogenic character that is unfurled in certain niches.
ORIGINAL
Itzek et al_final.pdf
Itzek et al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/1185682019-08-30T11:36:05Zcom_10033_6815com_10033_6814col_10033_6886
Hoffmann, Christine
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Agerer, Franziska
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Buntru, Alexander
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Neske, Florian
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Chhatwal, G Singh
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Ohlsen, Knut
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Hauck, Christof R
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Lehrstuhl Zellbiologie X908, Universität Konstanz, Universitätsstr. 10, 78457 Konstanz, Germany.
2011-01-04T15:30:24Z
2011-01-04T15:30:24Z
2010-12-15
Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens. 2010, 123 (Pt 24):4280-91 J. Cell. Sci.
1477-9137
21098633
10.1242/jcs.064006
http://hdl.handle.net/10033/118568
Journal of cell science
Staphylococcus aureus, which is a leading cause of hospital-acquired infections, binds via fibronectin to integrin α5β1, a process that can promote host colonization in vivo. Integrin engagement induces actin cytoskeleton rearrangements that result in the uptake of S. aureus by non-professional phagocytic cells. Interestingly, we found that fibronectin-binding S. aureus trigger the redistribution of membrane microdomain components. In particular, ganglioside GM1 and GPI-linked proteins were recruited upon integrin β1 engagement, and disruption of membrane microdomains blocked bacterial internalization. Several membrane-microdomain-associated proteins, such as flotillin-1 and flotillin-2, as well as caveolin, were recruited to sites of bacterial attachment. Whereas dominant-negative versions of flotillin-2 did not affect bacterial attachment or internalization, cells deficient for caveolin-1 (Cav1(-/-)) showed increased uptake of S. aureus and other Fn-binding pathogens. Recruitment of membrane microdomains to cell-associated bacteria was unaltered in Cav1(-/-) cells. However, fluorescence recovery after photobleaching (FRAP) revealed an enhanced mobility of membrane-microdomain-associated proteins in the absence of caveolin-1. Enhanced membrane microdomain mobility and increased uptake of S. aureus was repressed by expression of wild-type caveolin-1, but not caveolin-1 G83S, which harbors a point mutation in the caveolin scaffolding domain. Similarly, chemical or physical stimulation of membrane fluidity led to increased uptake of S. aureus. These results highlight a crucial role for caveolin-1 in negative regulation of membrane microdomain mobility, thereby affecting endocytosis of bacteria-engaged integrins. This process might not only limit host cell invasion by integrin-binding bacterial pathogens, but might also be physiologically relevant for integrin-mediated cell adhesion.
en
Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens.
Article
2011-12-15T00:00:00Z
Staphylococcus aureus, which is a leading cause of hospital-acquired infections, binds via fibronectin to integrin α5β1, a process that can promote host colonization in vivo. Integrin engagement induces actin cytoskeleton rearrangements that result in the uptake of S. aureus by non-professional phagocytic cells. Interestingly, we found that fibronectin-binding S. aureus trigger the redistribution of membrane microdomain components. In particular, ganglioside GM1 and GPI-linked proteins were recruited upon integrin β1 engagement, and disruption of membrane microdomains blocked bacterial internalization. Several membrane-microdomain-associated proteins, such as flotillin-1 and flotillin-2, as well as caveolin, were recruited to sites of bacterial attachment. Whereas dominant-negative versions of flotillin-2 did not affect bacterial attachment or internalization, cells deficient for caveolin-1 (Cav1(-/-)) showed increased uptake of S. aureus and other Fn-binding pathogens. Recruitment of membrane microdomains to cell-associated bacteria was unaltered in Cav1(-/-) cells. However, fluorescence recovery after photobleaching (FRAP) revealed an enhanced mobility of membrane-microdomain-associated proteins in the absence of caveolin-1. Enhanced membrane microdomain mobility and increased uptake of S. aureus was repressed by expression of wild-type caveolin-1, but not caveolin-1 G83S, which harbors a point mutation in the caveolin scaffolding domain. Similarly, chemical or physical stimulation of membrane fluidity led to increased uptake of S. aureus. These results highlight a crucial role for caveolin-1 in negative regulation of membrane microdomain mobility, thereby affecting endocytosis of bacteria-engaged integrins. This process might not only limit host cell invasion by integrin-binding bacterial pathogens, but might also be physiologically relevant for integrin-mediated cell adhesion.
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oai:repository.helmholtz-hzi.de:10033/1205452019-08-30T11:36:05Zcom_10033_6815com_10033_6814col_10033_6886
Aziz, Ramy K
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Kansal, Rita
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Aronow, Bruce J
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Taylor, William L
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Rowe, Sarah L
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Kubal, Michael
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Chhatwal, Gursharan S
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Kotb, Malak
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Research Services, Veterans Affairs Medical Center, Memphis, Tennessee, United States of America. ramy.aziz@salmonella.org
2011-01-28T09:23:00Z
2011-01-28T09:23:00Z
2010
Microevolution of group A streptococci in vivo: capturing regulatory networks engaged in sociomicrobiology, niche adaptation, and hypervirulence. 2010, 5 (4):e9798 PLoS ONE
1932-6203
20418946
10.1371/journal.pone.0009798
http://hdl.handle.net/10033/120545
PloS one
The onset of infection and the switch from primary to secondary niches are dramatic environmental changes that not only alter bacterial transcriptional programs, but also perturb their sociomicrobiology, often driving minor subpopulations with mutant phenotypes to prevail in specific niches. Having previously reported that M1T1 Streptococcus pyogenes become hypervirulent in mice due to selection of mutants in the covRS regulatory genes, we set out to dissect the impact of these mutations in vitro and in vivo from the impact of other adaptive events. Using a murine subcutaneous chamber model to sample the bacteria prior to selection or expansion of mutants, we compared gene expression dynamics of wild type (WT) and previously isolated animal-passaged (AP) covS mutant bacteria both in vitro and in vivo, and we found extensive transcriptional alterations of pathoadaptive and metabolic gene sets associated with invasion, immune evasion, tissue-dissemination, and metabolic reprogramming. In contrast to the virulence-associated differences between WT and AP bacteria, Phenotype Microarray analysis showed minor in vitro phenotypic differences between the two isogenic variants. Additionally, our results reflect that WT bacteria's rapid host-adaptive transcriptional reprogramming was not sufficient for their survival, and they were outnumbered by hypervirulent covS mutants with SpeB(-)/Sda(high) phenotype, which survived up to 14 days in mice chambers. Our findings demonstrate the engagement of unique regulatory modules in niche adaptation, implicate a critical role for bacterial genetic heterogeneity that surpasses transcriptional in vivo adaptation, and portray the dynamics underlying the selection of hypervirulent covS mutants over their parental WT cells.
en
Microevolution of group A streptococci in vivo: capturing regulatory networks engaged in sociomicrobiology, niche adaptation, and hypervirulence.
Article
2018-06-13T00:53:33Z
The onset of infection and the switch from primary to secondary niches are dramatic environmental changes that not only alter bacterial transcriptional programs, but also perturb their sociomicrobiology, often driving minor subpopulations with mutant phenotypes to prevail in specific niches. Having previously reported that M1T1 Streptococcus pyogenes become hypervirulent in mice due to selection of mutants in the covRS regulatory genes, we set out to dissect the impact of these mutations in vitro and in vivo from the impact of other adaptive events. Using a murine subcutaneous chamber model to sample the bacteria prior to selection or expansion of mutants, we compared gene expression dynamics of wild type (WT) and previously isolated animal-passaged (AP) covS mutant bacteria both in vitro and in vivo, and we found extensive transcriptional alterations of pathoadaptive and metabolic gene sets associated with invasion, immune evasion, tissue-dissemination, and metabolic reprogramming. In contrast to the virulence-associated differences between WT and AP bacteria, Phenotype Microarray analysis showed minor in vitro phenotypic differences between the two isogenic variants. Additionally, our results reflect that WT bacteria's rapid host-adaptive transcriptional reprogramming was not sufficient for their survival, and they were outnumbered by hypervirulent covS mutants with SpeB(-)/Sda(high) phenotype, which survived up to 14 days in mice chambers. Our findings demonstrate the engagement of unique regulatory modules in niche adaptation, implicate a critical role for bacterial genetic heterogeneity that surpasses transcriptional in vivo adaptation, and portray the dynamics underlying the selection of hypervirulent covS mutants over their parental WT cells.
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Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/1233042019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
Bunk, Boyke
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Schulz, Arne
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Stammen, Simon
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Münch, Richard
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Warren, Martin J
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Rohde, Manfred
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Jahn, Dieter
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Biedendieck, Rebekka
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Institute of Microbiology; Technische Universität Braunschweig; Braunschweig, Germany.
2011-03-02T15:05:00Z
2011-03-02T15:05:00Z
2011-03-02T15:05:00Z
A short story about a big magic bug. 2010, 1 (2):85-91notBioeng Bugs
1949-1026
21326933
10.4161/bbug.1.2.11101
http://hdl.handle.net/10033/123304
Bioengineered bugs
Bacillus megaterium, the "big beast," is a Gram-positive bacterium with a size of 4 × 1.5 µm. During the last years, it became more and more popular in the field of biotechnology for its recombinant protein production capacity. For the purpose of intra- as well as extracellular protein synthesis several vectors were constructed and commercialized (MoBiTec GmbH, Germany). On the basis of two compatible vectors, a T7 RNA polymerase driven protein production system was established. Vectors for chromosomal integration enable the direct manipulation of the genome. The vitamin B(12) biosynthesis of B. megaterium served as a model for the systematic development of a production strain using these tools. For this purpose, the overexpression of chromosomal and plasmid encoded genes and operons, the synthesis of anti-sense RNA for gene silencing, the removal of inhibitory regulatory elements in combination with the utilization of strong promoters, directed protein design, and the recombinant production of B(12) binding proteins to overcome feedback inhibition were successfully employed. For further system biotechnology based optimization strategies the genome sequence will provide a closer look into genomic capacities of B. megaterium. DNA arrays are available. Proteome, fluxome and metabolome analyses are possible. All data can be integrated by using a novel bioinformatics platform. Finally, the size of the "big beast" B. megaterium invites for cell biology research projects. All these features provide a solid basis for challenging biotechnological approaches.
ENG
A short story about a big magic bug.
Article
2018-06-12T18:11:50Z
Bacillus megaterium, the "big beast," is a Gram-positive bacterium with a size of 4 × 1.5 µm. During the last years, it became more and more popular in the field of biotechnology for its recombinant protein production capacity. For the purpose of intra- as well as extracellular protein synthesis several vectors were constructed and commercialized (MoBiTec GmbH, Germany). On the basis of two compatible vectors, a T7 RNA polymerase driven protein production system was established. Vectors for chromosomal integration enable the direct manipulation of the genome. The vitamin B(12) biosynthesis of B. megaterium served as a model for the systematic development of a production strain using these tools. For this purpose, the overexpression of chromosomal and plasmid encoded genes and operons, the synthesis of anti-sense RNA for gene silencing, the removal of inhibitory regulatory elements in combination with the utilization of strong promoters, directed protein design, and the recombinant production of B(12) binding proteins to overcome feedback inhibition were successfully employed. For further system biotechnology based optimization strategies the genome sequence will provide a closer look into genomic capacities of B. megaterium. DNA arrays are available. Proteome, fluxome and metabolome analyses are possible. All data can be integrated by using a novel bioinformatics platform. Finally, the size of the "big beast" B. megaterium invites for cell biology research projects. All these features provide a solid basis for challenging biotechnological approaches.
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2019-08-30 11:36:32.807
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1241092019-08-30T11:36:33Zcom_10033_6815com_10033_6814col_10033_6886
Kaur, Simran Jeet
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Nerlich, Andreas
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500
Bergmann, Simone
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Rohde, Manfred
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Fulde, Marcus
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Zähner, Dorothea
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Hanski, Emanuel
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Zinkernagel, Annelies
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Nizet, Victor
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Chhatwal, Gursharan S
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Talay, Susanne R
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Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
2011-03-10T12:34:53Z
2011-03-10T12:34:53Z
2010-09-03
The CXC chemokine-degrading protease SpyCep of Streptococcus pyogenes promotes its uptake into endothelial cells. 2010, 285 (36):27798-805 J. Biol. Chem.
1083-351X
20562101
10.1074/jbc.M109.098053
http://hdl.handle.net/10033/124109
The Journal of biological chemistry
Streptococcus pyogenes expresses the LPXTG motif-containing cell envelope serine protease SpyCep (also called ScpC, PrtS) that degrades and inactivates the major chemoattractant interleukin 8 (IL-8), thereby impairing host neutrophil recruitment. In this study, we identified a novel function of SpyCep: the ability to mediate uptake into primary human endothelial cells. SpyCep triggered its uptake into endothelial cells but not into human epithelial cells originating from pharynx or lung, indicating an endothelial cell-specific uptake mechanism. SpyCep mediated cellular invasion by an endosomal/lysosomal pathway distinct from the caveolae-mediated invasion pathway of S. pyogenes. Recombinant expression and purification of proteolytically active SpyCep and a series of subfragments allowed functional dissection of the domains responsible for endothelial cell invasion and IL-8 degradation. The N-terminal PR domain was sufficient to mediate endothelial cell invasion, whereas for IL-8-degrading activity, the protease domain and the flanking A domain were required. A polyclonal rabbit serum raised against the recombinant protease efficiently blocked the invasion-mediating activity of SpyCep but not its proteolytic function, further indicating that SpyCep-mediated internalization is independent from its enzymatic activity. SpyCep may thus specifically mediate its own uptake as secreted protein into human endothelial cells.
en
Animals
Antibodies
Cell Line
Cloning, Molecular
Endocytosis
Endosomes
Endothelial Cells
Humans
Interleukin-8
Lysosomes
Peptide Hydrolases
Protein Structure, Tertiary
Protein Transport
Streptococcus pyogenes
The CXC chemokine-degrading protease SpyCep of Streptococcus pyogenes promotes its uptake into endothelial cells.
Article
2011-09-15T00:00:00Z
Streptococcus pyogenes expresses the LPXTG motif-containing cell envelope serine protease SpyCep (also called ScpC, PrtS) that degrades and inactivates the major chemoattractant interleukin 8 (IL-8), thereby impairing host neutrophil recruitment. In this study, we identified a novel function of SpyCep: the ability to mediate uptake into primary human endothelial cells. SpyCep triggered its uptake into endothelial cells but not into human epithelial cells originating from pharynx or lung, indicating an endothelial cell-specific uptake mechanism. SpyCep mediated cellular invasion by an endosomal/lysosomal pathway distinct from the caveolae-mediated invasion pathway of S. pyogenes. Recombinant expression and purification of proteolytically active SpyCep and a series of subfragments allowed functional dissection of the domains responsible for endothelial cell invasion and IL-8 degradation. The N-terminal PR domain was sufficient to mediate endothelial cell invasion, whereas for IL-8-degrading activity, the protease domain and the flanking A domain were required. A polyclonal rabbit serum raised against the recombinant protease efficiently blocked the invasion-mediating activity of SpyCep but not its proteolytic function, further indicating that SpyCep-mediated internalization is independent from its enzymatic activity. SpyCep may thus specifically mediate its own uptake as secreted protein into human endothelial cells.
ORIGINAL
Kaur et al_final.pdf
Kaur et al_final.pdf
original manuscript
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2019-08-30 11:36:33.116
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1297482019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Itzek, Andreas
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Gillen, Christine M
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Fulde, Marcus
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Friedrichs, Claudia
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Rodloff, Arne C
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Chhatwal, Gursharan S
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Nitsche-Schmitz, Daniel Patric
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Department of Medical Microbiology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
2011-05-18T10:49:27Z
2011-05-18T10:49:27Z
2010
Contribution of plasminogen activation towards the pathogenic potential of oral streptococci. 2010, 5 (11):e13826 PLoS ONE
1932-6203
21072208
10.1371/journal.pone.0013826
http://hdl.handle.net/10033/129748
PloS one
Oral streptococci are a heterogeneous group of human commensals, with a potential to cause serious infections. Activation of plasminogen has been shown to increase the virulence of typical human pathogenic streptococci such as S. pneumoniae. One important factor for plasminogen activation is the streptococcal α-enolase. Here we report that plasminogen activation is also common in oral streptococci species involved in clinical infection and that it depends on the action of human plasminogen activators. The ability to activate plasminogen did not require full conservation of the internal plasminogen binding sequence motif FYDKERKVY of α-enolase that was previously described as crucial for increased plasminogen binding, activation and virulence. Instead, experiments with recombinant α-enolase variants indicate that the naturally occurring variations do not impair plasminogen binding. In spite of these variations in the internal plasminogen binding motif oral streptococci showed similar activation of plasminogen. We conclude that the pathomechanism of plasminogen activation is conserved in oral streptococci that cause infections in human. This may contribute to their opportunistic pathogenic character that is unfurled in certain niches.
en
Amino Acid Sequence
Bacterial Proteins
Binding Sites
Electrophoresis, Polyacrylamide Gel
Fibrinolysin
Humans
Immunoblotting
Molecular Sequence Data
Mouth
Mutation
Phosphopyruvate Hydratase
Plasminogen
Plasminogen Activators
Protein Binding
Sequence Homology, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Streptococcal Infections
Streptococcus
Streptococcus oralis
Virulence
Contribution of plasminogen activation towards the pathogenic potential of oral streptococci.
Article
2018-06-13T17:10:59Z
Oral streptococci are a heterogeneous group of human commensals, with a potential to cause serious infections. Activation of plasminogen has been shown to increase the virulence of typical human pathogenic streptococci such as S. pneumoniae. One important factor for plasminogen activation is the streptococcal α-enolase. Here we report that plasminogen activation is also common in oral streptococci species involved in clinical infection and that it depends on the action of human plasminogen activators. The ability to activate plasminogen did not require full conservation of the internal plasminogen binding sequence motif FYDKERKVY of α-enolase that was previously described as crucial for increased plasminogen binding, activation and virulence. Instead, experiments with recombinant α-enolase variants indicate that the naturally occurring variations do not impair plasminogen binding. In spite of these variations in the internal plasminogen binding motif oral streptococci showed similar activation of plasminogen. We conclude that the pathomechanism of plasminogen activation is conserved in oral streptococci that cause infections in human. This may contribute to their opportunistic pathogenic character that is unfurled in certain niches.
ORIGINAL
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1385702019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Fulde, Marcus
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Rohde, Manfred
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Hitzmann, Angela
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Preissner, Klaus T
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Nitsche-Schmitz, D Patric
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Nerlich, Andreas
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Chhatwal, Gursharan Singh
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Bergmann, Simone
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Department of Medical Microbiology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany. Marcus.Fulde@helmholtz-hzi.de
2011-08-02T13:41:44Z
2011-08-02T13:41:44Z
2011-02-24
SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration. 2011, 434 (3):523-35 Biochem. J.
1470-8728
21210764
10.1042/BJ20101121
http://hdl.handle.net/10033/138570
The Biochemical journal
Streptococcus canis is an important zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. In the present paper we report the binding of human plasminogen to S. canis and the recruitment of proteolytically active plasmin on its surface. The binding receptor for plasminogen was identified as a novel M-like protein designated SCM (S. canis M-like protein). SPR (surface plasmon resonance) analyses, radioactive dot-blot analyses and heterologous expression on the surface of Streptococcus gordonii confirmed the plasminogen-binding capability of SCM. The binding domain was located within the N-terminus of SCM, which specifically bound to the C-terminal part of plasminogen (mini-plasminogen) comprising kringle domain 5 and the catalytic domain. In the presence of urokinase, SCM mediated plasminogen activation on the bacterial surface that was inhibited by serine protease inhibitors and lysine amino acid analogues. Surface-bound plasmin effectively degraded purified fibrinogen as well as fibrin clots, resulting in the dissolution of fibrin thrombi. Electron microscopic illustration and time-lapse imaging demonstrated bacterial transmigration through fibrinous thrombi. The present study has led, for the first time, to the identification of SCM as a novel receptor for (mini)-plasminogen mediating the fibrinolytic activity of S. canis.
en
Animals
Bacterial Proteins
Binding Sites
Carrier Proteins
Catalytic Domain
Cats
Dogs
Fibrin
Fibrinogen
Fibrinolysin
Host-Pathogen Interactions
Humans
Kringles
Plasma
Plasminogen
Protein Binding
Streptococcus
Swine
SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration.
Article
2012-03-15T00:00:00Z
Streptococcus canis is an important zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. In the present paper we report the binding of human plasminogen to S. canis and the recruitment of proteolytically active plasmin on its surface. The binding receptor for plasminogen was identified as a novel M-like protein designated SCM (S. canis M-like protein). SPR (surface plasmon resonance) analyses, radioactive dot-blot analyses and heterologous expression on the surface of Streptococcus gordonii confirmed the plasminogen-binding capability of SCM. The binding domain was located within the N-terminus of SCM, which specifically bound to the C-terminal part of plasminogen (mini-plasminogen) comprising kringle domain 5 and the catalytic domain. In the presence of urokinase, SCM mediated plasminogen activation on the bacterial surface that was inhibited by serine protease inhibitors and lysine amino acid analogues. Surface-bound plasmin effectively degraded purified fibrinogen as well as fibrin clots, resulting in the dissolution of fibrin thrombi. Electron microscopic illustration and time-lapse imaging demonstrated bacterial transmigration through fibrinous thrombi. The present study has led, for the first time, to the identification of SCM as a novel receptor for (mini)-plasminogen mediating the fibrinolytic activity of S. canis.
ORIGINAL
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1396892019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Bergmann, René
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Dinkla, Katrin
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Nitsche-Schmitz, D Patric
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Graham, Rikki M A
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Lüttge, Melanie
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Sanderson-Smith, Martina L
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Nerlich, Andreas
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Rohde, Manfred
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Chhatwal, Gursharan S
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Dept. of Medical Microbiology, Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.
2011-08-15T09:10:24Z
2011-08-15T09:10:24Z
2011-02
Biological functions of GCS3, a novel plasminogen-binding protein of Streptococcus dysgalactiae ssp. equisimilis. 2011, 301 (2):157-64 Int. J. Med. Microbiol.
1618-0607
20951639
10.1016/j.ijmm.2010.06.007
http://hdl.handle.net/10033/139689
International journal of medical microbiology : IJMM
Increasing awareness of the relevance of Streptococcus dysgalactiae ssp. equisimilis as a human pathogen motivates the analysis of its pathomechanisms. One of the mechanisms that increases infectivity and dissemination of several streptococcal species is the recruitment and subsequent activation of host plasminogen on the streptococcal surface. This study identified GCS3 as a novel plasminogen-binding M protein of S. dysgalactiae ssp. equisimilis and revealed a difference in the mode of binding as compared to the plasminogen-binding protein PAM of S. pyogenes. In contrast to PAM, GCS3 did not bind to the kringle 1-3 region of plasminogen. Despite this difference, GCS3 exerts the same function of recruiting plasminogen to the streptococcal surface, which can be activated by streptokinase and host plasminogen activators to serve as a spreading factor. Moreover, we demonstrate a role of GCS3 in plasminogen-dependent streptococcal adherence to human pharyngeal cells (cell line Detroit 562) that indicates an additional function of the protein as an adhesin in the oral cavity.
en
Adhesins, Bacterial
Bacterial Adhesion
Bacterial Proteins
Carrier Proteins
Cell Line
Epithelial Cells
Humans
Plasminogen
Streptococcus
Virulence Factors
Biological functions of GCS3, a novel plasminogen-binding protein of Streptococcus dysgalactiae ssp. equisimilis.
Article
2018-06-13T01:05:37Z
Increasing awareness of the relevance of Streptococcus dysgalactiae ssp. equisimilis as a human pathogen motivates the analysis of its pathomechanisms. One of the mechanisms that increases infectivity and dissemination of several streptococcal species is the recruitment and subsequent activation of host plasminogen on the streptococcal surface. This study identified GCS3 as a novel plasminogen-binding M protein of S. dysgalactiae ssp. equisimilis and revealed a difference in the mode of binding as compared to the plasminogen-binding protein PAM of S. pyogenes. In contrast to PAM, GCS3 did not bind to the kringle 1-3 region of plasminogen. Despite this difference, GCS3 exerts the same function of recruiting plasminogen to the streptococcal surface, which can be activated by streptokinase and host plasminogen activators to serve as a spreading factor. Moreover, we demonstrate a role of GCS3 in plasminogen-dependent streptococcal adherence to human pharyngeal cells (cell line Detroit 562) that indicates an additional function of the protein as an adhesin in the oral cavity.
ORIGINAL
Bergmann et al_final.pdf
Bergmann et al_final.pdf
original manuscript
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Figs_Bergmann.pdf
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figures to manuscript
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CC-LICENSE
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LICENSE
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THUMBNAIL
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TEXT
Bergmann et al_final.pdf.txt
Bergmann et al_final.pdf.txt
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Figs_Bergmann.pdf.txt
Extracted Text
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10033/139689
oai:hzi.openrepository.com:10033/139689
2019-08-30 11:25:43.518
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/1420102019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Marjenberg, Zoe R
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500
Ellis, Ian R
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500
Hagan, Robert M
103440582da80d8b06ce321343071977
500
Prabhakaran, Sabitha
58180d4fc133cce559c0cdb201502c5a
500
Höök, Magnus
50c95630a5bf8d2e4c4f8455c750849e
500
Talay, Susanne R
5a6000962c21b07f4c6cda30597c0701
500
Potts, Jennifer R
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Staunton, David
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Schwarz-Linek, Ulrich
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Biomedical Sciences Research Complex, University of St. Andrews, St. Andrews KY16 9ST, Scotland, United Kingdom.
2011-09-09T08:48:51Z
2011-09-09T08:48:51Z
2011-01-21
Cooperative binding and activation of fibronectin by a bacterial surface protein. 2011, 286 (3):1884-94 J. Biol. Chem.
1083-351X
21059652
10.1074/jbc.M110.183053
http://hdl.handle.net/10033/142010
The Journal of biological chemistry
Integrin-dependent cell invasion of some pathogenic bacteria is mediated by surface proteins targeting the extracellular matrix protein fibronectin (FN). Although the structural basis for bacterial FN recognition is well understood, it has been unclear why proteins such as streptococcal SfbI contain several FN-binding sites. We used microcalorimetry to reveal cooperative binding of FN fragments to arrays of binding sites in SfbI. In combination with thermodynamic analyses, functional cell-based assays show that SfbI induces conformational changes in the N-terminal 100-kDa region of FN (FN100kDa), most likely by competition with intramolecular interactions defining an inactive state of FN100kDa. This study provides insights into how long range conformational changes resulting in FN activation may be triggered by bacterial pathogens.
en
Adhesins, Bacterial
Binding Sites
Cells, Cultured
Fibroblasts
Fibronectins
Humans
Protein Binding
Streptococcus pyogenes
Cooperative binding and activation of fibronectin by a bacterial surface protein.
Article
2018-06-12T22:16:51Z
Integrin-dependent cell invasion of some pathogenic bacteria is mediated by surface proteins targeting the extracellular matrix protein fibronectin (FN). Although the structural basis for bacterial FN recognition is well understood, it has been unclear why proteins such as streptococcal SfbI contain several FN-binding sites. We used microcalorimetry to reveal cooperative binding of FN fragments to arrays of binding sites in SfbI. In combination with thermodynamic analyses, functional cell-based assays show that SfbI induces conformational changes in the N-terminal 100-kDa region of FN (FN100kDa), most likely by competition with intramolecular interactions defining an inactive state of FN100kDa. This study provides insights into how long range conformational changes resulting in FN activation may be triggered by bacterial pathogens.
ORIGINAL
Marjenberg et al_final.pdf
Marjenberg et al_final.pdf
original manuscript
application/pdf
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CC-LICENSE
license_url
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LICENSE
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THUMBNAIL
Marjenberg et al_final.pdf.jpg
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Generated Thumbnail
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TEXT
Marjenberg et al_final.pdf.txt
Marjenberg et al_final.pdf.txt
Extracted Text
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10033/142010
oai:hzi.openrepository.com:10033/142010
2019-08-30 11:37:23.903
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2037292019-08-30T11:32:16Zcom_10033_6815com_10033_6814col_10033_6886
Willenborg, J
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Fulde, M
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de Greeff, A
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Rohde, Manfred
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Smith, H E
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Valentin-Weigand, P
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Goethe, R
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Institute for Microbiology, University of Veterinary Medicine, Hannover, Germany.
2012-01-19T14:34:52Z
2012-01-19T14:34:52Z
2011-06
Role of glucose and CcpA in capsule expression and virulence of Streptococcus suis. 2011, 157 (Pt 6):1823-33 Microbiology (Reading, Engl.)
1465-2080
21349980
10.1099/mic.0.046417-0
http://hdl.handle.net/10033/203729
Microbiology (Reading, England)
Streptococcus suis is one of the most important pathogens in pigs and is also an emerging zoonotic agent. After crossing the epithelial barrier, S. suis causes bacteraemia, resulting in meningitis, endocarditis and bronchopneumonia. Since the host environment seems to be an important regulatory component for virulence, we related expression of virulence determinants of S. suis to glucose availability during growth and to the sugar metabolism regulator catabolite control protein A (CcpA). We found that expression of the virulence-associated genes arcB, representing arcABC operon expression, cps2A, representing capsular locus expression, as well as sly, ofs, sao and epf, differed significantly between exponential and early stationary growth of a highly virulent serotype 2 strain. Deletion of ccpA altered the expression of the surface-associated virulence factors arcB, sao and eno, as well as the two currently proven virulence factors in pigs, ofs and cps2A, in early exponential growth. Global expression analysis using a cDNA expression array revealed 259 differentially expressed genes in early exponential growth, of which 141 were more highly expressed in the CcpA mutant strain 10ΔccpA and 118 were expressed to a lower extent. Interestingly, among the latter genes, 18 could be related to capsule and cell wall synthesis. Correspondingly, electron microscopy characterization of strain 10ΔccpA revealed a markedly reduced thickness of the capsule. This phenotype correlated with enhanced binding to porcine plasma proteins and a reduced resistance to killing by porcine neutrophils. Taken together, our data demonstrate that CcpA has a significant effect on the capsule synthesis and virulence properties of S. suis.
en
Animals
Bacterial Capsules
Bacterial Proteins
DNA, Complementary
Gene Expression Profiling
Gene Expression Regulation, Bacterial
Glucose
Mutation
Oligonucleotide Array Sequence Analysis
Repressor Proteins
Streptococcus suis
Swine
Virulence
Virulence Factors
Role of glucose and CcpA in capsule expression and virulence of Streptococcus suis.
Article
2012-06-15T00:00:00Z
Streptococcus suis is one of the most important pathogens in pigs and is also an emerging zoonotic agent. After crossing the epithelial barrier, S. suis causes bacteraemia, resulting in meningitis, endocarditis and bronchopneumonia. Since the host environment seems to be an important regulatory component for virulence, we related expression of virulence determinants of S. suis to glucose availability during growth and to the sugar metabolism regulator catabolite control protein A (CcpA). We found that expression of the virulence-associated genes arcB, representing arcABC operon expression, cps2A, representing capsular locus expression, as well as sly, ofs, sao and epf, differed significantly between exponential and early stationary growth of a highly virulent serotype 2 strain. Deletion of ccpA altered the expression of the surface-associated virulence factors arcB, sao and eno, as well as the two currently proven virulence factors in pigs, ofs and cps2A, in early exponential growth. Global expression analysis using a cDNA expression array revealed 259 differentially expressed genes in early exponential growth, of which 141 were more highly expressed in the CcpA mutant strain 10ΔccpA and 118 were expressed to a lower extent. Interestingly, among the latter genes, 18 could be related to capsule and cell wall synthesis. Correspondingly, electron microscopy characterization of strain 10ΔccpA revealed a markedly reduced thickness of the capsule. This phenotype correlated with enhanced binding to porcine plasma proteins and a reduced resistance to killing by porcine neutrophils. Taken together, our data demonstrate that CcpA has a significant effect on the capsule synthesis and virulence properties of S. suis.
ORIGINAL
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2019-08-30 11:32:16.879
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2105692019-08-30T11:32:17Zcom_10033_6815com_10033_6814col_10033_6886
Rato, Márcia G
dafebfacf45016a0a2fefb35d995e749
500
Nerlich, Andreas
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500
Bergmann, René
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500
Bexiga, Ricardo
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500
Nunes, Sandro F
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500
Vilela, Cristina L
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500
Santos-Sanches, Ilda
e9117f3c5400c0a2002b582184c59f4c
500
Chhatwal, Gursharan S
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Centro de Recursos Microbiológicos, Departamento de Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal.
2012-02-13T09:47:17Z
2012-02-13T09:47:17Z
2011-07
Virulence gene pool detected in bovine group C Streptococcus dysgalactiae subsp. dysgalactiae isolates by use of a group A S. pyogenes virulence microarray. 2011, 49 (7):2470-9 J. Clin. Microbiol.
1098-660X
21525223
10.1128/JCM.00008-11
http://hdl.handle.net/10033/210569
Journal of clinical microbiology
A custom-designed microarray containing 220 virulence genes of Streptococcus pyogenes (group A Streptococcus [GAS]) was used to test group C Streptococcus dysgalactiae subsp. dysgalactiae (GCS) field strains causing bovine mastitis and group C or group G Streptococcus dysgalactiae subsp. equisimilis (GCS/GGS) isolates from human infections, with the latter being used for comparative purposes, for the presence of virulence genes. All bovine and all human isolates carried a fraction of the 220 genes (23% and 39%, respectively). The virulence genes encoding streptolysin S, glyceraldehyde-3-phosphate dehydrogenase, the plasminogen-binding M-like protein PAM, and the collagen-like protein SclB were detected in the majority of both bovine and human isolates (94 to 100%). Virulence factors, usually carried by human beta-hemolytic streptococcal pathogens, such as streptokinase, laminin-binding protein, and the C5a peptidase precursor, were detected in all human isolates but not in bovine isolates. Additionally, GAS bacteriophage-associated virulence genes encoding superantigens, DNase, and/or streptodornase were detected in bovine isolates (72%) but not in the human isolates. Determinants located in non-bacteriophage-related mobile elements, such as the gene encoding R28, were detected in all bovine and human isolates. Several virulence genes, including genes of bacteriophage origin, were shown to be expressed by reverse transcriptase PCR (RT-PCR). Phylogenetic analysis of superantigen gene sequences revealed a high level (>98%) of identity among genes of bovine GCS, of the horse pathogen Streptococcus equi subsp. equi, and of the human pathogen GAS. Our findings indicate that alpha-hemolytic bovine GCS, an important mastitis pathogen and considered to be a nonhuman pathogen, carries important virulence factors responsible for virulence and pathogenesis in humans.
en
Animals
Bacterial Proteins
Cattle
DNA, Bacterial
Gene Expression Profiling
Gene Pool
Humans
Interspersed Repetitive Sequences
Microarray Analysis
Molecular Sequence Data
Reverse Transcriptase Polymerase Chain Reaction
Sequence Analysis, DNA
Streptococcal Infections
Streptococcus
Streptococcus Phages
Streptococcus pyogenes
Virulence Factors
Virulence gene pool detected in bovine group C Streptococcus dysgalactiae subsp. dysgalactiae isolates by use of a group A S. pyogenes virulence microarray.
Article
2018-06-13T17:00:15Z
A custom-designed microarray containing 220 virulence genes of Streptococcus pyogenes (group A Streptococcus [GAS]) was used to test group C Streptococcus dysgalactiae subsp. dysgalactiae (GCS) field strains causing bovine mastitis and group C or group G Streptococcus dysgalactiae subsp. equisimilis (GCS/GGS) isolates from human infections, with the latter being used for comparative purposes, for the presence of virulence genes. All bovine and all human isolates carried a fraction of the 220 genes (23% and 39%, respectively). The virulence genes encoding streptolysin S, glyceraldehyde-3-phosphate dehydrogenase, the plasminogen-binding M-like protein PAM, and the collagen-like protein SclB were detected in the majority of both bovine and human isolates (94 to 100%). Virulence factors, usually carried by human beta-hemolytic streptococcal pathogens, such as streptokinase, laminin-binding protein, and the C5a peptidase precursor, were detected in all human isolates but not in bovine isolates. Additionally, GAS bacteriophage-associated virulence genes encoding superantigens, DNase, and/or streptodornase were detected in bovine isolates (72%) but not in the human isolates. Determinants located in non-bacteriophage-related mobile elements, such as the gene encoding R28, were detected in all bovine and human isolates. Several virulence genes, including genes of bacteriophage origin, were shown to be expressed by reverse transcriptase PCR (RT-PCR). Phylogenetic analysis of superantigen gene sequences revealed a high level (>98%) of identity among genes of bovine GCS, of the horse pathogen Streptococcus equi subsp. equi, and of the human pathogen GAS. Our findings indicate that alpha-hemolytic bovine GCS, an important mastitis pathogen and considered to be a nonhuman pathogen, carries important virulence factors responsible for virulence and pathogenesis in humans.
ORIGINAL
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Rato et al_final.pdf
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2135712019-08-30T11:26:13Zcom_10033_6815com_10033_6814col_10033_6886
Amelung, Silva
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Nerlich, Andreas
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Rohde, Manfred
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Spellerberg, Barbara
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Cole, Jason N
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Nizet, Victor
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Chhatwal, Gursharan S
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Talay, Susanne R
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Department of Medical Microbiology, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
2012-02-29T13:58:03Z
2012-02-29T13:58:03Z
2011-08
The FbaB-type fibronectin-binding protein of Streptococcus pyogenes promotes specific invasion into endothelial cells. 2011, 13 (8):1200-11 Cell. Microbiol.
1462-5822
21615663
10.1111/j.1462-5822.2011.01610.x
http://hdl.handle.net/10033/213571
Cellular microbiology
Invasive serotype M3 Streptococcus pyogenes are among the most frequently isolated organisms from patients suffering from invasive streptococcal disease and have the potential to invade primary human endothelial cells (EC) via a rapid and efficient mechanism. FbaB protein, the fibronectin-binding protein expressed by M3 S. pyogenes, was herein identified as a potent invasin for EC. By combining heterologous gene expression with allelic replacement, we demonstrate that FbaB is essential and sufficient to trigger EC invasion via a Rac1-dependent phagocytosis-like uptake. FbaB-mediated uptake follows the classical endocytic pathway with lysosomal destination. FbaB is demonstrated to be a streptococcal invasin exhibiting EC tropism. FbaB thus initiates a process that may contribute to the deep tissue tropism and spread of invasive S. pyogenes isolates into the vascular EC lining.
en
Adhesins, Bacterial
Carrier Proteins
Cells, Cultured
Endocytosis
Endothelial Cells
Fibronectins
Host-Pathogen Interactions
Humans
Streptococcus pyogenes
Virulence Factors
rac1 GTP-Binding Protein
The FbaB-type fibronectin-binding protein of Streptococcus pyogenes promotes specific invasion into endothelial cells.
Article
2012-08-15T00:00:00Z
Invasive serotype M3 Streptococcus pyogenes are among the most frequently isolated organisms from patients suffering from invasive streptococcal disease and have the potential to invade primary human endothelial cells (EC) via a rapid and efficient mechanism. FbaB protein, the fibronectin-binding protein expressed by M3 S. pyogenes, was herein identified as a potent invasin for EC. By combining heterologous gene expression with allelic replacement, we demonstrate that FbaB is essential and sufficient to trigger EC invasion via a Rac1-dependent phagocytosis-like uptake. FbaB-mediated uptake follows the classical endocytic pathway with lysosomal destination. FbaB is demonstrated to be a streptococcal invasin exhibiting EC tropism. FbaB thus initiates a process that may contribute to the deep tissue tropism and spread of invasive S. pyogenes isolates into the vascular EC lining.
ORIGINAL
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2019-08-30 11:26:13.435
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2148502019-08-30T11:27:46Zcom_10033_6815com_10033_6814col_10033_6886
Härtel, Tobias
01446d585e54cd439ae7c9fd93f89260
500
Klein, Matthias
efa060cae141c78423b91ee109815263
500
Koedel, Uwe
97fd470e75c744a16f92674be6576416
500
Rohde, Manfred
9d59d6cfa4e7b93322b57bce461b1a4f
500
Petruschka, Lothar
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Hammerschmidt, Sven
721efda1f965cd4be1552565a54d8b5b
500
Department of Genetics of Microorganisms, Interfaculty Institute for Genetics and Functional Genomics, Ernst Moritz Arndt Universität Greifswald, Friedrich-Ludwig-Jahn-Str. 15a, D-17487 Greifswald, Germany.
2012-03-08T14:59:12Z
2012-03-08T14:59:12Z
2011-01
Impact of glutamine transporters on pneumococcal fitness under infection-related conditions. 2011, 79 (1):44-58 Infect. Immun.
1098-5522
21078855
10.1128/IAI.00855-10
http://hdl.handle.net/10033/214850
Infection and immunity
The genomic analysis of Streptococcus pneumoniae predicted six putative glutamine uptake systems, which are expressed under in vitro conditions, as shown here by reverse transcription-PCR. Four of these operons consist of glnHPQ, while two lack glnH, which encodes a soluble glutamine-binding protein. Here, we studied the impact of two of these glutamine ATP-binding cassette transporters on S. pneumoniae D39 virulence and phagocytosis, which consist of GlnQ and a translationally fused protein of GlnH and GlnP. Mice infected intranasally with D39Δgln0411/0412 showed significantly increased survival times and a significant delay in the development of pneumococcal pneumonia compared to those infected with D39, as observed in real time using bioluminescent pneumococci. In a mouse sepsis model, the mutant D39Δgln0411/0412 showed only moderate but significant attenuation. In contrast, the D39Δgln1098/1099 knockout strain was massively attenuated in the pneumonia and septicemia mouse infection model. To cause pneumonia or sepsis with D39Δgln1098/1099, infection doses 100- to 10,000-fold higher than those used for wild-type strain D39 were required. In an experimental mouse meningitis model, D39Δgln1098/1099 produced decreased levels of white blood cells in cerebrospinal fluid and showed decreased numbers of bacteria in the bloodstream compared to D39 and D39Δgln0411/0412. Phagocytosis experiments revealed significantly decreased intracellular survival rates of mutants D39Δgln1098/1099 and D39Δgln0411/0412 compared to wild-type D39, suggesting that the deficiency of Gln uptake systems impairs resistance to oxidative stress. Taken together, our results demonstrate that both glutamine uptake systems are required for full virulence of pneumococci but exhibit different impacts on the pathogenesis of pneumococci under in vivo conditions.
en
Archived with thanks to Infection and immunity
Animals
Bacterial Proteins
Carrier Proteins
Cell Line
Computational Biology
Gene Expression Regulation, Bacterial
Meningitis, Bacterial
Mice
Mutation
Pneumococcal Infections
Streptococcus pneumoniae
Impact of glutamine transporters on pneumococcal fitness under infection-related conditions.
Article
2018-06-13T03:41:57Z
The genomic analysis of Streptococcus pneumoniae predicted six putative glutamine uptake systems, which are expressed under in vitro conditions, as shown here by reverse transcription-PCR. Four of these operons consist of glnHPQ, while two lack glnH, which encodes a soluble glutamine-binding protein. Here, we studied the impact of two of these glutamine ATP-binding cassette transporters on S. pneumoniae D39 virulence and phagocytosis, which consist of GlnQ and a translationally fused protein of GlnH and GlnP. Mice infected intranasally with D39Δgln0411/0412 showed significantly increased survival times and a significant delay in the development of pneumococcal pneumonia compared to those infected with D39, as observed in real time using bioluminescent pneumococci. In a mouse sepsis model, the mutant D39Δgln0411/0412 showed only moderate but significant attenuation. In contrast, the D39Δgln1098/1099 knockout strain was massively attenuated in the pneumonia and septicemia mouse infection model. To cause pneumonia or sepsis with D39Δgln1098/1099, infection doses 100- to 10,000-fold higher than those used for wild-type strain D39 were required. In an experimental mouse meningitis model, D39Δgln1098/1099 produced decreased levels of white blood cells in cerebrospinal fluid and showed decreased numbers of bacteria in the bloodstream compared to D39 and D39Δgln0411/0412. Phagocytosis experiments revealed significantly decreased intracellular survival rates of mutants D39Δgln1098/1099 and D39Δgln0411/0412 compared to wild-type D39, suggesting that the deficiency of Gln uptake systems impairs resistance to oxidative stress. Taken together, our results demonstrate that both glutamine uptake systems are required for full virulence of pneumococci but exhibit different impacts on the pathogenesis of pneumococci under in vivo conditions.
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ORIGINAL
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Helmholtz Zentrum für Infektionsforschung Repository
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2012-03-22T10:33:56Z
2012-03-22T10:33:56Z
2011
Complete genome sequence of Bacteroides helcogenes type strain (P 36-108). 2011, 4 (1):45-53 Stand Genomic Sci
1944-3277
21475586
10.4056/sigs.1513795
http://hdl.handle.net/10033/216249
Standards in genomic sciences
Bacteroides helcogenes Benno et al. 1983 is of interest because of its isolated phylogenetic location and, although it has been found in pig feces and is known to be pathogenic for pigs, occurrence of this bacterium is rare and it does not cause significant damage in intensive animal husbandry. The genome of B. helcogenes P 36-108(T) is already the fifth completed and published type strain genome from the genus Bacteroides in the family Bacteroidaceae. The 3,998,906 bp long genome with its 3,353 protein-coding and 83 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Bacteroides helcogenes type strain (P 36-108).
Article
2018-06-12T21:57:02Z
Bacteroides helcogenes Benno et al. 1983 is of interest because of its isolated phylogenetic location and, although it has been found in pig feces and is known to be pathogenic for pigs, occurrence of this bacterium is rare and it does not cause significant damage in intensive animal husbandry. The genome of B. helcogenes P 36-108(T) is already the fifth completed and published type strain genome from the genus Bacteroides in the family Bacteroidaceae. The 3,998,906 bp long genome with its 3,353 protein-coding and 83 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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pati et al_final.pdf
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2019-08-30 11:25:11.147
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-03-22T12:18:30Z
2012-03-22T12:18:30Z
2011
Complete genome sequence of Calditerrivibrio nitroreducens type strain (Yu37-1). 2011, 4 (1):54-62 Stand Genomic Sci
1944-3277
21475587
10.4056/sigs.1523807
http://hdl.handle.net/10033/216269
Standards in genomic sciences
Calditerrivibrio nitroreducens Iino et al. 2008 is the type species of the genus Calditerrivibrio. The species is of interest because of its important role in the nitrate cycle as nitrate reducer and for its isolated phylogenetic position in the Tree of Life. Here we describe the features of this organism, together with the complete genome sequence and annotation. This is the third complete genome sequence of a member of the family Deferribacteraceae. The 2,216,552 bp long genome with its 2,128 protein-coding and 50 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Calditerrivibrio nitroreducens type strain (Yu37-1).
Article
2018-06-12T22:06:56Z
Calditerrivibrio nitroreducens Iino et al. 2008 is the type species of the genus Calditerrivibrio. The species is of interest because of its important role in the nitrate cycle as nitrate reducer and for its isolated phylogenetic position in the Tree of Life. Here we describe the features of this organism, together with the complete genome sequence and annotation. This is the third complete genome sequence of a member of the family Deferribacteraceae. The 2,216,552 bp long genome with its 2,128 protein-coding and 50 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
pitluck at al_final.pdf
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Open Access publication
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oai:hzi.openrepository.com:10033/216269
2019-08-30 11:26:13.019
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-03-29T09:00:44Z
2012-03-29T09:00:44Z
2011-07-01
Complete genome sequence of Haliscomenobacter hydrossis type strain (O). 2011, 4 (3):352-60 Stand Genomic Sci
1944-3277
21886862
10.4056/sigs.1964579
http://hdl.handle.net/10033/216990
Standards in genomic sciences
Haliscomenobacter hydrossis van Veen et al. 1973 is the type species of the genus Haliscomenobacter, which belongs to order "Sphingobacteriales". The species is of interest because of its isolated phylogenetic location in the tree of life, especially the so far genomically uncharted part of it, and because the organism grows in a thin, hardly visible hyaline sheath. Members of the species were isolated from fresh water of lakes and from ditch water. The genome of H. hydrossis is the first completed genome sequence reported from a member of the family "Saprospiraceae". The 8,771,651 bp long genome with its three plasmids of 92 kbp, 144 kbp and 164 kbp length contains 6,848 protein-coding and 60 RNA genes, and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Haliscomenobacter hydrossis type strain (O).
Article
2018-06-12T22:51:25Z
Haliscomenobacter hydrossis van Veen et al. 1973 is the type species of the genus Haliscomenobacter, which belongs to order "Sphingobacteriales". The species is of interest because of its isolated phylogenetic location in the tree of life, especially the so far genomically uncharted part of it, and because the organism grows in a thin, hardly visible hyaline sheath. Members of the species were isolated from fresh water of lakes and from ditch water. The genome of H. hydrossis is the first completed genome sequence reported from a member of the family "Saprospiraceae". The 8,771,651 bp long genome with its three plasmids of 92 kbp, 144 kbp and 164 kbp length contains 6,848 protein-coding and 60 RNA genes, and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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2019-08-30 11:25:11.363
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-03-29T09:19:29Z
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2011
Complete genome sequence of Leadbetterella byssophila type strain (4M15). 2011, 4 (1):2-12 Stand Genomic Sci
1944-3277
21475582
10.4056/sigs.1413518
http://hdl.handle.net/10033/216992
Standards in genomic sciences
Leadbetterella byssophila Weon et al. 2005 is the type species of the genus Leadbetterella of the family Cytophagaceae in the phylum Bacteroidetes. Members of the phylum Bacteroidetes are widely distributed in nature, especially in aquatic environments. They are of special interest for their ability to degrade complex biopolymers. L. byssophila occupies a rather isolated position in the tree of life and is characterized by its ability to hydrolyze starch and gelatine, but not agar, cellulose or chitin. Here we describe the features of this organism, together with the complete genome sequence, and annotation. L. byssophila is already the 16(th) member of the family Cytophagaceae whose genome has been sequenced. The 4,059,653 bp long single replicon genome with its 3,613 protein-coding and 53 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Leadbetterella byssophila type strain (4M15).
Article
2018-06-12T22:09:18Z
Leadbetterella byssophila Weon et al. 2005 is the type species of the genus Leadbetterella of the family Cytophagaceae in the phylum Bacteroidetes. Members of the phylum Bacteroidetes are widely distributed in nature, especially in aquatic environments. They are of special interest for their ability to degrade complex biopolymers. L. byssophila occupies a rather isolated position in the tree of life and is characterized by its ability to hydrolyze starch and gelatine, but not agar, cellulose or chitin. Here we describe the features of this organism, together with the complete genome sequence, and annotation. L. byssophila is already the 16(th) member of the family Cytophagaceae whose genome has been sequenced. The 4,059,653 bp long single replicon genome with its 3,613 protein-coding and 53 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
abt et al_final.pdf
abt et al_final.pdf
Open Access publication
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https://hzi.openrepository.com/bitstream/10033/216992/1/abt%20et%20al_final.pdf
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10033/216992
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2019-08-30 11:25:11.353
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-03-29T10:15:30Z
2012-03-29T10:15:30Z
2011-07-01
Complete genome sequence of Mahella australiensis type strain (50-1 BON). 2011, 4 (3):331-41 Stand Genomic Sci
1944-3277
21886860
10.4056/sigs.1864526
http://hdl.handle.net/10033/216993
Standards in genomic sciences
Mahella australiensis Bonilla Salinas et al. 2004 is the type species of the genus Mahella, which belongs to the family Thermoanaerobacteraceae. The species is of interest because it differs from other known anaerobic spore-forming bacteria in its G+C content, and in certain phenotypic traits, such as carbon source utilization and relationship to temperature. Moreover, it has been discussed that this species might be an indigenous member of petroleum and oil reservoirs. This is the first completed genome sequence of a member of the genus Mahella and the ninth completed type strain genome sequence from the family Thermoanaerobacteraceae. The 3,135,972 bp long genome with its 2,974 protein-coding and 59 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Mahella australiensis type strain (50-1 BON).
Article
2018-06-12T21:54:36Z
Mahella australiensis Bonilla Salinas et al. 2004 is the type species of the genus Mahella, which belongs to the family Thermoanaerobacteraceae. The species is of interest because it differs from other known anaerobic spore-forming bacteria in its G+C content, and in certain phenotypic traits, such as carbon source utilization and relationship to temperature. Moreover, it has been discussed that this species might be an indigenous member of petroleum and oil reservoirs. This is the first completed genome sequence of a member of the genus Mahella and the ninth completed type strain genome sequence from the family Thermoanaerobacteraceae. The 3,135,972 bp long genome with its 2,974 protein-coding and 59 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2019-08-30 11:25:11.39
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-08-23T07:51:04Z
2012-08-23T07:51:04Z
2011
Complete genome sequence of Weeksella virosa type strain (9751). 2011, 4 (1):81-90 Stand Genomic Sci
1944-3277
21475590
10.4056/sigs.1603927
http://hdl.handle.net/10033/239651
Standards in genomic sciences
Weeksella virosa Holmes et al. 1987 is the sole member and type species of the genus Weeksella which belongs to the family Flavobacteriaceae of the phylum Bacteroidetes. Twenty-nine isolates, collected from clinical specimens provided the basis for the taxon description. While the species seems to be a saprophyte of the mucous membranes of healthy man and warm-blooded animals a causal relationship with disease has been reported in a few instances. Except for the ability to produce indole and to hydrolyze Tween and proteins such as casein and gelatin, this aerobic, non-motile, non-pigmented bacterial species is metabolically inert in most traditional biochemical tests. The 2,272,954 bp long genome with its 2,105 protein-coding and 76 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Weeksella virosa type strain (9751).
Article
421347
255385
2018-06-12T18:12:43Z
Weeksella virosa Holmes et al. 1987 is the sole member and type species of the genus Weeksella which belongs to the family Flavobacteriaceae of the phylum Bacteroidetes. Twenty-nine isolates, collected from clinical specimens provided the basis for the taxon description. While the species seems to be a saprophyte of the mucous membranes of healthy man and warm-blooded animals a causal relationship with disease has been reported in a few instances. Except for the ability to produce indole and to hydrolyze Tween and proteins such as casein and gelatin, this aerobic, non-motile, non-pigmented bacterial species is metabolically inert in most traditional biochemical tests. The 2,272,954 bp long genome with its 2,105 protein-coding and 76 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
TEXT
lang et al_final.pdf.txt
lang et al_final.pdf.txt
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THUMBNAIL
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ORIGINAL
lang et al_final.pdf
lang et al_final.pdf
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Complete genome sequence of Desulfobulbus propionicus type strain (1pr3). 2011, 4 (1):100-10 Stand Genomic Sci
1944-3277
21475592
10.4056/sigs.1613929
http://hdl.handle.net/10033/216989
Standards in genomic sciences
Desulfobulbus propionicus Widdel 1981 is the type species of the genus Desulfobulbus, which belongs to the family Desulfobulbaceae. The species is of interest because of its great implication in the sulfur cycle in aquatic sediments, its large substrate spectrum and a broad versatility in using various fermentation pathways. The species was the first example of a pure culture known to disproportionate elemental sulfur to sulfate and sulfide. This is the first completed genome sequence of a member of the genus Desulfobulbus and the third published genome sequence from a member of the family Desulfobulbaceae. The 3,851,869 bp long genome with its 3,351 protein-coding and 57 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Desulfobulbus propionicus type strain (1pr3).
Article
2018-06-12T17:47:18Z
Desulfobulbus propionicus Widdel 1981 is the type species of the genus Desulfobulbus, which belongs to the family Desulfobulbaceae. The species is of interest because of its great implication in the sulfur cycle in aquatic sediments, its large substrate spectrum and a broad versatility in using various fermentation pathways. The species was the first example of a pure culture known to disproportionate elemental sulfur to sulfate and sulfide. This is the first completed genome sequence of a member of the genus Desulfobulbus and the third published genome sequence from a member of the family Desulfobulbaceae. The 3,851,869 bp long genome with its 3,351 protein-coding and 57 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2011
Complete genome sequence of Paludibacter propionicigenes type strain (WB4). 2011, 4 (1):36-44 Stand Genomic Sci
1944-3277
21475585
10.4056/sigs.1503846
http://hdl.handle.net/10033/216996
Standards in genomic sciences
Paludibacter propionicigenes Ueki et al. 2006 is the type species of the genus Paludibacter, which belongs to the family Porphyromonadaceae. The species is of interest because of the position it occupies in the tree of life where it can be found in close proximity to members of the genus Dysgonomonas. This is the first completed genome sequence of a member of the genus Paludibacter and the third sequence from the family Porphyromonadaceae. The 3,685,504 bp long genome with its 3,054 protein-coding and 64 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Paludibacter propionicigenes type strain (WB4).
Article
2018-06-13T14:16:37Z
Paludibacter propionicigenes Ueki et al. 2006 is the type species of the genus Paludibacter, which belongs to the family Porphyromonadaceae. The species is of interest because of the position it occupies in the tree of life where it can be found in close proximity to members of the genus Dysgonomonas. This is the first completed genome sequence of a member of the genus Paludibacter and the third sequence from the family Porphyromonadaceae. The 3,685,504 bp long genome with its 3,054 protein-coding and 64 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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2012-03-29T10:40:47Z
2011-07-01
Complete genome sequence of Nitratifractor salsuginis type strain (E9I37-1). 2011, 4 (3):322-30 Stand Genomic Sci
1944-3277
21886859
10.4056/sigs.1844518
http://hdl.handle.net/10033/217009
Standards in genomic sciences
Nitratifractor salsuginis Nakagawa et al. 2005 is the type species of the genus Nitratifractor, a member of the family Nautiliaceae. The species is of interest because of its high capacity for nitrate reduction via conversion to N(2) through respiration, which is a key compound in plant nutrition. The strain is also of interest because it represents the first mesophilic and facultatively anaerobic member of the Epsilonproteobacteria reported to grow on molecular hydrogen. This is the first completed genome sequence of a member of the genus Nitratifractor and the second sequence from the family Nautiliaceae. The 2,101,285 bp long genome with its 2,121 protein-coding and 54 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Nitratifractor salsuginis type strain (E9I37-1).
Article
2018-06-13T01:20:04Z
Nitratifractor salsuginis Nakagawa et al. 2005 is the type species of the genus Nitratifractor, a member of the family Nautiliaceae. The species is of interest because of its high capacity for nitrate reduction via conversion to N(2) through respiration, which is a key compound in plant nutrition. The strain is also of interest because it represents the first mesophilic and facultatively anaerobic member of the Epsilonproteobacteria reported to grow on molecular hydrogen. This is the first completed genome sequence of a member of the genus Nitratifractor and the second sequence from the family Nautiliaceae. The 2,101,285 bp long genome with its 2,121 protein-coding and 54 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2012-03-29T11:44:32Z
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2011-07-01
Complete genome sequence of Syntrophobotulus glycolicus type strain (FlGlyR). 2011, 4 (3):371-80 Stand Genomic Sci
1944-3277
21886864
10.4056/sigs.2004684
http://hdl.handle.net/10033/217010
Standards in genomic sciences
Syntrophobotulus glycolicus Friedrich et al. 1996 is currently the only member of the genus Syntrophobotulus within the family Peptococcaceae. The species is of interest because of its isolated phylogenetic location in the genome-sequenced fraction of tree of life. When grown in pure culture with glyoxylate as carbon source the organism utilizes glyoxylate through fermentative oxidation, whereas, when grown in syntrophic co-culture with homoacetogenic or methanogenic bacteria, it is able to oxidize glycolate to carbon dioxide and hydrogen. No other organic or inorganic carbon source is utilized by S. glycolicus. The subdivision of the family Peptococcaceae into genera does not reflect the natural relationships, particularly regarding the genera most closely related to Syntrophobotulus. Both Desulfotomaculum and Pelotomaculum are paraphyletic assemblages, and the taxonomic classification is in significant conflict with the 16S rRNA data. S. glycolicus is already the ninth member of the family Peptococcaceae with a completely sequenced and publicly available genome. The 3,406,739 bp long genome with its 3,370 protein-coding and 69 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Syntrophobotulus glycolicus type strain (FlGlyR).
Article
2018-06-12T18:11:01Z
Syntrophobotulus glycolicus Friedrich et al. 1996 is currently the only member of the genus Syntrophobotulus within the family Peptococcaceae. The species is of interest because of its isolated phylogenetic location in the genome-sequenced fraction of tree of life. When grown in pure culture with glyoxylate as carbon source the organism utilizes glyoxylate through fermentative oxidation, whereas, when grown in syntrophic co-culture with homoacetogenic or methanogenic bacteria, it is able to oxidize glycolate to carbon dioxide and hydrogen. No other organic or inorganic carbon source is utilized by S. glycolicus. The subdivision of the family Peptococcaceae into genera does not reflect the natural relationships, particularly regarding the genera most closely related to Syntrophobotulus. Both Desulfotomaculum and Pelotomaculum are paraphyletic assemblages, and the taxonomic classification is in significant conflict with the 16S rRNA data. S. glycolicus is already the ninth member of the family Peptococcaceae with a completely sequenced and publicly available genome. The 3,406,739 bp long genome with its 3,370 protein-coding and 69 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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2012-04-26T09:17:45Z
2012-04-26T09:17:45Z
2011-07-01
Complete genome sequence of the acetate-degrading sulfate reducer Desulfobacca acetoxidans type strain (ASRB2). 2011, 4 (3):393-401 Stand Genomic Sci
1944-3277
21886866
10.4056/sigs.2064705
http://hdl.handle.net/10033/220751
Standards in genomic sciences
Desulfobacca acetoxidans Elferink et al. 1999 is the type species of the genus Desulfobacca, which belongs to the family Syntrophaceae in the class Deltaproteobacteria. The species was first observed in a study on the competition of sulfate-reducers and acetoclastic methanogens for acetate in sludge. D. acetoxidans is considered to be the most abundant acetate-degrading sulfate reducer in sludge. It is of interest due to its isolated phylogenetic location in the 16S rRNA-based tree of life. This is the second completed genome sequence of a member of the family Syntrophaceae to be published and only the third genome sequence from a member of the order Syntrophobacterales. The 3,282,536 bp long genome with its 2,969 protein-coding and 54 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the acetate-degrading sulfate reducer Desulfobacca acetoxidans type strain (ASRB2).
Article
2018-06-13T21:36:21Z
Desulfobacca acetoxidans Elferink et al. 1999 is the type species of the genus Desulfobacca, which belongs to the family Syntrophaceae in the class Deltaproteobacteria. The species was first observed in a study on the competition of sulfate-reducers and acetoclastic methanogens for acetate in sludge. D. acetoxidans is considered to be the most abundant acetate-degrading sulfate reducer in sludge. It is of interest due to its isolated phylogenetic location in the 16S rRNA-based tree of life. This is the second completed genome sequence of a member of the family Syntrophaceae to be published and only the third genome sequence from a member of the order Syntrophobacterales. The 3,282,536 bp long genome with its 2,969 protein-coding and 54 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
göker et al_final.pdf
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2012-04-26T09:51:42Z
2012-04-26T09:51:42Z
2011-07-01
Complete genome sequence of the hyperthermophilic chemolithoautotroph Pyrolobus fumarii type strain (1A). 2011, 4 (3):381-92 Stand Genomic Sci
1944-3277
21886865
10.4056/sigs.2014648
http://hdl.handle.net/10033/220753
Standards in genomic sciences
Pyrolobus fumarii Blöchl et al. 1997 is the type species of the genus Pyrolobus, which belongs to the crenarchaeal family Pyrodictiaceae. The species is a facultatively microaerophilic non-motile crenarchaeon. It is of interest because of its isolated phylogenetic location in the tree of life and because it is a hyperthermophilic chemolithoautotroph known as the primary producer of organic matter at deep-sea hydrothermal vents. P. fumarii exhibits currently the highest optimal growth temperature of all life forms on earth (106°C). This is the first completed genome sequence of a member of the genus Pyrolobus to be published and only the second genome sequence from a member of the family Pyrodictiaceae. Although Diversa Corporation announced the completion of sequencing of the P. fumarii genome on September 25, 2001, this sequence was never released to the public. The 1,843,267 bp long genome with its 1,986 protein-coding and 52 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the hyperthermophilic chemolithoautotroph Pyrolobus fumarii type strain (1A).
Article
2018-06-12T20:05:48Z
Pyrolobus fumarii Blöchl et al. 1997 is the type species of the genus Pyrolobus, which belongs to the crenarchaeal family Pyrodictiaceae. The species is a facultatively microaerophilic non-motile crenarchaeon. It is of interest because of its isolated phylogenetic location in the tree of life and because it is a hyperthermophilic chemolithoautotroph known as the primary producer of organic matter at deep-sea hydrothermal vents. P. fumarii exhibits currently the highest optimal growth temperature of all life forms on earth (106°C). This is the first completed genome sequence of a member of the genus Pyrolobus to be published and only the second genome sequence from a member of the family Pyrodictiaceae. Although Diversa Corporation announced the completion of sequencing of the P. fumarii genome on September 25, 2001, this sequence was never released to the public. The 1,843,267 bp long genome with its 1,986 protein-coding and 52 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
anderson-göker et al_final.pdf
anderson-göker et al_final.pdf
Open Access
application/pdf
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2011-07-01
Complete genome sequence of the thermophilic sulfur-reducer Hippea maritima type strain (MH(2)). 2011, 4 (3):303-11 Stand Genomic Sci
1944-3277
21886857
10.4056/sigs.1814460
http://hdl.handle.net/10033/220772
Standards in genomic sciences
Hippea maritima (Miroshnichenko et al. 1999) is the type species of the genus Hippea, which belongs to the family Desulfurellaceae within the class Deltaproteobacteria. The anaerobic, moderately thermophilic marine sulfur-reducer was first isolated from shallow-water hot vents in Matipur Harbor, Papua New Guinea. H. maritima was of interest for genome sequencing because of its isolated phylogenetic location, as a distant next neighbor of the genus Desulfurella. Strain MH(2) (T) is the first type strain from the order Desulfurellales with a completely sequenced genome. The 1,694,430 bp long linear genome with its 1,723 protein-coding and 57 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the thermophilic sulfur-reducer Hippea maritima type strain (MH(2)).
Article
2018-06-12T16:41:42Z
Hippea maritima (Miroshnichenko et al. 1999) is the type species of the genus Hippea, which belongs to the family Desulfurellaceae within the class Deltaproteobacteria. The anaerobic, moderately thermophilic marine sulfur-reducer was first isolated from shallow-water hot vents in Matipur Harbor, Papua New Guinea. H. maritima was of interest for genome sequencing because of its isolated phylogenetic location, as a distant next neighbor of the genus Desulfurella. Strain MH(2) (T) is the first type strain from the order Desulfurellales with a completely sequenced genome. The 1,694,430 bp long linear genome with its 1,723 protein-coding and 57 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2012-05-03T08:39:51Z
2012-05-03T08:39:51Z
2011-07-01
Complete genome sequence of Tsukamurella paurometabola type strain (no. 33). 2011, 4 (3):342-51 Stand Genomic Sci
1944-3277
21886861
10.4056/sigs.1894556
http://hdl.handle.net/10033/221812
Standards in genomic sciences
Tsukamurella paurometabola corrig. (Steinhaus 1941) Collins et al. 1988 is the type species of the genus Tsukamurella, which is the type genus to the family Tsukamurellaceae. The species is not only of interest because of its isolated phylogenetic location, but also because it is a human opportunistic pathogen with some strains of the species reported to cause lung infection, lethal meningitis, and necrotizing tenosynovitis. This is the first completed genome sequence of a member of the genus Tsukamurella and the first genome sequence of a member of the family Tsukamurellaceae. The 4,479,724 bp long genome contains a 99,806 bp long plasmid and a total of 4,335 protein-coding and 56 RNA genes, and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Tsukamurella paurometabola type strain (no. 33).
Article
2018-06-12T22:46:37Z
Tsukamurella paurometabola corrig. (Steinhaus 1941) Collins et al. 1988 is the type species of the genus Tsukamurella, which is the type genus to the family Tsukamurellaceae. The species is not only of interest because of its isolated phylogenetic location, but also because it is a human opportunistic pathogen with some strains of the species reported to cause lung infection, lethal meningitis, and necrotizing tenosynovitis. This is the first completed genome sequence of a member of the genus Tsukamurella and the first genome sequence of a member of the family Tsukamurellaceae. The 4,479,724 bp long genome contains a 99,806 bp long plasmid and a total of 4,335 protein-coding and 56 RNA genes, and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
THUMBNAIL
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2011-07-01
Complete genome sequence of Treponema succinifaciens type strain (6091). 2011, 4 (3):361-70 Stand Genomic Sci
1944-3277
21886863
10.4056/sigs.1984594
http://hdl.handle.net/10033/220776
Standards in genomic sciences
Treponema succinifaciens Cwyk and Canale-Parola 1981 is of interest because this strictly anaerobic, apathogenic member of the genus Treponema oxidizes carbohydrates and couples the Embden-Meyerhof pathway via activity of a pyruvate-formate lyase to the production of acetyl-coenzyme A and formate. This feature separates this species from most other anaerobic spirochetes. The genome of T. succinifaciens 6091(T) is only the second completed and published type strain genome from the genus Treponema in the family Spirochaetaceae. The 2,897,425 bp long genome with one plasmid harbors 2,723 protein-coding and 63 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Treponema succinifaciens type strain (6091).
Article
2018-06-12T22:52:08Z
Treponema succinifaciens Cwyk and Canale-Parola 1981 is of interest because this strictly anaerobic, apathogenic member of the genus Treponema oxidizes carbohydrates and couples the Embden-Meyerhof pathway via activity of a pyruvate-formate lyase to the production of acetyl-coenzyme A and formate. This feature separates this species from most other anaerobic spirochetes. The genome of T. succinifaciens 6091(T) is only the second completed and published type strain genome from the genus Treponema in the family Spirochaetaceae. The 2,897,425 bp long genome with one plasmid harbors 2,723 protein-coding and 63 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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2012-04-26T11:27:49Z
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2011
Complete genome sequence of Truepera radiovictrix type strain (RQ-24). 2011, 4 (1):91-9 Stand Genomic Sci
1944-3277
21475591
10.4056/sigs.1563919
http://hdl.handle.net/10033/220780
Standards in genomic sciences
Truepera radiovictrix Albuquerque et al. 2005 is the type species of the genus Truepera within the phylum "Deinococcus/Thermus". T. radiovictrix is of special interest not only because of its isolated phylogenetic location in the order Deinococcales, but also because of its ability to grow under multiple extreme conditions in alkaline, moderately saline, and high temperature habitats. Of particular interest is the fact that, T. radiovictrix is also remarkably resistant to ionizing radiation, a feature it shares with members of the genus Deinococcus. This is the first completed genome sequence of a member of the family Trueperaceae and the fourth type strain genome sequence from a member of the order Deinococcales. The 3,260,398 bp long genome with its 2,994 protein-coding and 52 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Truepera radiovictrix type strain (RQ-24).
Article
2018-06-12T22:58:09Z
Truepera radiovictrix Albuquerque et al. 2005 is the type species of the genus Truepera within the phylum "Deinococcus/Thermus". T. radiovictrix is of special interest not only because of its isolated phylogenetic location in the order Deinococcales, but also because of its ability to grow under multiple extreme conditions in alkaline, moderately saline, and high temperature habitats. Of particular interest is the fact that, T. radiovictrix is also remarkably resistant to ionizing radiation, a feature it shares with members of the genus Deinococcus. This is the first completed genome sequence of a member of the family Trueperaceae and the fourth type strain genome sequence from a member of the order Deinococcales. The 3,260,398 bp long genome with its 2,994 protein-coding and 52 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
ivanova et al_final.pdf
ivanova et al_final.pdf
Open Access publication
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2010
Complete genome sequence of Acidaminococcus fermentans type strain (VR4). 2010, 3 (1):1-14 Stand Genomic Sci
1944-3277
21304687
10.4056/sigs.1002553
http://hdl.handle.net/10033/225679
Standards in genomic sciences
Acidaminococcus fermentans (Rogosa 1969) is the type species of the genus Acidaminococcus, and is of phylogenetic interest because of its isolated placement in a genomically little characterized region of the Firmicutes. A. fermentans is known for its habitation of the gastrointestinal tract and its ability to oxidize trans-aconitate. Its anaerobic fermentation of glutamate has been intensively studied and will now be complemented by the genomic basis. The strain described in this report is a nonsporulating, nonmotile, Gram-negative coccus, originally isolated from a pig alimentary tract. Here we describe the features of this organism, together with the complete genome sequence, and annotation. This is the first complete genome sequence of a member of the family Acidaminococcaceae, and the 2,329,769 bp long genome with its 2,101 protein-coding and 81 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Acidaminococcus fermentans type strain (VR4).
Article
2018-06-12T23:29:23Z
Acidaminococcus fermentans (Rogosa 1969) is the type species of the genus Acidaminococcus, and is of phylogenetic interest because of its isolated placement in a genomically little characterized region of the Firmicutes. A. fermentans is known for its habitation of the gastrointestinal tract and its ability to oxidize trans-aconitate. Its anaerobic fermentation of glutamate has been intensively studied and will now be complemented by the genomic basis. The strain described in this report is a nonsporulating, nonmotile, Gram-negative coccus, originally isolated from a pig alimentary tract. Here we describe the features of this organism, together with the complete genome sequence, and annotation. This is the first complete genome sequence of a member of the family Acidaminococcaceae, and the 2,329,769 bp long genome with its 2,101 protein-coding and 81 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2010
Complete genome sequence of Acetohalobium arabaticum type strain (Z-7288). 2010, 3 (1):57-65 Stand Genomic Sci
1944-3277
21304692
10.4056/sigs.1062906
http://hdl.handle.net/10033/225674
Standards in genomic sciences
Acetohalobium arabaticum Zhilina and Zavarzin 1990 is of special interest because of its physiology and its participation in the anaerobic C(1)-trophic chain in hypersaline environments. This is the first completed genome sequence of the family Halobacteroidaceae and only the second genome sequence in the order Halanaerobiales. The 2,469,596 bp long genome with its 2,353 protein-coding and 90 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Acetohalobium arabaticum type strain (Z-7288).
Article
2018-06-13T03:45:25Z
Acetohalobium arabaticum Zhilina and Zavarzin 1990 is of special interest because of its physiology and its participation in the anaerobic C(1)-trophic chain in hypersaline environments. This is the first completed genome sequence of the family Halobacteroidaceae and only the second genome sequence in the order Halanaerobiales. The 2,469,596 bp long genome with its 2,353 protein-coding and 90 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
CC-LICENSE
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sikorski-lapidus et al_final.pdf.txt
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10033/225674
oai:hzi.openrepository.com:10033/225674
2019-08-30 11:36:05.241
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-05-31T09:47:12Z
2012-05-31T09:47:12Z
2010
Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1). 2010, 3 (1):66-75 Stand Genomic Sci
1944-3277
21304693
10.4056/sigs.1072907
http://hdl.handle.net/10033/226833
Standards in genomic sciences
Ignisphaera aggregans Niederberger et al. 2006 is the type and sole species of genus Ignisphaera. This archaeal species is characterized by a coccoid-shape and is strictly anaerobic, moderately acidophilic, heterotrophic hyperthermophilic and fermentative. The type strain AQ1.S1(T) was isolated from a near neutral, boiling spring in Kuirau Park, Rotorua, New Zealand. This is the first completed genome sequence of the genus Ignisphaera and the fifth genome (fourth type strain) sequence in the family Desulfurococcaceae. The 1,875,953 bp long genome with its 2,009 protein-coding and 52 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).
Article
2018-06-13T17:04:19Z
Ignisphaera aggregans Niederberger et al. 2006 is the type and sole species of genus Ignisphaera. This archaeal species is characterized by a coccoid-shape and is strictly anaerobic, moderately acidophilic, heterotrophic hyperthermophilic and fermentative. The type strain AQ1.S1(T) was isolated from a near neutral, boiling spring in Kuirau Park, Rotorua, New Zealand. This is the first completed genome sequence of the genus Ignisphaera and the fifth genome (fourth type strain) sequence in the family Desulfurococcaceae. The 1,875,953 bp long genome with its 2,009 protein-coding and 52 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
göker-held et al_final.pdf
göker-held et al_final.pdf
Open Access publication
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TEXT
göker-held et al_final.pdf.txt
göker-held et al_final.pdf.txt
Extracted Text
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MD5
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THUMBNAIL
göker-held et al_final.pdf.jpg
göker-held et al_final.pdf.jpg
Generated Thumbnail
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10033/226833
oai:hzi.openrepository.com:10033/226833
2019-08-30 11:36:32.766
Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/2268512019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
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2012-05-31T10:11:37Z
2012-05-31T10:11:37Z
2010
Complete genome sequence of Meiothermus ruber type strain (21). 2010, 3 (1):26-36 Stand Genomic Sci
1944-3277
21304689
10.4056/sigs.1032748
http://hdl.handle.net/10033/226851
Standards in genomic sciences
Meiothermus ruber (Loginova et al. 1984) Nobre et al. 1996 is the type species of the genus Meiothermus. This thermophilic genus is of special interest, as its members share relatively low degrees of 16S rRNA gene sequence similarity and constitute a separate evolutionary lineage from members of the genus Thermus, from which they can generally be distinguished by their slightly lower temperature optima. The temperature related split is in accordance with the chemotaxonomic feature of the polar lipids. M. ruber is a representative of the low-temperature group. This is the first completed genome sequence of the genus Meiothermus and only the third genome sequence to be published from a member of the family Thermaceae. The 3,097,457 bp long genome with its 3,052 protein-coding and 53 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Meiothermus ruber type strain (21).
Article
2018-06-12T17:19:08Z
Meiothermus ruber (Loginova et al. 1984) Nobre et al. 1996 is the type species of the genus Meiothermus. This thermophilic genus is of special interest, as its members share relatively low degrees of 16S rRNA gene sequence similarity and constitute a separate evolutionary lineage from members of the genus Thermus, from which they can generally be distinguished by their slightly lower temperature optima. The temperature related split is in accordance with the chemotaxonomic feature of the polar lipids. M. ruber is a representative of the low-temperature group. This is the first completed genome sequence of the genus Meiothermus and only the third genome sequence to be published from a member of the family Thermaceae. The 3,097,457 bp long genome with its 3,052 protein-coding and 53 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
tindall et al_final.pdf
tindall et al_final.pdf
Open Access publication
application/pdf
3843629
https://hzi.openrepository.com/bitstream/10033/226851/1/tindall%20et%20al_final.pdf
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Complete genome sequence of Meiothermus silvanus type strain (VI-R2). 2010, 3 (1):37-46 Stand Genomic Sci
1944-3277
21304690
10.4056/sigs.1042812
http://hdl.handle.net/10033/226834
Standards in genomic sciences
Meiothermus silvanus (Tenreiro et al. 1995) Nobre et al. 1996 belongs to a thermophilic genus whose members share relatively low degrees of 16S rRNA gene sequence similarity. Meiothermus constitutes an evolutionary lineage separate from members of the genus Thermus, from which they can generally be distinguished by their slightly lower temperature optima. M. silvanus is of special interest as it causes colored biofilms in the paper making industry and may thus be of economic importance as a biofouler. This is the second completed genome sequence of a member of the genus Meiothermus and only the third genome sequence to be published from a member of the family Thermaceae. The 3,721,669 bp long genome with its 3,667 protein-coding and 55 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Meiothermus silvanus type strain (VI-R2).
Article
2018-06-14T09:17:06Z
Meiothermus silvanus (Tenreiro et al. 1995) Nobre et al. 1996 belongs to a thermophilic genus whose members share relatively low degrees of 16S rRNA gene sequence similarity. Meiothermus constitutes an evolutionary lineage separate from members of the genus Thermus, from which they can generally be distinguished by their slightly lower temperature optima. M. silvanus is of special interest as it causes colored biofilms in the paper making industry and may thus be of economic importance as a biofouler. This is the second completed genome sequence of a member of the genus Meiothermus and only the third genome sequence to be published from a member of the family Thermaceae. The 3,721,669 bp long genome with its 3,667 protein-coding and 55 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2010
Complete genome sequence of Aminobacterium colombiense type strain (ALA-1). 2010, 2 (3):280-9 Stand Genomic Sci
1944-3277
21304712
10.4056/sigs.902116
http://hdl.handle.net/10033/226811
Standards in genomic sciences
Aminobacterium colombiense Baena et al. 1999 is the type species of the genus Aminobacterium. This genus is of large interest because of its isolated phylogenetic location in the family Synergistaceae, its strictly anaerobic lifestyle, and its ability to grow by fermentation of a limited range of amino acids but not carbohydrates. Here we describe the features of this organism, together with the complete genome sequence and annotation. This is the second completed genome sequence of a member of the family Synergistaceae and the first genome sequence of a member of the genus Aminobacterium. The 1,980,592 bp long genome with its 1,914 protein-coding and 56 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Aminobacterium colombiense type strain (ALA-1).
Article
2018-06-13T14:16:55Z
Aminobacterium colombiense Baena et al. 1999 is the type species of the genus Aminobacterium. This genus is of large interest because of its isolated phylogenetic location in the family Synergistaceae, its strictly anaerobic lifestyle, and its ability to grow by fermentation of a limited range of amino acids but not carbohydrates. Here we describe the features of this organism, together with the complete genome sequence and annotation. This is the second completed genome sequence of a member of the family Synergistaceae and the first genome sequence of a member of the genus Aminobacterium. The 1,980,592 bp long genome with its 1,914 protein-coding and 56 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
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oai:repository.helmholtz-hzi.de:10033/2268322019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
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2012-05-31T09:33:25Z
2012-05-31T09:33:25Z
2010
Complete genome sequence of Denitrovibrio acetiphilus type strain (N2460). 2010, 2 (3):270-9 Stand Genomic Sci
1944-3277
21304711
10.4056/sigs.892105
http://hdl.handle.net/10033/226832
Standards in genomic sciences
Denitrovibrio acetiphilus Myhr and Torsvik 2000 is the type species of the genus Denitrovibrio in the bacterial family Deferribacteraceae. It is of phylogenetic interest because there are only six genera described in the family Deferribacteraceae. D. acetiphilus was isolated as a representative of a population reducing nitrate to ammonia in a laboratory column simulating the conditions in off-shore oil recovery fields. When nitrate was added to this column undesirable hydrogen sulfide production was stopped because the sulfate reducing populations were superseded by these nitrate reducing bacteria. Here we describe the features of this marine, mesophilic, obligately anaerobic organism respiring by nitrate reduction, together with the complete genome sequence, and annotation. This is the second complete genome sequence of the order Deferribacterales and the class Deferribacteres, which is the sole class in the phylum Deferribacteres. The 3,222,077 bp genome with its 3,034 protein-coding and 51 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Denitrovibrio acetiphilus type strain (N2460).
Article
2018-06-13T04:10:08Z
Denitrovibrio acetiphilus Myhr and Torsvik 2000 is the type species of the genus Denitrovibrio in the bacterial family Deferribacteraceae. It is of phylogenetic interest because there are only six genera described in the family Deferribacteraceae. D. acetiphilus was isolated as a representative of a population reducing nitrate to ammonia in a laboratory column simulating the conditions in off-shore oil recovery fields. When nitrate was added to this column undesirable hydrogen sulfide production was stopped because the sulfate reducing populations were superseded by these nitrate reducing bacteria. Here we describe the features of this marine, mesophilic, obligately anaerobic organism respiring by nitrate reduction, together with the complete genome sequence, and annotation. This is the second complete genome sequence of the order Deferribacterales and the class Deferribacteres, which is the sole class in the phylum Deferribacteres. The 3,222,077 bp genome with its 3,034 protein-coding and 51 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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2012-05-31T10:32:46Z
2012-05-31T10:32:46Z
2010
Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type strain (SEBR 4207). 2010, 3 (1):85-92 Stand Genomic Sci
1944-3277
21304695
10.4056/sigs.1092865
http://hdl.handle.net/10033/226835
Standards in genomic sciences
Dethiosulfovibrio peptidovorans Magot et al. 1997 is the type species of the genus Dethiosulfovibrio of the family Synergistaceae in the recently created phylum Synergistetes. The strictly anaerobic, vibriod, thiosulfate-reducing bacterium utilizes peptides and amino acids, but neither sugars nor fatty acids. It was isolated from an offshore oil well where it was been reported to be involved in pitting corrosion of mild steel. Initially, this bacterium was described as a distant relative of the genus Thermoanaerobacter, but was not assigned to a genus, it was subsequently placed into the novel phylum Synergistetes. A large number of repeats in the genome sequence prevented an economically justifiable closure of the last gaps. This is only the third published genome from a member of the phylum Synergistetes. The 2,576,359 bp long genome consists of three contigs with 2,458 protein-coding and 59 RNA genes and is part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type strain (SEBR 4207).
Article
2018-06-12T22:17:00Z
Dethiosulfovibrio peptidovorans Magot et al. 1997 is the type species of the genus Dethiosulfovibrio of the family Synergistaceae in the recently created phylum Synergistetes. The strictly anaerobic, vibriod, thiosulfate-reducing bacterium utilizes peptides and amino acids, but neither sugars nor fatty acids. It was isolated from an offshore oil well where it was been reported to be involved in pitting corrosion of mild steel. Initially, this bacterium was described as a distant relative of the genus Thermoanaerobacter, but was not assigned to a genus, it was subsequently placed into the novel phylum Synergistetes. A large number of repeats in the genome sequence prevented an economically justifiable closure of the last gaps. This is only the third published genome from a member of the phylum Synergistetes. The 2,576,359 bp long genome consists of three contigs with 2,458 protein-coding and 59 RNA genes and is part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
labutti et al_final.pdf
labutti et al_final.pdf
Open Access publication
application/pdf
3439894
https://hzi.openrepository.com/bitstream/10033/226835/1/labutti%20et%20al_final.pdf
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2012-05-31T11:19:02Z
2012-05-31T11:19:02Z
2011-10-15
Complete genome sequence of the gliding, heparinolytic Pedobacter saltans type strain (113). 2011, 5 (1):30-40 Stand Genomic Sci
1944-3277
22180808
10.4056/sigs.2154937
http://hdl.handle.net/10033/226872
Standards in genomic sciences
Pedobacter saltans Steyn et al. 1998 is one of currently 32 species in the genus Pedobacter within the family Sphingobacteriaceae. The species is of interest for its isolated location in the tree of life. Like other members of the genus P. saltans is heparinolytic. Cells of P. saltans show a peculiar gliding, dancing motility and can be distinguished from other Pedobacter strains by their ability to utilize glycerol and the inability to assimilate D-cellobiose. The genome presented here is only the second completed genome sequence of a type strain from a member of the family Sphingobacteriaceae to be published. The 4,635,236 bp long genome with its 3,854 protein-coding and 67 RNA genes consists of one chromosome, and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the gliding, heparinolytic Pedobacter saltans type strain (113).
Article
2018-06-13T15:30:51Z
Pedobacter saltans Steyn et al. 1998 is one of currently 32 species in the genus Pedobacter within the family Sphingobacteriaceae. The species is of interest for its isolated location in the tree of life. Like other members of the genus P. saltans is heparinolytic. Cells of P. saltans show a peculiar gliding, dancing motility and can be distinguished from other Pedobacter strains by their ability to utilize glycerol and the inability to assimilate D-cellobiose. The genome presented here is only the second completed genome sequence of a type strain from a member of the family Sphingobacteriaceae to be published. The 4,635,236 bp long genome with its 3,854 protein-coding and 67 RNA genes consists of one chromosome, and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2012-08-02T12:41:09Z
2012-08-02T12:41:09Z
2011-10-15
Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus tusciae type strain (T2) and reclassification in the new genus, Kyrpidia gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family Alicyclobacillaceae da Costa and Rainey, 2010. 2011, 5 (1):121-34 Stand Genomic Sci
1944-3277
22180816
10.4056/sigs.2144922
http://hdl.handle.net/10033/237052
Standards in genomic sciences
Bacillus tusciae Bonjour & Aragno 1994 is a hydrogen-oxidizing, thermoacidophilic spore former that lives as a facultative chemolithoautotroph in solfataras. Although 16S rRNA gene sequencing was well established at the time of the initial description of the organism, 16S sequence data were not available and the strain was placed into the genus Bacillus based on limited chemotaxonomic information. Despite the now obvious misplacement of strain T2 as a member of the genus Bacillus in 16S rRNA-based phylogenetic trees, the misclassification remained uncorrected for many years, which was likely due to the extremely difficult, analysis-hampering cultivation conditions and poor growth rate of the strain. Here we provide a taxonomic re-evaluation of strain T2T (= DSM 2912 = NBRC 15312) and propose its reclassification as the type strain of a new species, Kyrpidia tusciae, and the type species of the new genus Kyrpidia, which is a sister-group of Alicyclobacillus. The family Alicyclobacillaceae da Costa and Rainey, 2010 is emended. The 3,384,766 bp genome with its 3,323 protein-coding and 78 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus tusciae type strain (T2) and reclassification in the new genus, Kyrpidia gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family Alicyclobacillaceae da Costa and Rainey, 2010.
Article
2018-06-12T22:50:06Z
Bacillus tusciae Bonjour & Aragno 1994 is a hydrogen-oxidizing, thermoacidophilic spore former that lives as a facultative chemolithoautotroph in solfataras. Although 16S rRNA gene sequencing was well established at the time of the initial description of the organism, 16S sequence data were not available and the strain was placed into the genus Bacillus based on limited chemotaxonomic information. Despite the now obvious misplacement of strain T2 as a member of the genus Bacillus in 16S rRNA-based phylogenetic trees, the misclassification remained uncorrected for many years, which was likely due to the extremely difficult, analysis-hampering cultivation conditions and poor growth rate of the strain. Here we provide a taxonomic re-evaluation of strain T2T (= DSM 2912 = NBRC 15312) and propose its reclassification as the type strain of a new species, Kyrpidia tusciae, and the type species of the new genus Kyrpidia, which is a sister-group of Alicyclobacillus. The family Alicyclobacillaceae da Costa and Rainey, 2010 is emended. The 3,384,766 bp genome with its 3,323 protein-coding and 78 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.
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oai:repository.helmholtz-hzi.de:10033/2276752019-08-30T11:36:59Zcom_10033_6815com_10033_6814col_10033_6886
Reissmann, Silvana
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500
Gillen, Christine M
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Fulde, Marcus
8e6c69232f5183b89bc38e4c9811ef00
500
Bergmann, René
89282da5816824b34e6e6c07a5cd4a30
500
Nerlich, Andreas
1264b12e2e8ac81308439634b5bdfd8f
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Rajkumari, Reena
b896d78ad28be49ae905979e98450768
500
Brahmadathan, Kootallur N
5a726c3fce0db03c60b85e46c5d063c0
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Chhatwal, Gursharan S
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Nitsche-Schmitz, D Patric
cb8c9f97bad4b6ed57d10ef22331a3f4
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Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Braunschweig, Germany.
2012-06-06T14:15:23Z
2012-06-06T14:15:23Z
2012
Region specific and worldwide distribution of collagen-binding M proteins with PARF motifs among human pathogenic streptococcal isolates. 2012, 7 (1):e30122 PLoS ONE
1932-6203
22253902
10.1371/journal.pone.0030122
http://hdl.handle.net/10033/227675
PloS one
Some of the variety of Streptococcus pyogenes and Streptococcus dysgalactiae ssp. equisimilis (SDSE) M proteins act as collagen-binding adhesins that facilitate acute infection. Moreover, their potential to trigger collagen autoimmunity has been implicated in the pathogenesis of acute rheumatic fever and attributed to a collagen-binding motif called PARF (peptide associated with rheumatic fever). For the first time we determine the rate of clinical isolates with collagen-binding M proteins that use a PARF motif (A/T/E)XYLXX(L/F)N in a defined geographic region, Vellore in South India. In this region both, incidence of streptococcal infections and prevalence of acute rheumatic fever are high. M proteins with PARF motif conferred collagen-binding activity to 3.9% of 153 S. pyogenes and 10.6% of 255 SDSE clinical isolates from Vellore. The PARF motif occurred in three S. pyogenes and 22 SDSE M protein types. In one of the S. pyogenes and five of the SDSE M proteins that contained the motif, collagen-binding was impaired, due to influences of other parts of the M protein molecule. The accumulated data on the collagen binding activity of certain M protein types allowed a reanalysis of published worldwide emm-typing data with the aim to estimate the rates of isolates that bind collagen via PARF. The results indicate that M proteins, which bind collagen via a PARF motif, are epidemiologically relevant in human infections, not only in Vellore. It is imperative to include the most relevant collagen-binding M types in vaccines. But when designing M protein based vaccines it should be considered that collagen binding motifs within the vaccine antigen remain potential risk factors.
en
Archived with thanks to PloS one
Amino Acid Motifs
Amino Acid Sequence
Bacterial Proteins
Collagen
Geography
Humans
India
Internationality
Molecular Sequence Data
Protein Binding
Protein Structure, Tertiary
Recombinant Proteins
Streptococcus pyogenes
Region specific and worldwide distribution of collagen-binding M proteins with PARF motifs among human pathogenic streptococcal isolates.
Article
2018-06-13T21:41:53Z
Some of the variety of Streptococcus pyogenes and Streptococcus dysgalactiae ssp. equisimilis (SDSE) M proteins act as collagen-binding adhesins that facilitate acute infection. Moreover, their potential to trigger collagen autoimmunity has been implicated in the pathogenesis of acute rheumatic fever and attributed to a collagen-binding motif called PARF (peptide associated with rheumatic fever). For the first time we determine the rate of clinical isolates with collagen-binding M proteins that use a PARF motif (A/T/E)XYLXX(L/F)N in a defined geographic region, Vellore in South India. In this region both, incidence of streptococcal infections and prevalence of acute rheumatic fever are high. M proteins with PARF motif conferred collagen-binding activity to 3.9% of 153 S. pyogenes and 10.6% of 255 SDSE clinical isolates from Vellore. The PARF motif occurred in three S. pyogenes and 22 SDSE M protein types. In one of the S. pyogenes and five of the SDSE M proteins that contained the motif, collagen-binding was impaired, due to influences of other parts of the M protein molecule. The accumulated data on the collagen binding activity of certain M protein types allowed a reanalysis of published worldwide emm-typing data with the aim to estimate the rates of isolates that bind collagen via PARF. The results indicate that M proteins, which bind collagen via a PARF motif, are epidemiologically relevant in human infections, not only in Vellore. It is imperative to include the most relevant collagen-binding M types in vaccines. But when designing M protein based vaccines it should be considered that collagen binding motifs within the vaccine antigen remain potential risk factors.
ORIGINAL
Reißmann et al_final.pdf
Reißmann et al_final.pdf
Open Access publication
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oai:repository.helmholtz-hzi.de:10033/2318132019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Raz, Assaf
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500
Talay, Susanne R
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Fischetti, Vincent A
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Bacterial Pathogenesis and Immunology, Rockefeller University, New York, USA. araz@rockefeller.edu
2012-07-03T08:40:21Z
2012-07-03T08:40:21Z
2012-05
Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes. 2012, 84 (4):631-47 Mol. Microbiol.
1365-2958
22512736
10.1111/j.1365-2958.2012.08047.x
http://hdl.handle.net/10033/231813
Molecular microbiology
Wall-anchored surface proteins are critical for the in vivo survival of Streptococcus pyogenes. Cues in the signal sequence direct the membrane translocation of surface proteins: M protein to the septum, and SfbI to the poles. Both proteins are subsequently anchored to the wall by the membrane bound enzyme sortase A. However, the cellular features of these pathways are not fully understood. Here we show that M protein and SfbI are anchored simultaneously throughout the cell cycle. M protein is rapidly anchored at the septum, and in part of the cell cycle, is anchored simultaneously at the mother and daughter septa. Conversely, SfbI accumulates gradually on peripheral peptidoglycan, resulting in a polar distribution. Sortase is not required for translocation of M protein or SfbI at their respective locations. Methicillin-induced unbalanced peptidoglycan synthesis diminishes surface M protein but not SfbI. Furthermore, overexpression of the division regulator DivIVA also diminishes surface M protein but increases SfbI. These results demonstrate a close connection between the regulation of cell division and protein anchoring. Better understanding of the spatial regulation of surface anchoring may lead to the identification of novel targets for the development of anti-infective agents, given the importance of surface molecules for pathogenesis.
en
Archived with thanks to Molecular microbiology
Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes.
Article
2013-05-15T00:00:00Z
Wall-anchored surface proteins are critical for the in vivo survival of Streptococcus pyogenes. Cues in the signal sequence direct the membrane translocation of surface proteins: M protein to the septum, and SfbI to the poles. Both proteins are subsequently anchored to the wall by the membrane bound enzyme sortase A. However, the cellular features of these pathways are not fully understood. Here we show that M protein and SfbI are anchored simultaneously throughout the cell cycle. M protein is rapidly anchored at the septum, and in part of the cell cycle, is anchored simultaneously at the mother and daughter septa. Conversely, SfbI accumulates gradually on peripheral peptidoglycan, resulting in a polar distribution. Sortase is not required for translocation of M protein or SfbI at their respective locations. Methicillin-induced unbalanced peptidoglycan synthesis diminishes surface M protein but not SfbI. Furthermore, overexpression of the division regulator DivIVA also diminishes surface M protein but increases SfbI. These results demonstrate a close connection between the regulation of cell division and protein anchoring. Better understanding of the spatial regulation of surface anchoring may lead to the identification of novel targets for the development of anti-infective agents, given the importance of surface molecules for pathogenesis.
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2335512019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Centanni, Manuela
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Bergmann, Simone
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Turroni, Silvia
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Hammerschmidt, Sven
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Chhatwal, Gursharan Singh
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Brigidi, Patrizia
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Candela, Marco
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Department of Pharmaceutical Sciences, University of Bologna, Bologna, Italy.
2012-07-13T09:12:54Z
2012-07-13T09:12:54Z
2012-04
Tumor necrosis factor alpha modulates the dynamics of the plasminogen-mediated early interaction between Bifidobacterium animalis subsp. lactis and human enterocytes. 2012, 78 (7):2465-9 Appl. Environ. Microbiol.
1098-5336
22287006
10.1128/AEM.07883-11
http://hdl.handle.net/10033/233551
Applied and environmental microbiology
The capacity to intervene with the host plasminogen system has recently been considered an important component in the interaction process between Bifidobacterium animalis subsp. lactis and the human host. However, its significance in the bifidobacterial microecology within the human gastrointestinal tract is still an open question. Here we demonstrate that human plasminogen favors the B. animalis subsp. lactis BI07 adhesion to HT29 cells. Prompting the HT29 cell capacity to activate plasminogen, tumor necrosis factor alpha (TNF-α) modulated the plasminogen-mediated bacterium-enterocyte interaction, reducing the bacterial adhesion to the enterocytes and enhancing migration to the luminal compartment.
en
Archived with thanks to Applied and environmental microbiology
Tumor necrosis factor alpha modulates the dynamics of the plasminogen-mediated early interaction between Bifidobacterium animalis subsp. lactis and human enterocytes.
Article
2018-06-13T15:12:37Z
The capacity to intervene with the host plasminogen system has recently been considered an important component in the interaction process between Bifidobacterium animalis subsp. lactis and the human host. However, its significance in the bifidobacterial microecology within the human gastrointestinal tract is still an open question. Here we demonstrate that human plasminogen favors the B. animalis subsp. lactis BI07 adhesion to HT29 cells. Prompting the HT29 cell capacity to activate plasminogen, tumor necrosis factor alpha (TNF-α) modulated the plasminogen-mediated bacterium-enterocyte interaction, reducing the bacterial adhesion to the enterocytes and enhancing migration to the luminal compartment.
ORIGINAL
Centanni et al_final.pdf
Centanni et al_final.pdf
original manuscript
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Figure 1 Centanni et al.pdf
Figure 1 Centanni et al.pdf
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10033/233551
oai:hzi.openrepository.com:10033/233551
2019-08-30 11:37:23.769
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2357752019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Lapidus, Alla
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Nolan, Matt
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Lucas, Susan
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500
Glavina Del Rio, Tijana
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500
Tice, Hope
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Cheng, Jan-Fang
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Tapia, Roxanne
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Han, Cliff
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Goodwin, Lynne
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Pitluck, Sam
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Liolios, Konstantinos
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Pagani, Ioanna
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500
Ivanova, Natalia
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Huntemann, Marcel
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Mavromatis, Konstantinos
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500
Mikhailova, Natalia
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Pati, Amrita
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Chen, Amy
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Palaniappan, Krishna
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Land, Miriam
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500
Brambilla, Evelyne-Marie
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Rohde, Manfred
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500
Abt, Birte
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500
Verbarg, Susanne
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Göker, Markus
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Bristow, James
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500
Eisen, Jonathan A
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500
Markowitz, Victor
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500
Hugenholtz, Philip
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500
Kyrpides, Nikos C
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500
Klenk, Hans-Peter
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500
Woyke, Tanja
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2012-07-25T14:52:28Z
2012-07-25T14:52:28Z
2011-12-31
Genome sequence of the filamentous, gliding Thiothrix nivea neotype strain (JP2(T)). 2011, 5 (3):398-406 Stand Genomic Sci
1944-3277
22675589
10.4056/sigs.2344929
http://hdl.handle.net/10033/235775
Standards in genomic sciences
Thiothrix nivea (Rabenhorst 1865) Winogradsky 1888 (Approved Lists 1980) emend. Larkin and Shinabarger 1983 is the type species of the genus Thiothrix in the family Thiotrichaceae. The species is of interest not only because of its isolated location in the yet to be genomically characterized region of the tree of life, but also because of its life-style with gliding gonidia, the multilayer sheath, rosettes, and the embedded sulfur granules. Strain JP2(T) is the neotype strain of the species which was first observed by Rabenhorst in 1865 and later reclassified by Winogradsky in 1888 into the then novel genus Thiothrix. This is the first completed (improved-high-quality-draft) genome sequence to be published of a member of the family Thiotrichaceae. The genome in its current assembly consists of 15 contigs in four scaffolds with a total of 4,691,711 bp bearing 4,542 protein-coding and 52 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Genome sequence of the filamentous, gliding Thiothrix nivea neotype strain (JP2(T)).
Article
2018-06-13T01:21:25Z
Thiothrix nivea (Rabenhorst 1865) Winogradsky 1888 (Approved Lists 1980) emend. Larkin and Shinabarger 1983 is the type species of the genus Thiothrix in the family Thiotrichaceae. The species is of interest not only because of its isolated location in the yet to be genomically characterized region of the tree of life, but also because of its life-style with gliding gonidia, the multilayer sheath, rosettes, and the embedded sulfur granules. Strain JP2(T) is the neotype strain of the species which was first observed by Rabenhorst in 1865 and later reclassified by Winogradsky in 1888 into the then novel genus Thiothrix. This is the first completed (improved-high-quality-draft) genome sequence to be published of a member of the family Thiotrichaceae. The genome in its current assembly consists of 15 contigs in four scaffolds with a total of 4,691,711 bp bearing 4,542 protein-coding and 52 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
Lapidus et al_final.pdf
Lapidus et al_final.pdf
Open Access publication
application/pdf
1878315
https://hzi.openrepository.com/bitstream/10033/235775/1/Lapidus%20et%20al_final.pdf
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license_url
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LICENSE
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MD5
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TEXT
Lapidus et al_final.pdf.txt
Lapidus et al_final.pdf.txt
Extracted Text
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THUMBNAIL
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Generated Thumbnail
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10033/235775
oai:hzi.openrepository.com:10033/235775
2019-08-30 11:37:23.813
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2358522019-08-30T11:37:24Zcom_10033_6815com_10033_6814col_10033_6886
Chertkov, Olga
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2012-07-26T10:23:55Z
2012-07-26T10:23:55Z
2011-10-15
Complete genome sequence of Tolumonas auensis type strain (TA 4). 2011, 5 (1):112-20 Stand Genomic Sci
1944-3277
22180815
10.4056/sigs.2184986
http://hdl.handle.net/10033/235852
Standards in genomic sciences
Tolumonas auensis Fischer-Romero et al. 1996 is currently the only validly named species of the genus Tolumonas in the family Aeromonadaceae. The strain is of interest because of its ability to produce toluene from phenylalanine and other phenyl precursors, as well as phenol from tyrosine. This is of interest because toluene is normally considered to be a tracer of anthropogenic pollution in lakes, but T. auensis represents a biogenic source of toluene. Other than Aeromonas hydrophila subsp. hydrophila, T. auensis strain TA 4(T) is the only other member in the family Aeromonadaceae with a completely sequenced type-strain genome. The 3,471,292 bp chromosome with a total of 3,288 protein-coding and 116 RNA genes was sequenced as part of the DOE Joint Genome Institute Program JBEI 2008.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Tolumonas auensis type strain (TA 4).
Article
2018-06-12T21:48:17Z
Tolumonas auensis Fischer-Romero et al. 1996 is currently the only validly named species of the genus Tolumonas in the family Aeromonadaceae. The strain is of interest because of its ability to produce toluene from phenylalanine and other phenyl precursors, as well as phenol from tyrosine. This is of interest because toluene is normally considered to be a tracer of anthropogenic pollution in lakes, but T. auensis represents a biogenic source of toluene. Other than Aeromonas hydrophila subsp. hydrophila, T. auensis strain TA 4(T) is the only other member in the family Aeromonadaceae with a completely sequenced type-strain genome. The 3,471,292 bp chromosome with a total of 3,288 protein-coding and 116 RNA genes was sequenced as part of the DOE Joint Genome Institute Program JBEI 2008.
ORIGINAL
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2019-08-30 11:37:24.199
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2370342019-08-30T11:37:44Zcom_10033_6815com_10033_6814col_10033_6886
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2012-08-02T11:22:23Z
2012-08-02T11:22:23Z
2011-04-29
Complete genome sequence of Odoribacter splanchnicus type strain (1651/6). 2011, 4 (2):200-9 Stand Genomic Sci
1944-3277
21677857
10.4056/sigs.1714269
http://hdl.handle.net/10033/237034
Standards in genomic sciences
Odoribacter splanchnicus (Werner et al. 1975) Hardham et al. 2008 is the type species of the genus Odoribacter, which belongs to the family Porphyromonadaceae in the order 'Bacteroidales'. The species is of interest because members of the Odoribacter form an isolated cluster within the Porphyromonadaceae. This is the first completed genome sequence of a member of the genus Odoribacter and the fourth sequence from the family Porphyromonadaceae. The 4,392,288 bp long genome with its 3,672 protein-coding and 74 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Odoribacter splanchnicus type strain (1651/6).
Article
2018-06-13T02:22:37Z
Odoribacter splanchnicus (Werner et al. 1975) Hardham et al. 2008 is the type species of the genus Odoribacter, which belongs to the family Porphyromonadaceae in the order 'Bacteroidales'. The species is of interest because members of the Odoribacter form an isolated cluster within the Porphyromonadaceae. This is the first completed genome sequence of a member of the genus Odoribacter and the fourth sequence from the family Porphyromonadaceae. The 4,392,288 bp long genome with its 3,672 protein-coding and 74 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
göker-gronow et al_final.pdf
göker-gronow et al_final.pdf
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2019-08-30 11:37:44.652
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2370242019-08-30T11:37:44Zcom_10033_6815com_10033_6814col_10033_6886
Bernardo-García, Noelia
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Bartual, Sergio G
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Fulde, Marcus
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Bergmann, Simone
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Hermoso, Juan A
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Department of Crystallography and Structural Biology, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
2012-08-02T11:44:02Z
2012-08-02T11:44:02Z
2011-10-01
Crystallization and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae. 2011, 67 (Pt 10):1285-9 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
1744-3091
22102049
10.1107/S1744309111030922
http://hdl.handle.net/10033/237024
Acta crystallographica. Section F, Structural biology and crystallization communications
Phosphoglycerate kinase (PGK) is a widespread two-domain enzyme that plays a critical role in the glycolytic pathway. Several glycolytic enzymes from streptococci have been identified as surface-exposed proteins that are involved in streptococcal virulence by their ability to bind host proteins. This binding allows pneumococcal cells to disseminate through the epithelial and endothelial layers. Crystallization of PGK from Streptococcus pneumoniae yielded orthorhombic crystals (space group I222, unit-cell parameters a = 62.73, b = 75.38, c = 83.63 Å). However, the unit cell of these crystals was not compatible with the presence of full-length PGK. Various analytical methods showed that only the N-terminal domain of PGK was present in the I222 crystals. The ternary complex of PGK with adenylyl imidodiphosphate (AMP-PNP) and 3-phospho-D-glycerate (3PGA) produced monoclinic crystals (space group P2(1), unit-cell parameters a = 40.35, b = 78.23, c = 59.03 Å, β = 96.34°). Molecular replacement showed that this new crystal form contained full-length PGK, thereby indicating the relevance of including substrates in order to avoid proteolysis during the crystallization process.
en
Archived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communications
Crystallization
Crystallography, X-Ray
Phosphoglycerate Kinase
Streptococcus pneumoniae
Crystallization and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae.
Article
2018-06-12T21:27:38Z
Phosphoglycerate kinase (PGK) is a widespread two-domain enzyme that plays a critical role in the glycolytic pathway. Several glycolytic enzymes from streptococci have been identified as surface-exposed proteins that are involved in streptococcal virulence by their ability to bind host proteins. This binding allows pneumococcal cells to disseminate through the epithelial and endothelial layers. Crystallization of PGK from Streptococcus pneumoniae yielded orthorhombic crystals (space group I222, unit-cell parameters a = 62.73, b = 75.38, c = 83.63 Å). However, the unit cell of these crystals was not compatible with the presence of full-length PGK. Various analytical methods showed that only the N-terminal domain of PGK was present in the I222 crystals. The ternary complex of PGK with adenylyl imidodiphosphate (AMP-PNP) and 3-phospho-D-glycerate (3PGA) produced monoclinic crystals (space group P2(1), unit-cell parameters a = 40.35, b = 78.23, c = 59.03 Å, β = 96.34°). Molecular replacement showed that this new crystal form contained full-length PGK, thereby indicating the relevance of including substrates in order to avoid proteolysis during the crystallization process.
ORIGINAL
bernardo-garcía et al_final.pdf
bernardo-garcía et al_final.pdf
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Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/2371712019-08-30T11:37:44Zcom_10033_6815com_10033_6814col_10033_6886
Chang, Yun-Juan
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Land, Miriam
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Hauser, Loren
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Del Rio, Tijana Glavina
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Lucas, Susan
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2012-08-03T14:29:30Z
2012-08-03T14:29:30Z
2011-10-15
Non-contiguous finished genome sequence and contextual data of the filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1-21). 2011, 5 (1):97-111 Stand Genomic Sci
1944-3277
22180814
10.4056/sigs.2114901
http://hdl.handle.net/10033/237171
Standards in genomic sciences
Ktedonobacter racemifer corrig. Cavaletti et al. 2007 is the type species of the genus Ktedonobacter, which in turn is the type genus of the family Ktedonobacteraceae, the type family of the order Ktedonobacterales within the class Ktedonobacteria in the phylum 'Chloroflexi'. Although K. racemifer shares some morphological features with the actinobacteria, it is of special interest because it was the first cultivated representative of a deep branching unclassified lineage of otherwise uncultivated environmental phylotypes tentatively located within the phylum 'Chloroflexi'. The aerobic, filamentous, non-motile, spore-forming Gram-positive heterotroph was isolated from soil in Italy. The 13,661,586 bp long non-contiguous finished genome consists of ten contigs and is the first reported genome sequence from a member of the class Ktedonobacteria. With its 11,453 protein-coding and 87 RNA genes, it is the largest prokaryotic genome reported so far. It comprises a large number of over-represented COGs, particularly genes associated with transposons, causing the genetic redundancy within the genome being considerably larger than expected by chance. This work is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Non-contiguous finished genome sequence and contextual data of the filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1-21).
Article
2018-06-13T19:58:24Z
Ktedonobacter racemifer corrig. Cavaletti et al. 2007 is the type species of the genus Ktedonobacter, which in turn is the type genus of the family Ktedonobacteraceae, the type family of the order Ktedonobacterales within the class Ktedonobacteria in the phylum 'Chloroflexi'. Although K. racemifer shares some morphological features with the actinobacteria, it is of special interest because it was the first cultivated representative of a deep branching unclassified lineage of otherwise uncultivated environmental phylotypes tentatively located within the phylum 'Chloroflexi'. The aerobic, filamentous, non-motile, spore-forming Gram-positive heterotroph was isolated from soil in Italy. The 13,661,586 bp long non-contiguous finished genome consists of ten contigs and is the first reported genome sequence from a member of the class Ktedonobacteria. With its 11,453 protein-coding and 87 RNA genes, it is the largest prokaryotic genome reported so far. It comprises a large number of over-represented COGs, particularly genes associated with transposons, causing the genetic redundancy within the genome being considerably larger than expected by chance. This work is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
Chang et al_final.pdf
Chang et al_final.pdf
Open Access publication
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Helmholtz Zentrum für Infektionsforschung Repository
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2012-08-07T12:23:26Z
2012-08-07T12:23:26Z
2011-10-15
Complete genome sequence of the gliding freshwater bacterium Fluviicola taffensis type strain (RW262). 2011, 5 (1):21-9 Stand Genomic Sci
1944-3277
22180807
10.4056/sigs.2124912
http://hdl.handle.net/10033/237552
Standards in genomic sciences
Fluviicola taffensis O'Sullivan et al. 2005 belongs to the monotypic genus Fluviicola within the family Cryomorphaceae. The species is of interest because of its isolated phylogenetic location in the genome-sequenced fraction of the tree of life. Strain RW262(T) forms a monophyletic lineage with uncultivated bacteria represented in freshwater 16S rRNA gene libraries. A similar phylogenetic differentiation occurs between freshwater and marine bacteria in the family Flavobacteriaceae, a sister family to Cryomorphaceae. Most remarkable is the inability of this freshwater bacterium to grow in the presence of Na(+) ions. All other genera in the family Cryomorphaceae are from marine habitats and have an absolute requirement for Na(+) ions or natural sea water. F. taffensis is the first member of the family Cryomorphaceae with a completely sequenced and publicly available genome. The 4,633,577 bp long genome with its 4,082 protein-coding and 49 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the gliding freshwater bacterium Fluviicola taffensis type strain (RW262).
Article
2018-06-12T16:48:39Z
Fluviicola taffensis O'Sullivan et al. 2005 belongs to the monotypic genus Fluviicola within the family Cryomorphaceae. The species is of interest because of its isolated phylogenetic location in the genome-sequenced fraction of the tree of life. Strain RW262(T) forms a monophyletic lineage with uncultivated bacteria represented in freshwater 16S rRNA gene libraries. A similar phylogenetic differentiation occurs between freshwater and marine bacteria in the family Flavobacteriaceae, a sister family to Cryomorphaceae. Most remarkable is the inability of this freshwater bacterium to grow in the presence of Na(+) ions. All other genera in the family Cryomorphaceae are from marine habitats and have an absolute requirement for Na(+) ions or natural sea water. F. taffensis is the first member of the family Cryomorphaceae with a completely sequenced and publicly available genome. The 4,633,577 bp long genome with its 4,082 protein-coding and 49 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2019-08-30 11:27:16.218
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-08-09T07:38:45Z
2012-08-09T07:38:45Z
2011-04-29
Complete genome sequence of Cellulophaga lytica type strain (LIM-21). 2011, 4 (2):221-32 Stand Genomic Sci
1944-3277
21677859
10.4056/sigs.1774329
http://hdl.handle.net/10033/237831
Standards in genomic sciences
Cellulophaga lytica (Lewin 1969) Johansen et al. 1999 is the type species of the genus Cellulophaga, which belongs to the family Flavobacteriaceae within the phylum 'Bacteroidetes' and was isolated from marine beach mud in Limon, Costa Rica. The species is of biotechnological interest because its members produce a wide range of extracellular enzymes capable of degrading proteins and polysaccharides. After the genome sequence of Cellulophaga algicola this is the second completed genome sequence of a member of the genus Cellulophaga. The 3,765,936 bp long genome with its 3,303 protein-coding and 55 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of Cellulophaga lytica type strain (LIM-21).
Article
421347
231830
2018-06-13T21:25:01Z
Cellulophaga lytica (Lewin 1969) Johansen et al. 1999 is the type species of the genus Cellulophaga, which belongs to the family Flavobacteriaceae within the phylum 'Bacteroidetes' and was isolated from marine beach mud in Limon, Costa Rica. The species is of biotechnological interest because its members produce a wide range of extracellular enzymes capable of degrading proteins and polysaccharides. After the genome sequence of Cellulophaga algicola this is the second completed genome sequence of a member of the genus Cellulophaga. The 3,765,936 bp long genome with its 3,303 protein-coding and 55 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
pati-abt et al_final.pdf
pati-abt et al_final.pdf
Open Access publication
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https://repository.helmholtz-hzi.de/bitstream/10033/237831/1/pati-abt%20et%20al_final.pdf
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TEXT
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THUMBNAIL
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Non-contiguous finished genome sequence of the opportunistic oral pathogen Prevotella multisaccharivorax type strain (PPPA20). 2011, 5 (1):41-9 Stand Genomic Sci
1944-3277
22180809
10.4056/sigs.2164949
http://hdl.handle.net/10033/237871
Standards in genomic sciences
Prevotella multisaccharivorax Sakamoto et al. 2005 is a species of the large genus Prevotella, which belongs to the family Prevotellaceae. The species is of medical interest because its members are able to cause diseases in the human oral cavity such as periodontitis, root caries and others. Although 77 Prevotella genomes have already been sequenced or are targeted for sequencing, this is only the second completed genome sequence of a type strain of a species within the genus Prevotella to be published. The 3,388,644 bp long genome is assembled in three non-contiguous contigs, harbors 2,876 protein-coding and 75 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Non-contiguous finished genome sequence of the opportunistic oral pathogen Prevotella multisaccharivorax type strain (PPPA20).
Article
2018-06-12T16:59:08Z
Prevotella multisaccharivorax Sakamoto et al. 2005 is a species of the large genus Prevotella, which belongs to the family Prevotellaceae. The species is of medical interest because its members are able to cause diseases in the human oral cavity such as periodontitis, root caries and others. Although 77 Prevotella genomes have already been sequenced or are targeted for sequencing, this is only the second completed genome sequence of a type strain of a species within the genus Prevotella to be published. The 3,388,644 bp long genome is assembled in three non-contiguous contigs, harbors 2,876 protein-coding and 75 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2012-05-25
Complete genome sequence of the termite hindgut bacterium Spirochaeta coccoides type strain (SPN1(T)), reclassification in the genus Sphaerochaeta as Sphaerochaeta coccoides comb. nov. and emendations of the family Spirochaetaceae and the genus Sphaerochaeta. 2012, 6 (2):194-209 Stand Genomic Sci
1944-3277
22768363
10.4056/sigs.2796069
http://hdl.handle.net/10033/240612
Standards in genomic sciences
Spirochaeta coccoides Dröge et al. 2006 is a member of the genus Spirochaeta Ehrenberg 1835, one of the oldest named genera within the Bacteria. S. coccoides is an obligately anaerobic, Gram-negative, non-motile, spherical bacterium that was isolated from the hindgut contents of the termite Neotermes castaneus. The species is of interest because it may play an important role in the digestion of breakdown products from cellulose and hemicellulose in the termite gut. Here we provide a taxonomic re-evaluation for strain SPN1(T), and based on physiological and genomic characteristics, we propose its reclassification as a novel species in the genus Sphaerochaeta, a recently published sister group of the Spirochaeta. The 2,227,296 bp long genome of strain SPN1(T) with its 1,866 protein-coding and 58 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the termite hindgut bacterium Spirochaeta coccoides type strain (SPN1(T)), reclassification in the genus Sphaerochaeta as Sphaerochaeta coccoides comb. nov. and emendations of the family Spirochaetaceae and the genus Sphaerochaeta.
Article
2018-06-13T21:26:02Z
Spirochaeta coccoides Dröge et al. 2006 is a member of the genus Spirochaeta Ehrenberg 1835, one of the oldest named genera within the Bacteria. S. coccoides is an obligately anaerobic, Gram-negative, non-motile, spherical bacterium that was isolated from the hindgut contents of the termite Neotermes castaneus. The species is of interest because it may play an important role in the digestion of breakdown products from cellulose and hemicellulose in the termite gut. Here we provide a taxonomic re-evaluation for strain SPN1(T), and based on physiological and genomic characteristics, we propose its reclassification as a novel species in the genus Sphaerochaeta, a recently published sister group of the Spirochaeta. The 2,227,296 bp long genome of strain SPN1(T) with its 1,866 protein-coding and 58 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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Complete genome sequence of the thermophilic sulfate-reducing ocean bacterium Thermodesulfatator indicus type strain (CIR29812(T)). 2012, 6 (2):155-64 Stand Genomic Sci
1944-3277
22768359
10.4056/sigs.2665915
http://hdl.handle.net/10033/240592
Standards in genomic sciences
Thermodesulfatator indicus Moussard et al. 2004 is a member of the Thermodesulfobacteriaceae, a family in the phylum Thermodesulfobacteria that is currently poorly characterized at the genome level. Members of this phylum are of interest because they represent a distinct, deep-branching, Gram-negative lineage. T. indicus is an anaerobic, thermophilic, chemolithoautotrophic sulfate reducer isolated from a deep-sea hydrothermal vent. Here we describe the features of this organism, together with the complete genome sequence, and annotation. The 2,322,224 bp long chromosome with its 2,233 protein-coding and 58 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the thermophilic sulfate-reducing ocean bacterium Thermodesulfatator indicus type strain (CIR29812(T)).
Article
2018-06-13T17:04:55Z
Thermodesulfatator indicus Moussard et al. 2004 is a member of the Thermodesulfobacteriaceae, a family in the phylum Thermodesulfobacteria that is currently poorly characterized at the genome level. Members of this phylum are of interest because they represent a distinct, deep-branching, Gram-negative lineage. T. indicus is an anaerobic, thermophilic, chemolithoautotrophic sulfate reducer isolated from a deep-sea hydrothermal vent. Here we describe the features of this organism, together with the complete genome sequence, and annotation. The 2,322,224 bp long chromosome with its 2,233 protein-coding and 58 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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Complete genome sequence of the aerobic, heterotroph Marinithermus hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent chimney. 2012, 6 (1):21-30 Stand Genomic Sci
1944-3277
22675595
10.4056/sigs.2435521
http://hdl.handle.net/10033/240638
Standards in genomic sciences
Marinithermus hydrothermalis Sako et al. 2003 is the type species of the monotypic genus Marinithermus. M. hydrothermalis T1(T) was the first isolate within the phylum "Thermus-Deinococcus" to exhibit optimal growth under a salinity equivalent to that of sea water and to have an absolute requirement for NaCl for growth. M. hydrothermalis T1(T) is of interest because it may provide a new insight into the ecological significance of the aerobic, thermophilic decomposers in the circulation of organic compounds in deep-sea hydrothermal vent ecosystems. This is the first completed genome sequence of a member of the genus Marinithermus and the seventh sequence from the family Thermaceae. Here we describe the features of this organism, together with the complete genome sequence and annotation. The 2,269,167 bp long genome with its 2,251 protein-coding and 59 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the aerobic, heterotroph Marinithermus hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent chimney.
Article
2018-06-12T22:44:22Z
Marinithermus hydrothermalis Sako et al. 2003 is the type species of the monotypic genus Marinithermus. M. hydrothermalis T1(T) was the first isolate within the phylum "Thermus-Deinococcus" to exhibit optimal growth under a salinity equivalent to that of sea water and to have an absolute requirement for NaCl for growth. M. hydrothermalis T1(T) is of interest because it may provide a new insight into the ecological significance of the aerobic, thermophilic decomposers in the circulation of organic compounds in deep-sea hydrothermal vent ecosystems. This is the first completed genome sequence of a member of the genus Marinithermus and the seventh sequence from the family Thermaceae. Here we describe the features of this organism, together with the complete genome sequence and annotation. The 2,269,167 bp long genome with its 2,251 protein-coding and 59 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
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oai:repository.helmholtz-hzi.de:10033/2408382019-08-30T11:28:51Zcom_10033_6815com_10033_6814col_10033_6886
Wargenau, Andreas
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Institut für Partikeltechnik, Technische Universität Braunschweig, Volkmaroder Straße 5, D-38104 Braunschweig, Germany. wargenau@a-wargenau.de
2012-08-31T14:35:10Z
2012-08-31T14:35:10Z
2011-12
On the origin of the electrostatic surface potential of Aspergillus niger spores in acidic environments. 2011, 162 (10):1011-7 Res. Microbiol.
1769-7123
21835241
10.1016/j.resmic.2011.07.006
http://hdl.handle.net/10033/240838
Research in microbiology
The electrostatic surface potential of fungal spores is generally regarded as potentially influencing spore aggregation and pellet formation in submerged cultures of filamentous fungi. Spores of Aspergillus niger are typically characterized by negative zeta potentials over a wide range of pH values. In this study, this particular behavior is ascribed to the presence of an extensive melanin coating. It is proposed on the basis of zeta potential and pigment extraction experiments that this outermost layer affects the pH-dependent surface potential in two manners: (i) by the addition of negative charges to the spore surface and (ii) by the pH-dependent release of melanin pigment. Chemical analyses revealed that deprotonation of melanin-bound carboxyl groups is most probably responsible for pigment release under acidic conditions. These findings were incorporated into a simple model which has the ability to qualitatively explain the results of zeta potential experiments and, moreover, to provide the basis for quantitative investigations on the role of electrostatics in spore aggregation.
en
Archived with thanks to Research in microbiology
Aspergillus niger
Environment
Hydrogen-Ion Concentration
Melanins
Microscopy, Electron, Transmission
Spores, Fungal
Static Electricity
Surface Properties
On the origin of the electrostatic surface potential of Aspergillus niger spores in acidic environments.
Article
2018-06-13T03:55:49Z
The electrostatic surface potential of fungal spores is generally regarded as potentially influencing spore aggregation and pellet formation in submerged cultures of filamentous fungi. Spores of Aspergillus niger are typically characterized by negative zeta potentials over a wide range of pH values. In this study, this particular behavior is ascribed to the presence of an extensive melanin coating. It is proposed on the basis of zeta potential and pigment extraction experiments that this outermost layer affects the pH-dependent surface potential in two manners: (i) by the addition of negative charges to the spore surface and (ii) by the pH-dependent release of melanin pigment. Chemical analyses revealed that deprotonation of melanin-bound carboxyl groups is most probably responsible for pigment release under acidic conditions. These findings were incorporated into a simple model which has the ability to qualitatively explain the results of zeta potential experiments and, moreover, to provide the basis for quantitative investigations on the role of electrostatics in spore aggregation.
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Backert, Steffen
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From the School for Medicine and Medical Science, University College Dublin, Belfield Campus, Dublin-4, Ireland. Steffen.Backert@ucd.ie.
2012-09-14T08:23:31Z
2012-09-14T08:23:31Z
2012
Rapid paracellular transmigration of Campylobacter jejuni across polarized epithelial cells without affecting TER: role of proteolytic-active HtrA cleaving E-cadherin but not fibronectin. 2012, 4 (1):3 Gut Pathog
1757-4749
22534208
10.1186/1757-4749-4-3
http://hdl.handle.net/10033/243991
Gut pathogens
ABSTRACT:
en
Archived with thanks to Gut pathogens
Rapid paracellular transmigration of Campylobacter jejuni across polarized epithelial cells without affecting TER: role of proteolytic-active HtrA cleaving E-cadherin but not fibronectin.
Article
2018-06-12T17:58:05Z
ABSTRACT:
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2019-08-30 11:27:46.419
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oai:repository.helmholtz-hzi.de:10033/2443322019-08-30T11:26:42Zcom_10033_6815com_10033_6814col_10033_6886
Haggar, Axana
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Nerlich, Andreas
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Kumar, Rajesh
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Abraham, Vinod J
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Brahmadathan, Kootallur N
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Ray, Pallab
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Dhanda, Vanita
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Joshua, John Melbin Jose
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Mehra, Narinder
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Bergmann, Rene
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Chhatwal, G Singh
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Norrby-Teglund, Anna
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Center for Infectious Medicine, Karolinska Institutet, Stockholm, Sweden.
2012-09-17T14:05:47Z
2012-09-17T14:05:47Z
2012-05
Clinical and microbiologic characteristics of invasive Streptococcus pyogenes infections in north and south India. 2012, 50 (5):1626-31 J. Clin. Microbiol.
1098-660X
22357508
10.1128/JCM.06697-11
http://hdl.handle.net/10033/244332
Journal of clinical microbiology
The lack of epidemiologic data on invasive Streptococcus pyogenes infections in many developing countries is concerning, as S. pyogenes infections are commonly endemic in these areas. Here we present the results of the first prospective surveillance study of invasive Streptococcus pyogenes infections in India. Fifty-four patients with invasive S. pyogenes infections were prospectively enrolled at two study sites, one in the north and one in the south of India. Sterile-site isolates were collected, and clinical information was documented using a standardized questionnaire. Available acute-phase sera were tested for their ability to inhibit superantigens produced by the patient's own isolate using a cell-based neutralizing assay. The most common clinical presentations were bacteremia without focus (30%), pneumonia (28%), and cellulitis (17%). Only two cases of streptococcal toxic shock syndrome and no cases of necrotizing fasciitis were identified. Characterization of the isolates revealed great heterogeneity, with 32 different emm subtypes and 29 different superantigen gene profiles being represented among the 49 sterile-site isolates. Analyses of acute-phase sera showed that only 20% of the cases in the north cohort had superantigen-neutralizing activity in their sera, whereas 50% of the cases from the south site had neutralizing activity. The results demonstrate that there are important differences in both clinical presentation and strain characteristics between invasive S. pyogenes infections in India and invasive S. pyogenes infections in Western countries. The findings underscore the importance of epidemiologic studies on streptococcal infections in India and have direct implications for current vaccine developments.
en
Archived with thanks to Journal of clinical microbiology
Adolescent
Adult
Aged
Aged, 80 and over
Antibodies, Bacterial
Antibodies, Neutralizing
Child
Child, Preschool
Female
Genotype
Humans
India
Infant
Infant, Newborn
Male
Middle Aged
Molecular Epidemiology
Questionnaires
Serotyping
Streptococcal Infections
Streptococcus pyogenes
Superantigens
Young Adult
Clinical and microbiologic characteristics of invasive Streptococcus pyogenes infections in north and south India.
Article
2018-06-12T16:43:42Z
The lack of epidemiologic data on invasive Streptococcus pyogenes infections in many developing countries is concerning, as S. pyogenes infections are commonly endemic in these areas. Here we present the results of the first prospective surveillance study of invasive Streptococcus pyogenes infections in India. Fifty-four patients with invasive S. pyogenes infections were prospectively enrolled at two study sites, one in the north and one in the south of India. Sterile-site isolates were collected, and clinical information was documented using a standardized questionnaire. Available acute-phase sera were tested for their ability to inhibit superantigens produced by the patient's own isolate using a cell-based neutralizing assay. The most common clinical presentations were bacteremia without focus (30%), pneumonia (28%), and cellulitis (17%). Only two cases of streptococcal toxic shock syndrome and no cases of necrotizing fasciitis were identified. Characterization of the isolates revealed great heterogeneity, with 32 different emm subtypes and 29 different superantigen gene profiles being represented among the 49 sterile-site isolates. Analyses of acute-phase sera showed that only 20% of the cases in the north cohort had superantigen-neutralizing activity in their sera, whereas 50% of the cases from the south site had neutralizing activity. The results demonstrate that there are important differences in both clinical presentation and strain characteristics between invasive S. pyogenes infections in India and invasive S. pyogenes infections in Western countries. The findings underscore the importance of epidemiologic studies on streptococcal infections in India and have direct implications for current vaccine developments.
ORIGINAL
Haggar et al_final.pdf
Haggar et al_final.pdf
original manuscript
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supplemental table 1
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CC-LICENSE
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THUMBNAIL
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oai:repository.helmholtz-hzi.de:10033/2458122019-08-30T11:27:46Zcom_10033_6815com_10033_6814col_10033_6886
Seitz, Maren
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Beineke, Andreas
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Fulde, Marcus
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1Institute for Microbiology, University of Veterinary Medicine Hannover, Hannover, Germany.
2012-09-25T14:41:28Z
2012-09-25T14:41:28Z
2012-09
A novel intranasal mouse model for mucosal colonization by Streptococcus suis serotype 2. 2012, 61 (Pt 9):1311-8 J. Med. Microbiol.
1473-5644
22556325
10.1099/jmm.0.043885-0
http://hdl.handle.net/10033/245812
Journal of medical microbiology
Streptococcus suis causes meningitis and various other diseases in pigs and humans. Healthy piglets carrying virulent Streptococcus suis strains on their mucosal surfaces are epidemiologically very important. The objective of this study was to establish an intranasal Streptococcus suis mouse model for invasion and colonization of the respiratory tract. CD1 mice were infected intranasally with a highly virulent Streptococcus suis serotype 2 strain under different conditions. Clinical, histological and bacteriological screenings revealed that invasion of host tissue occurred in the majority of mice only after predisposition with 12.5 µl 1 % acetic acid per nostril. Severe fibrinosuppurative or purulent necrotizing pneumonia associated with Streptococcus suis was a common manifestation. Furthermore, a novel model to study nasopharyngeal colonization was established by reducing the volume of 1 % acetic acid per nostril to 5 µl prior to Streptococcus suis application. This model mimics asymptomatic carriage in swine, as all mice carried Streptococcus suis on their respiratory mucosa at 7 days post-infection (p.i.) in moderate to high numbers without the development of pneumonia or any other invasive Streptococcus suis disease. This intranasal Streptococcus suis model was applied to investigate the function of suilysin (SLY) in colonization. Although an isogenic SLY mutant was isolated from the upper respiratory tract at a lower recovery rate than its wild-type parental strain at 14 days p.i., the differences were not significant and did not indicate severe attenuation in colonization. In conclusion, this work describes to the best of our knowledge the first intranasal mouse model to study colonization of the respiratory tract by a highly virulent Streptococcus suis pathotype.
en
Archived with thanks to Journal of medical microbiology
A novel intranasal mouse model for mucosal colonization by Streptococcus suis serotype 2.
Article
2013-09-15T00:00:00Z
Streptococcus suis causes meningitis and various other diseases in pigs and humans. Healthy piglets carrying virulent Streptococcus suis strains on their mucosal surfaces are epidemiologically very important. The objective of this study was to establish an intranasal Streptococcus suis mouse model for invasion and colonization of the respiratory tract. CD1 mice were infected intranasally with a highly virulent Streptococcus suis serotype 2 strain under different conditions. Clinical, histological and bacteriological screenings revealed that invasion of host tissue occurred in the majority of mice only after predisposition with 12.5 µl 1 % acetic acid per nostril. Severe fibrinosuppurative or purulent necrotizing pneumonia associated with Streptococcus suis was a common manifestation. Furthermore, a novel model to study nasopharyngeal colonization was established by reducing the volume of 1 % acetic acid per nostril to 5 µl prior to Streptococcus suis application. This model mimics asymptomatic carriage in swine, as all mice carried Streptococcus suis on their respiratory mucosa at 7 days post-infection (p.i.) in moderate to high numbers without the development of pneumonia or any other invasive Streptococcus suis disease. This intranasal Streptococcus suis model was applied to investigate the function of suilysin (SLY) in colonization. Although an isogenic SLY mutant was isolated from the upper respiratory tract at a lower recovery rate than its wild-type parental strain at 14 days p.i., the differences were not significant and did not indicate severe attenuation in colonization. In conclusion, this work describes to the best of our knowledge the first intranasal mouse model to study colonization of the respiratory tract by a highly virulent Streptococcus suis pathotype.
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oai:repository.helmholtz-hzi.de:10033/2461312019-08-30T11:28:24Zcom_10033_6815com_10033_6814col_10033_6886
Herrmann, Jennifer
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500
Elnakady, Yasser A
a45afefa71fae62d126d6d72e8dcf0f0
500
Wiedmann, Romina M
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Ullrich, Angelika
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Rohde, Manfred
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Kazmaier, Uli
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Vollmar, Angelika M
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Müller, Rolf
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Helmholtz Institute for Pharmaceutical Research Saarland, Helmholtz Centre for Infection Research and Department of Pharmaceutical Biotechnology, Saarland University, Saarbrücken, Germany.
2012-09-27T09:11:28Z
2012-09-27T09:11:28Z
2012
Pretubulysin: from hypothetical biosynthetic intermediate to potential lead in tumor therapy. 2012, 7 (5):e37416 PLoS ONE
1932-6203
22616003
10.1371/journal.pone.0037416
http://hdl.handle.net/10033/246131
PloS one
Pretubulysin is a natural product that is found in strains of myxobacteria in only minute amounts. It represents the first enzyme-free intermediate in the biosynthesis of tubulysins and undergoes post-assembly acylation and oxidation reactions. Pretubulysin inhibits the growth of cultured mammalian cells, as do tubulysins, which are already in advanced preclinical development as anticancer and antiangiogenic agents. The mechanism of action of this highly potent compound class involves the depolymerization of microtubules, thereby inducing mitotic arrest. Supply issues with naturally occurring derivatives can now be circumvented by the total synthesis of pretubulysin, which, in contrast to tubulysin, is synthetically accessible in gram-scale quantities. We show that the simplified precursor is nearly equally potent to the parent compound. Pretubulysin induces apoptosis and inhibits cancer cell migration and tubulin assembly in vitro. Consequently, pretubulysin appears to be an ideal candidate for future development in preclinical trials and is a very promising early lead structure in cancer therapy.
en
Archived with thanks to PloS one
Angiogenesis Inhibitors
Animals
Antineoplastic Agents
Apoptosis
Cell Line, Tumor
Cell Migration Inhibition
Hep G2 Cells
Humans
Mice
Microtubules
Mitosis
Myxococcales
Oligopeptides
Proto-Oncogene Proteins c-bcl-2
Tubulin
Pretubulysin: from hypothetical biosynthetic intermediate to potential lead in tumor therapy.
Article
2018-06-13T19:54:23Z
Pretubulysin is a natural product that is found in strains of myxobacteria in only minute amounts. It represents the first enzyme-free intermediate in the biosynthesis of tubulysins and undergoes post-assembly acylation and oxidation reactions. Pretubulysin inhibits the growth of cultured mammalian cells, as do tubulysins, which are already in advanced preclinical development as anticancer and antiangiogenic agents. The mechanism of action of this highly potent compound class involves the depolymerization of microtubules, thereby inducing mitotic arrest. Supply issues with naturally occurring derivatives can now be circumvented by the total synthesis of pretubulysin, which, in contrast to tubulysin, is synthetically accessible in gram-scale quantities. We show that the simplified precursor is nearly equally potent to the parent compound. Pretubulysin induces apoptosis and inhibits cancer cell migration and tubulin assembly in vitro. Consequently, pretubulysin appears to be an ideal candidate for future development in preclinical trials and is a very promising early lead structure in cancer therapy.
ORIGINAL
herrmann,jennifer et al_final.pdf
herrmann,jennifer et al_final.pdf
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2019-08-30 11:28:24.052
Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/2461322019-08-30T11:27:46Zcom_10033_6815com_10033_6814col_10033_6886
Wollein Waldetoft, Kristofer
dc2902609309c098e17ea630748a3e50
500
Svensson, Lisbeth
912a06118b411332e64017024bd8ecf4
500
Mörgelin, Matthias
3b24bbdfdbc2401bc3afa6678a7b152e
500
Olin, Anders I
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Nitsche-Schmitz, D Patric
cb8c9f97bad4b6ed57d10ef22331a3f4
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Björck, Lars
edbbb91a692d5f0833b117bc7357fd3b
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Frick, Inga-Maria
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Division of Infection Medicine, Department of Clinical Sciences, Lund University, SE-221 84 Lund, Sweden. kristofer.wollein_waldetoft@med.lu.se
2012-09-27T09:54:17Z
2012-09-27T09:54:17Z
2012-07-20
Streptococcal surface proteins activate the contact system and control its antibacterial activity. 2012, 287 (30):25010-8 J. Biol. Chem.
1083-351X
22648411
10.1074/jbc.M112.373217
http://hdl.handle.net/10033/246132
The Journal of biological chemistry
Group G streptococci (GGS) are important bacterial pathogens in humans. Here, we investigated the interactions between GGS and the contact system, a procoagulant and proinflammatory proteolytic cascade that, upon activation, also generates antibacterial peptides. Two surface proteins of GGS, protein FOG and protein G (PG), were found to bind contact system proteins. Experiments utilizing contact protein-deficient human plasma and isogenic GGS mutant strains lacking FOG or PG showed that FOG and PG both activate the procoagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen, generating the proinflammatory bradykinin peptide and additional high molecular weight kininogen fragments containing the antimicrobial peptide NAT-26. On the other hand, PG protected the bacteria against the antibacterial effect of NAT-26. These findings underline the significance of the contact system in innate immunity and demonstrate that GGS have evolved surface proteins to exploit and modulate its effects.
en
Archived with thanks to The Journal of biological chemistry
Streptococcal surface proteins activate the contact system and control its antibacterial activity.
Article
2018-06-13T19:47:23Z
Group G streptococci (GGS) are important bacterial pathogens in humans. Here, we investigated the interactions between GGS and the contact system, a procoagulant and proinflammatory proteolytic cascade that, upon activation, also generates antibacterial peptides. Two surface proteins of GGS, protein FOG and protein G (PG), were found to bind contact system proteins. Experiments utilizing contact protein-deficient human plasma and isogenic GGS mutant strains lacking FOG or PG showed that FOG and PG both activate the procoagulant branch of the contact system. In contrast, only FOG induced cleavage of high molecular weight kininogen, generating the proinflammatory bradykinin peptide and additional high molecular weight kininogen fragments containing the antimicrobial peptide NAT-26. On the other hand, PG protected the bacteria against the antibacterial effect of NAT-26. These findings underline the significance of the contact system in innate immunity and demonstrate that GGS have evolved surface proteins to exploit and modulate its effects.
ORIGINAL
Wollein Waldetoft et al_final.pdf
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Helmholtz Zentrum für Infektionsforschung Repository
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2012-10-04T10:21:23Z
2012-10-04T10:21:23Z
2012-03-19
Complete genome sequence of the sulfur compounds oxidizing chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)). 2012, 6 (1):94-103 Stand Genomic Sci
1944-3277
22675602
10.4056/sigs.2456004
http://hdl.handle.net/10033/246991
Standards in genomic sciences
Sulfuricurvum kujiense Kodama and Watanabe 2004 is the type species of the monotypic genus Sulfuricurvum, which belongs to the family Helicobacteraceae in the class Epsilonproteobacteria. The species is of interest because it is frequently found in crude oil and oil sands where it utilizes various reduced sulfur compounds such as elemental sulfur, sulfide and thiosulfate as electron donors. Members of the species do not utilize sugars, organic acids or hydrocarbons as carbon and energy sources. This genome sequence represents the type strain of the only species in the genus Sulfuricurvum. The genome, which consists of a circular chromosome of 2,574,824 bp length and four plasmids of 118,585 bp, 71,513 bp, 51,014 bp, and 3,421 bp length, respectively, harboring a total of 2,879 protein-coding and 61 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the sulfur compounds oxidizing chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).
Article
2018-06-13T15:17:47Z
Sulfuricurvum kujiense Kodama and Watanabe 2004 is the type species of the monotypic genus Sulfuricurvum, which belongs to the family Helicobacteraceae in the class Epsilonproteobacteria. The species is of interest because it is frequently found in crude oil and oil sands where it utilizes various reduced sulfur compounds such as elemental sulfur, sulfide and thiosulfate as electron donors. Members of the species do not utilize sugars, organic acids or hydrocarbons as carbon and energy sources. This genome sequence represents the type strain of the only species in the genus Sulfuricurvum. The genome, which consists of a circular chromosome of 2,574,824 bp length and four plasmids of 118,585 bp, 71,513 bp, 51,014 bp, and 3,421 bp length, respectively, harboring a total of 2,879 protein-coding and 61 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2019-08-30 11:28:23.731
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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2012-10-04T14:33:06Z
2011-12-31
Complete genome sequence of the thermophilic sulfur-reducer Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea hydrothermal vent. 2011, 5 (3):407-15 Stand Genomic Sci
1944-3277
22675590
10.4056/sigs.2465574
http://hdl.handle.net/10033/247011
Standards in genomic sciences
Desulfurobacterium thermolithotrophum L'Haridon et al. 1998 is the type species of the genus Desulfurobacterium which belongs to the family Desulfurobacteriaceae. The species is of interest because it represents the first thermophilic bacterium that can act as a primary producer in the temperature range of 45-75 °C (optimum 70°C) and is incapable of growing under microaerophilic conditions. Strain BSA(T) preferentially synthesizes high-melting-point fatty acids (C(18) and C(20)) which is hypothesized to be a strategy to ensure the functionality of the membrane at high growth temperatures. This is the second completed genome sequence of a member of the family Desulfurobacteriaceae and the first sequence from the genus Desulfurobacterium. The 1,541,968 bp long genome harbors 1,543 protein-coding and 51 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Complete genome sequence of the thermophilic sulfur-reducer Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea hydrothermal vent.
Article
2018-06-13T16:02:38Z
Desulfurobacterium thermolithotrophum L'Haridon et al. 1998 is the type species of the genus Desulfurobacterium which belongs to the family Desulfurobacteriaceae. The species is of interest because it represents the first thermophilic bacterium that can act as a primary producer in the temperature range of 45-75 °C (optimum 70°C) and is incapable of growing under microaerophilic conditions. Strain BSA(T) preferentially synthesizes high-melting-point fatty acids (C(18) and C(20)) which is hypothesized to be a strategy to ensure the functionality of the membrane at high growth temperatures. This is the second completed genome sequence of a member of the family Desulfurobacteriaceae and the first sequence from the genus Desulfurobacterium. The 1,541,968 bp long genome harbors 1,543 protein-coding and 51 RNA genes and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
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2012-05-25
Permanent draft genome sequence of the gliding predator Saprospira grandis strain Sa g1 (= HR1). 2012, 6 (2):210-9 Stand Genomic Sci
1944-3277
22768364
10.4056/sigs.2816096
http://hdl.handle.net/10033/247131
Standards in genomic sciences
Saprospira grandis Gross 1911 is a member of the Saprospiraceae, a family in the class 'Sphingobacteria' that remains poorly characterized at the genomic level. The species is known for preying on other marine bacteria via 'ixotrophy'. S. grandis strain Sa g1 was isolated from decaying crab carapace in France and was selected for genome sequencing because of its isolated location in the tree of life. Only one type strain genome has been published so far from the Saprospiraceae, while the sequence of strain Sa g1 represents the second genome to be published from a non-type strain of S. grandis. Here we describe the features of this organism, together with the complete genome sequence and annotation. The 4,495,250 bp long Improved-High-Quality draft of the genome with its 3,536 protein-coding and 62 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
en
Archived with thanks to Standards in genomic sciences
Permanent draft genome sequence of the gliding predator Saprospira grandis strain Sa g1 (= HR1).
Article
2018-06-12T23:55:07Z
Saprospira grandis Gross 1911 is a member of the Saprospiraceae, a family in the class 'Sphingobacteria' that remains poorly characterized at the genomic level. The species is known for preying on other marine bacteria via 'ixotrophy'. S. grandis strain Sa g1 was isolated from decaying crab carapace in France and was selected for genome sequencing because of its isolated location in the tree of life. Only one type strain genome has been published so far from the Saprospiraceae, while the sequence of strain Sa g1 represents the second genome to be published from a non-type strain of S. grandis. Here we describe the features of this organism, together with the complete genome sequence and annotation. The 4,495,250 bp long Improved-High-Quality draft of the genome with its 3,536 protein-coding and 62 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
ORIGINAL
Mavromatis et al_final.pdf
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2012-05-25
Genome sequence of the ocean sediment bacterium Saccharomonospora marina type strain (XMU15(T)). 2012, 6 (2):265-75 Stand Genomic Sci
1944-3277
22768369
10.4056/sigs.2655905
http://hdl.handle.net/10033/247140
Standards in genomic sciences
Saccharomonospora marina Liu et al. 2010 is a member of the genus Saccharomonospora, in the family Pseudonocardiaceae that is poorly characterized at the genome level thus far. Members of the genus Saccharomonospora are of interest because they originate from diverse habitats, such as leaf litter, manure, compost, surface of peat, moist, over-heated grain, and ocean sediment, where they might play a role in the primary degradation of plant material by attacking hemicellulose. Organisms belonging to the genus are usually Gram-positive staining, non-acid fast, and classify among the actinomycetes. Here we describe the features of this organism, together with the complete genome sequence (permanent draft status), and annotation. The 5,965,593 bp long chromosome with its 5,727 protein-coding and 57 RNA genes was sequenced as part of the DOE funded Community Sequencing Program (CSP) 2010 at the Joint Genome Institute (JGI).
en
Archived with thanks to Standards in genomic sciences
Genome sequence of the ocean sediment bacterium Saccharomonospora marina type strain (XMU15(T)).
Article
2018-06-12T18:08:58Z
Saccharomonospora marina Liu et al. 2010 is a member of the genus Saccharomonospora, in the family Pseudonocardiaceae that is poorly characterized at the genome level thus far. Members of the genus Saccharomonospora are of interest because they originate from diverse habitats, such as leaf litter, manure, compost, surface of peat, moist, over-heated grain, and ocean sediment, where they might play a role in the primary degradation of plant material by attacking hemicellulose. Organisms belonging to the genus are usually Gram-positive staining, non-acid fast, and classify among the actinomycetes. Here we describe the features of this organism, together with the complete genome sequence (permanent draft status), and annotation. The 5,965,593 bp long chromosome with its 5,727 protein-coding and 57 RNA genes was sequenced as part of the DOE funded Community Sequencing Program (CSP) 2010 at the Joint Genome Institute (JGI).
ORIGINAL
Klenk et al_final.pdf
Klenk et al_final.pdf
Open Access publication
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Helmholtz Zentrum für Infektionsforschung Repository
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Branitzki-Heinemann, Katja
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Okumura, Cheryl Y
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Völlger, Lena
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Kawakami, Yuko
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Kawakami, Toshiaki
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Naim, Hassan Y
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Nizet, Victor
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Von Köckritz-Blickwede, Maren
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Department of Pediatrics, University of California San Diego, La Jolla, CA 92093, USA.
2012-10-08T12:37:28Z
2012-10-08T12:37:28Z
2012-08-15
A novel role for the transcription factor HIF-1α in the formation of mast cell extracellular traps. 2012, 446 (1):159-63 Biochem. J.
1470-8728
22738198
10.1042/BJ20120658
http://hdl.handle.net/10033/247551
The Biochemical journal
MCs (mast cells) are critical components of the host innate immune defence against bacterial pathogens, providing a variety of intra- and extra-cellular antimicrobial functions. In the present study we show, for the first time, that the transcriptional regulator HIF-1α (hypoxia-inducible factor-1α) mediates the extracellular antimicrobial activity of human and murine MCs by increasing the formation of MCETs (MC extracellular traps).
en
Archived with thanks to The Biochemical journal
A novel role for the transcription factor HIF-1α in the formation of mast cell extracellular traps.
Article
2013-02-15T00:00:00Z
MCs (mast cells) are critical components of the host innate immune defence against bacterial pathogens, providing a variety of intra- and extra-cellular antimicrobial functions. In the present study we show, for the first time, that the transcriptional regulator HIF-1α (hypoxia-inducible factor-1α) mediates the extracellular antimicrobial activity of human and murine MCs by increasing the formation of MCETs (MC extracellular traps).
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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