2024-03-28T08:40:19Zhttp://repository.helmholtz-hzi.de/oai/requestoai:repository.helmholtz-hzi.de:10033/84062019-08-30T11:32:37Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Goodfellow, Alison M.
author
Hibble, Megan
author
Talay, Susanne R.
author
Kreikemeyer, Bernd
author
Currie, Bart J.
author
Sriprakash, Kadaba S.
author
Chhatwal, Gursharan S.
2007-02-14T15:47:11Z
2000-01
Journal of Clinical Microbiology 2000 38(1):389-392
0095-1137
10618121
http://hdl.handle.net/10033/8406
88729
en_US
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
URL
https://hzi.openrepository.com/bitstream/10033/8406/1/Godfellow%20et%20al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8406/7/Godfellow%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/85072019-08-30T11:32:38Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Dominik, Katja
author
Höfle, Manfred G.
2007-02-19T09:14:13Z
2002-07
Applied and Environmental Microbiology 2002 68(7):3606-3613
0099-2240
12089049
10.1128/AEM.68.7.3606-3613.2002
http://hdl.handle.net/10033/8507
126806
en_US
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
URL
https://hzi.openrepository.com/bitstream/10033/8507/1/Dominik%20and%20H%c3%b6fle_final.pdf
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Dominik and Höfle_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8507/7/Dominik%20and%20H%c3%b6fle_final.pdf.txt
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Dominik and Höfle_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/85092019-08-30T11:32:38Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Jansen, W. T. M.
author
Bolm, M.
author
Balling, R.
author
Chhatwal, G. S.
author
Schnabel, R.
2007-02-19T09:20:40Z
2002-09
Infection and Immunity 2002 70(9):5202-5207
0019-9567
12183571
10.1128/IAI.70.9.5202-5207.2002
http://hdl.handle.net/10033/8509
128270
en_US
Copyright © 2002, American Society for Microbiology
Hydrogen Peroxide-Mediated Killing of Caenorhabditis elegans by Streptococcus pyogenes
URL
https://hzi.openrepository.com/bitstream/10033/8509/1/Jansen%20et%20al_final.pdf
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MD5
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Jansen et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8509/7/Jansen%20et%20al_final.pdf.txt
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Jansen et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/85002019-08-30T11:32:38Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Erdogan, Sezgin
author
Fagan, Peter K.
author
Talay, Susanne R.
author
Rohde, Manfred
author
Ferrieri, Patricia
author
Flores, Aurea E.
author
Guzmán, Carlos A.
author
Walker, Mark J.
author
Chhatwal, Gursharan S.
2007-02-19T08:48:58Z
2002-02
Infection and Immunity 2002 70(2):803-811
0019-9567
11796614
http://hdl.handle.net/10033/8500
127721
en_US
Copyright © 2002, American Society for Microbiology
Molecular Analysis of Group B Protective Surface Protein, a New Cell Surface Protective Antigen of Group B Streptococci
URL
https://hzi.openrepository.com/bitstream/10033/8500/1/Erdogan%20et%20al_final.pdf
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Erdogan et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8500/7/Erdogan%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/86112019-08-30T11:32:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Barthel, Manja
author
Hapfelmeier, Siegfried
author
Quintanilla-Martínez, Leticia
author
Kremer, Marcus
author
Rohde, Manfred
author
Hogardt, Michael
author
Pfeffer, Klaus
author
Rüssmann, Holger
author
Hardt, Wolf-Dietrich
2007-02-20T13:07:06Z
2003-05
Infection and Immunity 2003 71(5):2839-2858
0019-9567
12704158
10.1128/IAI.71.5.2839-2858.2003
http://hdl.handle.net/10033/8611
153285
en_US
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
URL
https://hzi.openrepository.com/bitstream/10033/8611/1/Barthel%20et%20al_final.pdf
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Barthel et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8611/7/Barthel%20et%20al_final.pdf.txt
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Barthel et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86182019-08-30T11:32:39Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Guzman, C A
author
Rohde, M
author
Chakraborty, T
author
Domann, E
author
Hudel, M
author
Wehland, J
author
Timmis, K N
2007-02-20T13:12:44Z
1995-09
Infection and Immunity 1995 63(9):3665-3673
0019-9567
7642305
http://hdl.handle.net/10033/8618
173508
en_US
Interaction of Listeria monocytogenes with mouse dendritic cells.
URL
https://hzi.openrepository.com/bitstream/10033/8618/1/Guzman%20et%20al_final.pdf
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Guzman et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8618/7/Guzman%20et%20al_final.pdf.txt
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Guzman et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/85312019-08-30T11:32:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Valenti-Weigand, P
author
Benkel, P
author
Rohde, Manfred
author
Chhatwal, G S
2007-02-19T10:37:07Z
1996-07
Infection and Immunity 1996 64(7):2467-2473
0019-9567
8698468
http://hdl.handle.net/10033/8531
174099
en_US
Entry and intracellular survival of group B streptococci in J774 macrophages.
URL
https://hzi.openrepository.com/bitstream/10033/8531/1/Valenti-Weigand%20et%20al.final.pdf
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MD5
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Valenti-Weigand et al.final.pdf
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https://hzi.openrepository.com/bitstream/10033/8531/7/Valenti-Weigand%20et%20al.final.pdf.txt
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Valenti-Weigand et al.final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/85322019-08-30T11:32:15Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Jerlström, P G
author
Talay, S R
author
Valentin-Weigand, P
author
Timmis, K N
author
Chhatwal, G S
2007-02-19T10:37:53Z
1996-07
Infection and Immunity 1996 64(7):2787-2793
0019-9567
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.
URL
https://hzi.openrepository.com/bitstream/10033/8532/1/Jerlstr%c3%b6m%20et%20al_final.pdf
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Jerlström et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8532/7/Jerlstr%c3%b6m%20et%20al_final.pdf.txt
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Jerlström et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/85342019-08-30T11:24:30Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Molinari, Gabriella
author
Talay, S R
author
Valentin-Weigand, P
author
Rohde, Manfred
author
Chhatwal, G S
2007-02-19T10:39:27Z
1997-04
Infection and Immunity 1997 65(4):1357-1363
0019-9567
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.
URL
https://hzi.openrepository.com/bitstream/10033/8534/1/Molinari%20et%20al_final.pdf
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MD5
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Molinari et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8534/7/Molinari%20et%20al_final.pdf.txt
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Molinari et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/85362019-08-30T11:24:30Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Dinkla, Katrin
author
Rohde, Manfred
author
Jansen, Wouter T.M.
author
Kaplan, Edward L.
author
Chhatwal, Gursharan S.
author
Talay, Susanne R.
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
Copyright © 2003, American Society for Clinical Investigation
Rheumatic fever–associated Streptococcus pyogenes isolates aggregate collagen
URL
https://hzi.openrepository.com/bitstream/10033/8536/1/Dinkla%20et%20al_final.pdf
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MD5
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Dinkla et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8536/7/Dinkla%20et%20al_final.pdf.txt
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Dinkla et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86352019-08-30T11:32:40Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Lünsdorf, H
author
Schairer, H U
author
Heidelbach, M
2007-02-20T13:31:37Z
1995-12
Journal of Bacteriology 1995 177(24):7092-7099
0021-9193
8522514
http://hdl.handle.net/10033/8635
177586
en_US
Localization of the stress protein SP21 in indole-induced spores, fruiting bodies, and heat-shocked cells of Stigmatella aurantiaca.
URL
https://hzi.openrepository.com/bitstream/10033/8635/1/lunsdorf%20et%20al_final.pdf
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MD5
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lunsdorf et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8635/7/lunsdorf%20et%20al_final.pdf.txt
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lunsdorf et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86382019-08-30T11:32:16Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Klee, S R
author
Tzschaschel, B D
author
Timmis, K N
author
Guzman, C A
2007-02-20T13:33:51Z
1997-04
Journal of Bacteriology 1997 179(7):2421-2425
0021-9193
9079931
http://hdl.handle.net/10033/8638
178982
en_US
Influence of different rol gene products on the chain length of Shigella dysenteriae type 1 lipopolysaccharide O antigen expressed by Shigella flexneri carrier strains.
URL
https://hzi.openrepository.com/bitstream/10033/8638/7/Klee%20et%20al_final.pdf
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MD5
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Klee et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8638/13/Klee%20et%20al_final.pdf.txt
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Klee et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86392019-08-30T11:32:40Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Medina, Eva
author
Rohde, Manfred
author
Chhatwal, Gursharan S.
2007-02-20T13:34:24Z
2003-09
Infection and Immunity 2003 71(9):5376-5380
0019-9567
12933887
10.1128/IAI.71.9.5376-5380.2003
http://hdl.handle.net/10033/8639
187312
en_US
Copyright © 2003, American Society for Microbiology
Intracellular Survival of Streptococcus pyogenes in Polymorphonuclear Cells Results in Increased Bacterial Virulence
URL
https://hzi.openrepository.com/bitstream/10033/8639/1/Medina%20et%20al_final.pdf
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MD5
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Medina et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8639/7/Medina%20et%20al_final.pdf.txt
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Medina et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86032019-08-30T11:24:31Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Su, G F
author
Brahmbhatt, H N
author
Wehland, J
author
Rohde, Manfred
author
Timmis, K N
2007-02-20T12:56:07Z
1992-08
Infection and Immunity 1992 60(8):3345-3359
0019-9567
1639503
http://hdl.handle.net/10033/8603
257321
Images
en_US
Construction of stable LamB-Shiga toxin B subunit hybrids: analysis of expression in Salmonella typhimurium aroA strains and stimulation of B subunit-specific mucosal and serum antibody responses.
URL
https://hzi.openrepository.com/bitstream/10033/8603/1/Su%20et%20al_final.pdf
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Su et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8603/7/Su%20et%20al_final.pdf.txt
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Su et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86042019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Talay, S R
author
Valentin-Weigand, P
author
Jerlström, P G
author
Timmis, K N
author
Chhatwal, G S
2007-02-20T12:56:42Z
1992-09
Infection and Immunity 1992 60(9):3837-3844
0019-9567
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.
URL
https://hzi.openrepository.com/bitstream/10033/8604/1/Talay%20et%20al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8604/7/Talay%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/86062019-08-30T11:24:31Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Walker, M J
author
Guzmán, C A
author
Rohde, Manfred
author
Timmis, K N
2007-02-20T12:59:02Z
1991-05
Infection and Immunity 1991 59(5):1739-1746
0019-9567
1708358
http://hdl.handle.net/10033/8606
257910
Images
en_US
Production of recombinant Bordetella pertussis serotype 2 fimbriae in Bordetella parapertussis and Bordetella bronchiseptica: utility of Escherichia coli gene expression signals.
URL
https://hzi.openrepository.com/bitstream/10033/8606/1/Walker%20et%20al_final.pdf
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Walker et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86082019-08-30T11:24:31Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Kadurugamuwa, J L
author
Rohde, Manfred
author
Wehland, J
author
Timmis, K N
2007-02-20T13:01:01Z
1991-10
Infection and Immunity 1991 59(10):3463-3471
0019-9567
1910001
http://hdl.handle.net/10033/8608
258907
Images
en_US
Intercellular spread of Shigella flexneri through a monolayer mediated by membranous protrusions and associated with reorganization of the cytoskeletal protein vinculin.
URL
https://hzi.openrepository.com/bitstream/10033/8608/1/Kadurugamuwa%20et%20al_final.pdf
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Kadurugamuwa et al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/8608/7/Kadurugamuwa%20et%20al_final.pdf.txt
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Kadurugamuwa et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86092019-08-30T11:25:43Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Guzmán, C A
author
Walker, M J
author
Rohde, Manfred
author
Timmis, K N
2007-02-20T13:01:36Z
1991-10
Infection and Immunity 1991 59(10):3787-3795
0019-9567
1716615
http://hdl.handle.net/10033/8609
258952
Images
en_US
Direct expression of Bordetella pertussis filamentous hemagglutinin in Escherichia coli and Salmonella typhimurium aroA.
URL
https://hzi.openrepository.com/bitstream/10033/8609/1/Guzman%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/86192019-08-30T11:25:11Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Walker, M J
author
Rohde, Manfred
author
Wehland, J
author
Timmis, K N
2007-02-20T13:15:13Z
1991-11
Infection and Immunity 1991 59(11):4238-4248
0019-9567
1682257
http://hdl.handle.net/10033/8619
259022
Images
en_US
Construction of minitransposons for constitutive and inducible expression of pertussis toxin in bvg-negative Bordetella bronchiseptica.
URL
https://hzi.openrepository.com/bitstream/10033/8619/1/Walker%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/86202019-08-30T11:25:43Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Walker, M J
author
Wehland, J
author
Timmis, K N
author
Raupach, B
author
Schmidt, M A
2007-02-20T13:15:51Z
1991-11
Infection and Immunity 1991 59(11):4249-4251
0019-9567
1718872
http://hdl.handle.net/10033/8620
259023
Images
en_US
Characterization of murine monoclonal antibodies that recognize defined epitopes of pertussis toxin and neutralize its toxic effect on Chinese hamster ovary cells.
URL
https://hzi.openrepository.com/bitstream/10033/8620/1/Walker%20et%20al_final.pdf
File
MD5
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Walker et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8620/7/Walker%20et%20al_final.pdf.txt
File
MD5
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Walker et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86212019-08-30T11:26:12Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Kessler, B
author
Marqués, S
author
Köhler, T
author
Ramos, J L
author
Timmis, K N
author
de Lorenzo, V
2007-02-20T13:16:52Z
1994-09
Journal of Bacteriology 1994 176(17):5578-5582
0021-9193
8071244
http://hdl.handle.net/10033/8621
196754
Images
en_US
Cross talk between catabolic pathways in Pseudomonas putida: XylS-dependent and -independent activation of the TOL meta operon requires the same cis-acting sequences within the Pm promoter.
URL
https://hzi.openrepository.com/bitstream/10033/8621/1/kessler%20et%20al_final.pdf
File
MD5
d7aba011d220c6d49bfdf879685b22dc
1334475
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kessler et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8621/7/kessler%20et%20al_final.pdf.txt
File
MD5
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text/plain
kessler et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86242019-08-30T11:25:43Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Niebuhr, K
author
Chakraborty, T
author
Rohde, Manfred
author
Gazlig, T
author
Jansen, B
author
Köllner, P
author
Wehland, J
2007-02-20T13:23:07Z
1993-07
Infection and Immunity 1993 61(7):2793-2802
0019-9567
8514381
http://hdl.handle.net/10033/8624
280923
Images
en_US
Localization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets".
URL
https://hzi.openrepository.com/bitstream/10033/8624/1/Niebuhr%20et%20al_final.pdf
File
MD5
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Niebuhr et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8624/7/Niebuhr%20et%20al_final.pdf.txt
File
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899854f70082cc1f63ee66cae9ad64d2
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Niebuhr et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86252019-08-30T11:24:25Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Güde, Hans
2007-02-20T13:23:51Z
1980-04
Applied and Environmental Microbiology 1980 39(4):756-763
0099-2240
http://hdl.handle.net/10033/8625
291415
en_US
Occurrence of Cytophagas in Sewage Plants
URL
https://hzi.openrepository.com/bitstream/10033/8625/1/G%c3%bcde_final.pdf
File
MD5
a2c54aad00696a3b5231c116388221d8
1358276
application/pdf
Güde_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8625/7/G%c3%bcde_final.pdf.txt
File
MD5
696505e2234286667ee73e3cc1cb4153
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text/plain
Güde_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86322019-08-30T11:26:12Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Kloos, D U
author
Strätz, M
author
Güttler, A
author
Steffan, R J
author
Timmis, K N
2007-02-20T13:29:29Z
1994-12
Journal of Bacteriology 1994 176(23):7352-7361
0021-9193
7961508
http://hdl.handle.net/10033/8632
197125
Images
en_US
Inducible cell lysis system for the study of natural transformation and environmental fate of DNA released by cell death.
URL
https://hzi.openrepository.com/bitstream/10033/8632/1/kloos%20et%20al_final.pdf
File
MD5
89540e50d330fb3b380deb5dc1f15bd4
2043697
application/pdf
kloos et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8632/7/kloos%20et%20al_final.pdf.txt
File
MD5
6bd5f3686d0c28c1a36aa75a234abdab
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text/plain
kloos et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86412019-08-30T11:25:43Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Lünsdorf, H
author
Niedrig, M
author
Fiebig, K
2007-02-20T13:35:37Z
1991-02
Journal of Bacteriology 1991 173(3):978-984
0021-9193
1991734
http://hdl.handle.net/10033/8641
207214
Images
en_US
Immunocytochemical localization of the coenzyme F420-reducing hydrogenase in Methanosarcina barkeri Fusaro.
URL
https://hzi.openrepository.com/bitstream/10033/8641/1/L%c3%bcnsdorf%2c%20Niedrig%20and%20Fiebig_final.pdf
File
MD5
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3092672
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Lünsdorf, Niedrig and Fiebig_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8641/7/L%c3%bcnsdorf%2c%20Niedrig%20and%20Fiebig_final.pdf.txt
File
MD5
6bc7b99e16e7e1449defd83509524e5d
38704
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Lünsdorf, Niedrig and Fiebig_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86442019-08-30T11:27:08Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Chhatwal, G S
author
Valentin-Weigand, P
author
Timmis, K N
2007-02-20T13:37:09Z
1990-09
Infection and Immunity 1990 58(9):3015-3019
0019-9567
2201643
http://hdl.handle.net/10033/8644
313604
en_US
Bacterial infection of wounds: fibronectin-mediated adherence group A and C streptococci to fibrin thrombi in vitro.
URL
https://hzi.openrepository.com/bitstream/10033/8644/1/Chhatwal%20et%20al_final.pdf
File
MD5
8177ffc738085188cee856d69c42f77e
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application/pdf
Chhatwal et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8644/7/Chhatwal%20et%20al_final.pdf.txt
File
MD5
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Chhatwal et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86502019-08-30T11:25:38Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Schulze, Kai
author
Medina, Eva
author
Chhatwal, Gursharan S.
author
Guzmán, Carlos A.
2007-02-20T13:40:07Z
2003-12
Infection and Immunity 2003 71(12):7197-7201
0019-9567
14638816
10.1128/IAI.71.12.7197-7201.2003
http://hdl.handle.net/10033/8650
308920
en_US
Copyright © 2003, American Society for Microbiology
Identification of B- and T-Cell Epitopes within the Fibronectin-Binding Domain of the SfbI Protein of Streptococcus pyogenes
URL
https://hzi.openrepository.com/bitstream/10033/8650/1/Schulze%20et%20al_final.pdf
File
MD5
9c80d4f6f66cb9cd4d9119277775818e
208932
application/pdf
Schulze et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8650/7/Schulze%20et%20al_final.pdf.txt
File
MD5
9d2698f8c5bbac1b47c7e134202393fe
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Schulze et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86592019-08-30T11:24:26Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Bolm, Maike
author
Jansen, Wouter T. M.
author
Schnabel, Ralf
author
Chhatwal, Gursharan S.
2007-02-20T14:32:48Z
2004-02
Infection and Immunity 2004 72(2):1192-1194
0019-9567
14742574
10.1128/IAI.72.2.1192-1194.2004
http://hdl.handle.net/10033/8659
321644
en_US
Copyright © 2004, American Society for Microbiology
Hydrogen Peroxide-Mediated Killing of Caenorhabditis elegans: a Common Feature of Different Streptococcal Species
URL
https://hzi.openrepository.com/bitstream/10033/8659/1/Bolm%20et%20al_final.pdf
File
MD5
cebcc279abb9f65505f5f6d079c011c2
154414
application/pdf
Bolm et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8659/7/Bolm%20et%20al_final.pdf.txt
File
MD5
f5b353fac3dda66043d441cbcbaf2585
13786
text/plain
Bolm et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86622019-08-30T11:26:13Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Tiedge, Henri
author
Lünsdorf, Heinrich
author
Schäfer, Günter
author
Schairer, Hans Ulrich
2007-02-20T14:34:49Z
1985-12
Proceedings of the National Academy of Sciences of the United States of America 1985 82(23):7874-7878
0027-8424
http://hdl.handle.net/10033/8662
390872
Images
en_US
Subunit stoichiometry and juxtaposition of the photosynthetic coupling factor 1: Immunoelectron microscopy using monoclonal antibodies
URL
https://hzi.openrepository.com/bitstream/10033/8662/1/Tiedge%20et%20al_final.pdf
File
MD5
1cab7b56179a29cefdac193fa32d2bfd
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Tiedge et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8662/7/Tiedge%20et%20al_final.pdf.txt
File
MD5
144a491d5486e4ec884797043697ccb9
25034
text/plain
Tiedge et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86632019-08-30T11:24:26Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Bergmann, Simone
author
Rohde, Manfred
author
Hammerschmidt, Sven
2007-02-20T14:35:49Z
2004-04
Infection and Immunity 2004 72(4):2416-2419
0019-9567
15039372
10.1128/IAI.72.4.2416-2419.2004
http://hdl.handle.net/10033/8663
375162
en_US
Copyright © 2004, American Society for Microbiology
Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus pneumoniae Is a Surface-Displayed Plasminogen-Binding Protein
URL
https://hzi.openrepository.com/bitstream/10033/8663/1/Bergmann%20et%20al_final.pdf
File
MD5
8ea73e12fc6053f804980872d7c09237
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Bergmann et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8663/7/Bergmann%20et%20al_final.pdf.txt
File
MD5
a540286fcb6167a13a507efef4c067b3
19631
text/plain
Bergmann et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86642019-08-30T11:25:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Goldmann, Oliver
author
Rohde, Manfred
author
Chhatwal, Gursharan Singh
author
Medina, Eva
2007-02-20T14:36:16Z
2004-05
Infection and Immunity 2004 72(5):2956-2963
0019-9567
15102808
10.1128/IAI.72.5.2956-2963.2004
http://hdl.handle.net/10033/8664
387899
en_US
Copyright © 2004, American Society for Microbiology
Role of Macrophages in Host Resistance to Group A Streptococci
URL
https://hzi.openrepository.com/bitstream/10033/8664/1/Goldmann%20et%20al_final.pdf
File
MD5
e645228d1311cc6a8a1c8623a6fcc06e
977582
application/pdf
Goldmann et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8664/7/Goldmann%20et%20al_final.pdf.txt
File
MD5
36c86586c64b1ab3b64d77af0430bbc2
42571
text/plain
Goldmann et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86652019-08-30T11:27:08Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Chávez, Francisco P.
author
Lünsdorf, Heinrich
author
Jerez, Carlos A.
2007-02-20T14:36:38Z
2004-05
Applied and Environmental Microbiology 2004 70(5):3064-3072
0099-2240
15128568
10.1128/AEM.70.5.3064-3072.2004
http://hdl.handle.net/10033/8665
404396
en_US
Copyright © 2004, American Society for Microbiology
Growth of Polychlorinated-Biphenyl-Degrading Bacteria in the Presence of Biphenyl and Chlorobiphenyls Generates Oxidative Stress and Massive Accumulation of Inorganic Polyphosphate
URL
https://hzi.openrepository.com/bitstream/10033/8665/1/Chavez%20et%20al_final.pdf
File
MD5
96999f0c0fd6fbbd3dfdadae9708f2f8
1219530
application/pdf
Chavez et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8665/7/Chavez%20et%20al_final.pdf.txt
File
MD5
ab744653590d973056bde01df078ef9b
40194
text/plain
Chavez et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/86822019-08-30T11:33:26Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
McArthur, J.
author
Medina, Eva
author
Mueller, A.
author
Chin, J.
author
Currie, B. J.
author
Sriprakash, K. S.
author
Talay, S. R.
author
Chhatwal, G. S.
author
Walker, M. J.
2007-02-21T08:17:55Z
2004-12
Infection and Immunity 2004 72(12):7342-7345
0019-9567
15557665
10.1128/IAI.72.12.7342-7345.2004
http://hdl.handle.net/10033/8682
529117
en_US
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
URL
https://hzi.openrepository.com/bitstream/10033/8682/1/McArthur%20et%20al_final.pdf
File
MD5
65e2a04402e8335be4b70c41db329362
238440
application/pdf
McArthur et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8682/7/McArthur%20et%20al_final.pdf.txt
File
MD5
c6cd485289441f620f7a1b8690b5d2c4
24187
text/plain
McArthur et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/87002019-08-30T11:25:07Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Pracht, Daniela
author
Elm, Christine
author
Gerber, Joachim
author
Bergmann, Simone
author
Rohde, Manfred
author
Seiler, Marleen
author
Kim, Kwang S.
author
Jenkinson, Howard F.
author
Nau, Roland
author
Hammerschmidt, Sven
2007-02-21T08:39:54Z
2005-05
Infection and Immunity 2005 73(5):2680-2689
0019-9567
15845469
10.1128/IAI.73.5.2680-2689.2005
http://hdl.handle.net/10033/8700
1087317
en_US
Copyright © 2005, American Society for Microbiology
PavA of Streptococcus pneumoniae Modulates Adherence, Invasion, and Meningeal Inflammation
URL
https://hzi.openrepository.com/bitstream/10033/8700/1/Pracht%20et%20al_final.pdf
File
MD5
6de4ed0b99293ef2425cfb6feca2f8ed
690336
application/pdf
Pracht et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8700/7/Pracht%20et%20al_final.pdf.txt
File
MD5
e36ae2cc82ed60fb9676ee386b679a9e
58053
text/plain
Pracht et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/87472019-08-30T11:25:09Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Machata, Silke
author
Hain, Torsten
author
Rohde, Manfred
author
Chakraborty, Trinad
2007-02-22T14:44:54Z
2005-12
Journal of Bacteriology 2005 187(24):8385-8394
0021-9193
16321943
10.1128/JB.187.24.8385-8394.2005
http://hdl.handle.net/10033/8747
1317001
en_US
Copyright © 2005, American Society for Microbiology
Simultaneous Deficiency of both MurA and p60 Proteins Generates a Rough Phenotype in Listeria monocytogenes
URL
https://hzi.openrepository.com/bitstream/10033/8747/1/machata%20et%20al_final.pdf
File
MD5
97ef2e40930a1dbf3c04c6607461f43b
513140
application/pdf
machata et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8747/7/machata%20et%20al_final.pdf.txt
File
MD5
0f3672e6e800f5b4498e7b79facdcc0a
51235
text/plain
machata et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/87632019-08-30T11:26:13Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Lünsdorf, Heinrich
author
Kristen, Ingeborg
author
Barth, Elke
2007-02-22T14:59:18Z
2006-06-27
BMC Microbiology 2006 6:59
1471-2180
16803626
10.1186/1471-2180-6-59
http://hdl.handle.net/10033/8763
1524781
Background Synthesis of cationic hydrous thorium dioxide colloids (ca. 1.0 to 1.7 nm) has been originally described by Müller [22] and Groot [11] and these have been used by Groot to stain acidic glucosaminoglycans for ultrastructure research of different tissues by conventional transmission electron microscopy. Results Synthesis of colloidal thorium dioxide has been modified and its use as a suitable stain of acidic mucopolysaccharides and other anionic biopolymers from bacteria, either as whole mount preparations or as preembedment labels, is described. The differences in stain behavior relative to commonly used rutheniumred-lysine and Alcian Blue™ electron dense acidic stains has been investigated and its use is exemplified for Pseudomonas aeruginosa adjacent cell wall biopolymers. For the first time thorificated biopolymers, i.e. bacterial outer cell wall layers, have been analysed at the ultrastructural level with electron energy loss spectroscopy (EELS) and electron spectroscopic imaging (ESI), leading to excellent contrast and signal strength for these extracellular biopolymers. Conclusion Application of cationic hydrous ThO2 colloids for tracing acidic groups of the bacterial surface and/or EPS has been shown to be rather effective by transmission electron microscopy. Because of its high electron density and its good diffusibility it stains and outlines electro-negative charges within these biopolymers. In combination with ESI, based on integrated energy-filtered electron microscopy (EFTEM) Th-densities and thus negative charge densities can be discriminated from other elemental densities, especially in environmental samples, such as biofilms.
en_US
Copyright © 2006 Lünsdorf et al; licensee BioMed Central Ltd.
Cationic hydrous thorium dioxide colloids – a useful tool for staining negatively charged surface matrices of bacteria for use in energy-filtered transmission electron microscopy
URL
https://hzi.openrepository.com/bitstream/10033/8763/1/l%c3%bcnsdorf%20et%20al_final.pdf
File
MD5
f7f0d6367251b19bdee84df8c557f957
946357
application/pdf
lünsdorf et al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/8763/7/l%c3%bcnsdorf%20et%20al_final.pdf.txt
File
MD5
bee1ab553b30bbd7735860988222e9a7
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lünsdorf et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/123072019-08-30T11:31:49Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Romero-Tabarez, Magally
author
Jansen, Rolf
author
Sylla, Marita
author
Lünsdorf, Heinrich
author
Häussler, Susanne
author
Santosa, Dwi A
author
Timmis, Kenneth N
author
Molinari, Gabriella
2007-06-08T14:05:25Z
2006-05-01
Antimicrob. Agents Chemother. 2006, 50(5):1701-9
0066-4804
16641438
10.1128/AAC.50.5.1701-1709.2006
http://hdl.handle.net/10033/12307
We report here the discovery, isolation, and chemical and preliminary biological characterization of a new antibiotic compound, 7-O-malonyl macrolactin A (MMA), produced by a Bacillus subtilis soil isolate. MMA is a bacteriostatic antibiotic that inhibits a number of multidrug-resistant gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and a small-colony variant of Burkholderia cepacia. MMA-treated staphylococci and enterococci were pseudomulticellular and exhibited multiple asymmetric initiation points of septum formation, indicating that MMA may inhibit a cell division function.
en
7-O-malonyl macrolactin A, a new macrolactin antibiotic from Bacillus subtilis active against methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and a small-colony variant of Burkholderia cepacia.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/12307/2/Molinari_AAC.pdf
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-1
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URL
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oai:repository.helmholtz-hzi.de:10033/123512019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Sugareva, Venelina
author
Härtl, Albert
author
Brock, Matthias
author
Hübner, Katrin
author
Rohde, Manfred
author
Heinekamp, Thorsten
author
Brakhage, Axel A
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.
en
Characterisation of the laccase-encoding gene abr2 of the dihydroxynaphthalene-like melanin gene cluster of Aspergillus fumigatus.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/12351/1/Sugareva_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/12351/8/Sugareva_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/145502019-08-30T11:35:14Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Burnett, Tracey A
author
Dinkla, Katrin
author
Rohde, Manfred
author
Chhatwal, Gursharan S
author
Uphoff, Cord
author
Srivastava, Mukesh
author
Cordwell, Stuart J
author
Geary, Steven
author
Liao, Xiaofen
author
Minion, F Chris
author
Walker, Mark J
author
Djordjevic, Steven P
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.
en
P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/14550/1/Burnettfinal.pdf
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URL
https://hzi.openrepository.com/bitstream/10033/14550/5/Burnettfinal.pdf.txt
File
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Burnettfinal.pdf.txt
oai:repository.helmholtz-hzi.de:10033/146302019-08-30T11:35:13Zcom_10033_6814col_10033_6885
Helmholtz Zentrum für Infektionsforschung Repository
author
Seibel, Jürgen
author
Hellmuth, Hendrik
author
Hofer, Bernd
author
Kicinska, Anna-Maria
author
Schmalbruch, Bodo
2007-11-19T14:44:40Z
2006-02-01
Chembiochem 2006, 7(2):310-20
1439-4227
16416490
10.1002/cbic.200500350
http://hdl.handle.net/10033/14630
Finding opportunities to construct sugar motifs and to transfer them to targets of biological relevance and rapid identification of glycosylation events are important goals for glycobiology and a field of increasing interest. Here we have applied an enzyme microarray screening system for the identification of new acceptor specificities of the glycosyltransferase R (GTFR) from Streptococcus oralis (E.C. 2.4.1.5), which was able to effect the synthesis of sugar motifs in short times and with low amounts of substrate. These observations resulted in the development of a convenient alpha-glycosylation by the non-Leloir glycosyltransferase GTFR, with sucrose as substrate and with different alcohols and amino acid derivatives as acceptors, for the synthesis of glycoethers and glycosylated amino acids not observed with the use of familiar GTFs with high sequence homology.
en
Identification of new acceptor specificities of glycosyltransferase R with the aid of substrate microarrays.
Article
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oai:repository.helmholtz-hzi.de:10033/147322019-08-30T11:24:31Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Nitsche, D Patric
author
Johansson, Helena M
author
Frick, Inga-Maria
author
Mörgelin, Matthias
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.
en
Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo.
Article
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oai:repository.helmholtz-hzi.de:10033/194322019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Rohde, Manfred
author
Mayer, H
department
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
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
Exocytotic process as a novel model for mineralization by osteoblasts in vitro and in vivo determined by electron microscopic analysis.
Article
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oai:repository.helmholtz-hzi.de:10033/195532019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
McMillan, David J
author
Sriprakash, Kadaba S
author
Chhatwal, Gursharan S
department
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
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
Genetic variation in group A streptococci.
Article
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oai:repository.helmholtz-hzi.de:10033/196132019-08-30T11:37:24Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Lee, Yong-Jin
author
Prange, Alexander
author
Lichtenberg, Henning
author
Rohde, Manfred
author
Dashti, Mona
author
Wiegel, Juergen
department
Department of Microbiology, The University of Georgia, Athens, GA 30602-2605, USA.
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
In situ analysis of sulfur species in sulfur globules produced from thiosulfate by Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/19613/1/Lee%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/196522019-08-30T11:37:24Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Dinkla, Katrin
author
Nitsche-Schmitz, D Patric
author
Barroso, Vanessa
author
Reissmann, Silvana
author
Johansson, Helena M
author
Frick, Inga-Maria
author
Rohde, Manfred
author
Chhatwal, Gursharan S
department
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
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
Identification of a streptococcal octapeptide motif involved in acute rheumatic fever.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/19652/1/Dinkla%20et%20al_final.pdf
File
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URL
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oai:repository.helmholtz-hzi.de:10033/198332019-08-30T11:37:44Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Walker, Mark J
author
Hollands, Andrew
author
Sanderson-Smith, Martina L
author
Cole, Jason N
author
Kirk, Joshua K
author
Henningham, Anna
author
McArthur, Jason D
author
Dinkla, Katrin
author
Aziz, Ramy K
author
Kansal, Rita G
author
Simpson, Amelia J
author
Buchanan, John T
author
Chhatwal, Gursharan S
author
Kotb, Malak
author
Nizet, Victor
department
School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.
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
DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/19833/1/Walker%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/243522019-08-30T11:26:42Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Nitsche-Schmitz, D Patric
author
Rohde, Manfred
author
Chhatwal, Gursharan S
department
Helmholtz Centre for Infection Research, Microbial Pathogenesis, Braunschweig, Germany.
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
Invasion mechanisms of Gram-positive pathogenic cocci.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/24352/1/Nitsche-Schimtz_final.pdf
File
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URL
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oai:repository.helmholtz-hzi.de:10033/246522019-08-30T11:34:48Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Friedrichs, C
author
Rodloff, A C
author
Chhatwal, G S
author
Schellenberger, W
author
Eschrich, K
department
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
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
Rapid identification of viridans streptococci by mass spectrometric discrimination.
article
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URL
https://hzi.openrepository.com/bitstream/10033/24652/5/friedrichs%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/290122019-08-30T11:27:16Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Vary, Patricia S
author
Biedendieck, Rebekka
author
Fuerch, Tobias
author
Meinhardt, Friedhelm
author
Rohde, Manfred
author
Deckwer, Wolf-Dieter
author
Jahn, Dieter
department
Department of Biological Sciences, Northern Illinois University, DeKalb, IL 60115, USA.
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--from simple soil bacterium to industrial protein production host.
Article
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oai:repository.helmholtz-hzi.de:10033/303972019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Heroven, Ann Kathrin
author
Böhme, Katja
author
Rohde, Manfred
author
Dersch, Petra
department
Institut für Mikrobiologie, Technische Universität Braunschweig, 38106 Braunschweig, Germany.
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
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URL
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oai:repository.helmholtz-hzi.de:10033/472372019-08-30T11:32:16Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Dinkla, K
author
Cole, J N
author
Cork, A J
author
Maamary, P G
author
McArthur, J D
author
Chhatwal, G S
author
Walker, M J
department
School of Biological Sciences, University of Wollongong, Wollongong, NSW, 2522, Australia.
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
M protein-mediated plasminogen binding is essential for the virulence of an invasive Streptococcus pyogenes isolate.
Article
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oai:repository.helmholtz-hzi.de:10033/485372019-08-30T11:32:17Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Molinari, Gabriella
author
Rohde, Manfred
author
Wilde, Christian
author
Just, Ingo
author
Aktories, Klaus
author
Chhatwal, Gursharan S
department
Department of Microbial Pathogenesis, GBF-German Research Centre for Biotechnology, Mascheroder Weg 1, 38124 Braunschweig, Germany.
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
Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/48537/1/Molinari%20et%20al_final.pdf
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https://hzi.openrepository.com/bitstream/10033/48537/7/Molinari%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/650542019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Dinkla, Katrin
author
Talay, Susanne R
author
Mörgelin, Matthias
author
Graham, Rikki M A
author
Rohde, Manfred
author
Nitsche-Schmitz, D Patric
author
Chhatwal, Gursharan S
department
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Braunschweig, Germany.
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
Crucial role of the CB3-region of collagen IV in PARF-induced acute rheumatic fever.
Article
URL
https://hzi.openrepository.com/bitstream/10033/65054/1/Dinkla%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/65054/7/Dinkla%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/847332019-08-30T11:34:48Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Mehboob, Farrakh
author
Junca, Howard
author
Schraa, Gosse
author
Stams, Alfons J M
department
Wageningen University, The Netherlands.
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
Growth of Pseudomonas chloritidismutans AW-1(T) on n-alkanes with chlorate as electron acceptor.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/84733/1/Mehboob%20et%20al_final.pdf
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URL
https://hzi.openrepository.com/bitstream/10033/84733/8/Mehboob%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/929422019-08-30T11:35:13Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Candela, Marco
author
Biagi, Elena
author
Centanni, Manuela
author
Turroni, Silvia
author
Vici, Manuela
author
Musiani, Francesco
author
Vitali, Beatrice
author
Bergmann, Simone
author
Hammerschmidt, Sven
author
Brigidi, Patrizia
department
Department of Pharmaceutical Sciences, CIRB-centre for Biotechnology, University of Bologna, Italy.
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
Bifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the host.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/92942/1/Candela%20et%20al_final.pdf
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URL
https://hzi.openrepository.com/bitstream/10033/92942/7/Candela%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/980532019-08-30T11:26:07Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Moeller, Ralf
author
Rohde, Manfred
author
Reitz, Günther
department
Department of Medical Microbiology, Helmholtz Centre for Infection Research, Inhoffenstr. 7, D-38124 Braunschweig, Germany
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
Effects of ionizing radiation on the survival of bacterial spares in artificial martia regolith
Article
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URL
https://hzi.openrepository.com/bitstream/10033/98053/1/Moeller%20et%20al_final.pdf
File
MD5
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URL
https://hzi.openrepository.com/bitstream/10033/98053/7/Moeller%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/1067782019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Reissmann, Silvana
author
Friedrichs, Claudia
author
Rajkumari, Reena
author
Itzek, Andreas
author
Fulde, Marcus
author
Rodloff, Arne C
author
Brahmadathan, Kootallur N
author
Chhatwal, Gursharan S
author
Nitsche-Schmitz, D Patric
department
Helmholtz Centre for Infection Research, Braunschweig, Germany.
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
Contribution of Streptococcus anginosus to infections caused by groups C and G streptococci, southern India.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/106778/1/Rei%c3%9fmann%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/106778/7/Rei%c3%9fmann%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/1111482019-08-30T11:31:49Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Candela, Marco
author
Centanni, Manuela
author
Fiori, Jessica
author
Biagi, Elena
author
Turroni, Silvia
author
Orrico, Catia
author
Bergmann, Simone
author
Hammerschmidt, Sven
author
Brigidi, Patrizia
department
Department of Pharmaceutical Sciences, University of Bologna, Italy.
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
DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/111148/1/Candela%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/111148/7/Candela%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/1169522019-08-30T11:35:39Zcom_10033_116429com_10033_6815com_10033_6814col_10033_116410
Helmholtz Zentrum für Infektionsforschung Repository
author
Wähe, Anna
author
Kasmapour, Bahram
author
Schmaderer, Christoph
author
Liebl, David
author
Sandhoff, Konrad
author
Nykjaer, Anders
author
Griffiths, Gareth
author
Gutierrez, Maximiliano G
department
European Molecular Biology Laboratory, Postfach 102209, 69117 Heidelberg, Germany.
2010-12-02T13:59:43Z
2010-07-15
Golgi-to-phagosome transport of acid sphingomyelinase and prosaposin is mediated by sortilin. 2010, 123 (Pt 14):2502-11 J. Cell. Sci.
1477-9137
20571055
10.1242/jcs.067686
http://hdl.handle.net/10033/116952
Journal of cell science
Sortilin, also known as neurotensin receptor 3 (NTR3), is a transmembrane protein with a dual function. It acts as a receptor for neuromediators and growth factors at the plasma membrane, but it has also been implicated in binding and transport of some lysosomal proteins. However, the role of sortilin during phagosome maturation has not been investigated before. Here, we show that in macrophages, sortilin is mainly localized in the Golgi and transported to latex-bead phagosomes (LBPs). Using live-cell imaging and electron microscopy, we found that sortilin is delivered to LBPs in a manner that depends on its cytoplasmic tail. We also show that sortilin participates in the direct delivery of acid sphingomyelinase (ASM) and prosaposin (PS) to the phagosome, bypassing fusion with lysosomal compartments. Further analysis confirmed that ASM and PS are targeted to the phagosome by sortilin in a Brefeldin-A-sensitive pathway. Analysis of primary macrophages isolated from Sort1(-/-) mice indicated that the delivery of ASM and PS, but not pro-cathepsin D, to LBPs was severely impaired. We propose a pathway mediated by sortilin by which selected lysosomal proteins are transported to the phagosome along a Golgi-dependent route during the maturation of phagosomes.
en
Golgi-to-phagosome transport of acid sphingomyelinase and prosaposin is mediated by sortilin.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/116952/6/W%c3%a4he%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/1171652019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Itzek, Andreas
author
Gillen, Christine M
author
Fulde, Marcus
author
Friedrichs, Claudia
author
Rodloff, Arne C
author
Chhatwal, Gursharan S
author
Nitsche-Schmitz, Daniel Patric
department
Department of Medical Microbiology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
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
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URL
https://hzi.openrepository.com/bitstream/10033/117165/1/Itzek%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/1185682019-08-30T11:36:05Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Hoffmann, Christine
author
Berking, Anne
author
Agerer, Franziska
author
Buntru, Alexander
author
Neske, Florian
author
Chhatwal, G Singh
author
Ohlsen, Knut
author
Hauck, Christof R
department
Lehrstuhl Zellbiologie X908, Universität Konstanz, Universitätsstr. 10, 78457 Konstanz, Germany.
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
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URL
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URL
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oai:repository.helmholtz-hzi.de:10033/1205452019-08-30T11:36:05Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Aziz, Ramy K
author
Kansal, Rita
author
Aronow, Bruce J
author
Taylor, William L
author
Rowe, Sarah L
author
Kubal, Michael
author
Chhatwal, Gursharan S
author
Walker, Mark J
author
Kotb, Malak
department
Research Services, Veterans Affairs Medical Center, Memphis, Tennessee, United States of America. ramy.aziz@salmonella.org
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
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URL
https://hzi.openrepository.com/bitstream/10033/120545/1/Aziz%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/1233042019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Bunk, Boyke
author
Schulz, Arne
author
Stammen, Simon
author
Münch, Richard
author
Warren, Martin J
author
Rohde, Manfred
author
Jahn, Dieter
author
Biedendieck, Rebekka
department
Institute of Microbiology; Technische Universität Braunschweig; Braunschweig, Germany.
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.
A short story about a big magic bug.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/123304/1/Bunk%20et%20al_final.pdf
File
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URL
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oai:repository.helmholtz-hzi.de:10033/1241092019-08-30T11:36:33Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Kaur, Simran Jeet
author
Nerlich, Andreas
author
Bergmann, Simone
author
Rohde, Manfred
author
Fulde, Marcus
author
Zähner, Dorothea
author
Hanski, Emanuel
author
Zinkernagel, Annelies
author
Nizet, Victor
author
Chhatwal, Gursharan S
author
Talay, Susanne R
department
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
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
The CXC chemokine-degrading protease SpyCep of Streptococcus pyogenes promotes its uptake into endothelial cells.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/124109/1/Kaur%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/1297482019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Itzek, Andreas
author
Gillen, Christine M
author
Fulde, Marcus
author
Friedrichs, Claudia
author
Rodloff, Arne C
author
Chhatwal, Gursharan S
author
Nitsche-Schmitz, Daniel Patric
department
Department of Medical Microbiology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
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
Contribution of plasminogen activation towards the pathogenic potential of oral streptococci.
Article
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URL
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oai:repository.helmholtz-hzi.de:10033/1385702019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Fulde, Marcus
author
Rohde, Manfred
author
Hitzmann, Angela
author
Preissner, Klaus T
author
Nitsche-Schmitz, D Patric
author
Nerlich, Andreas
author
Chhatwal, Gursharan Singh
author
Bergmann, Simone
department
Department of Medical Microbiology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany. Marcus.Fulde@helmholtz-hzi.de
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
SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/138570/1/Fulde%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/1396892019-08-30T11:25:43Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Bergmann, René
author
Dinkla, Katrin
author
Nitsche-Schmitz, D Patric
author
Graham, Rikki M A
author
Lüttge, Melanie
author
Sanderson-Smith, Martina L
author
Nerlich, Andreas
author
Rohde, Manfred
author
Chhatwal, Gursharan S
department
Dept. of Medical Microbiology, Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.
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
Biological functions of GCS3, a novel plasminogen-binding protein of Streptococcus dysgalactiae ssp. equisimilis.
Article
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URL
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URL
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oai:repository.helmholtz-hzi.de:10033/1420102019-08-30T11:37:23Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Marjenberg, Zoe R
author
Ellis, Ian R
author
Hagan, Robert M
author
Prabhakaran, Sabitha
author
Höök, Magnus
author
Talay, Susanne R
author
Potts, Jennifer R
author
Staunton, David
author
Schwarz-Linek, Ulrich
department
Biomedical Sciences Research Complex, University of St. Andrews, St. Andrews KY16 9ST, Scotland, United Kingdom.
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
Cooperative binding and activation of fibronectin by a bacterial surface protein.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/142010/1/Marjenberg%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2037292019-08-30T11:32:16Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Willenborg, J
author
Fulde, M
author
de Greeff, A
author
Rohde, Manfred
author
Smith, H E
author
Valentin-Weigand, P
author
Goethe, R
department
Institute for Microbiology, University of Veterinary Medicine, Hannover, Germany.
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
Role of glucose and CcpA in capsule expression and virulence of Streptococcus suis.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/203729/1/Willenborg%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/203729/7/Willenborg%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/2105692019-08-30T11:32:17Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Rato, Márcia G
author
Nerlich, Andreas
author
Bergmann, René
author
Bexiga, Ricardo
author
Nunes, Sandro F
author
Vilela, Cristina L
author
Santos-Sanches, Ilda
author
Chhatwal, Gursharan S
department
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
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
Virulence gene pool detected in bovine group C Streptococcus dysgalactiae subsp. dysgalactiae isolates by use of a group A S. pyogenes virulence microarray.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/210569/1/Rato%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/210569/7/Rato%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/2135692019-08-30T11:24:31Zcom_10033_116429com_10033_6815com_10033_6814col_10033_116410
Helmholtz Zentrum für Infektionsforschung Repository
author
de Souza Carvalho, Cristiane
author
Kasmapour, Bahram
author
Gronow, Achim
author
Rohde, Manfred
author
Rabinovitch, Michel
author
Gutierrez, Maximiliano Gabriel
department
Department of Vaccinology and Applied Microbiology, Research Group Phagosome Biology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.
2012-02-29T13:03:04Z
2011-08
Internalization, phagolysosomal biogenesis and killing of mycobacteria in enucleated epithelial cells. 2011, 13 (8):1234-49 Cell. Microbiol.
1462-5822
21658173
10.1111/j.1462-5822.2011.01615.x
http://hdl.handle.net/10033/213569
Cellular microbiology
Bacterial and parasitic intracellular pathogens or their secreted products have been shown to induce host cell transcriptional responses, which may benefit the host, favour the microorganism or be unrelated to the infection. In most instances, however, it is not known if the host cell nucleus is proximately required for the development of an intracellular infection. This information can be obtained by the infection of artificially enucleated host cells (cytoplasts). This model, although rather extensively used in studies of viral infection, has only been applied to few bacterial pathogens, which do not include Mycobacterium spp. Here, we investigate the internalization, phagosome biogenesis and survival of M. smegmatis in enucleated type II alveolar epithelial cells. Cytoplasts were infected with M. smegmatis, but the percentage of infection was significantly lower than that of nucleated cells. Scanning electron microscopy indicated that in both cells and cytoplasts, bacteria were internalized by a phagocytosis-like mechanism. Interestingly, phagosome fusion with lysosomes and mycobacterial killing were both more efficient in enucleated than in nucleated cells, a finding that may be correlated with the increased number of autophagic vesicles developed in cytoplasts. We provide evidence that although quantitative changes were observed, the full development of the infection, as well as mycobacterial killing did not require the presence of the host cell nucleus.
en
Internalization, phagolysosomal biogenesis and killing of mycobacteria in enucleated epithelial cells.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/213569/1/Carvalho%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2135712019-08-30T11:26:13Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Amelung, Silva
author
Nerlich, Andreas
author
Rohde, Manfred
author
Spellerberg, Barbara
author
Cole, Jason N
author
Nizet, Victor
author
Chhatwal, Gursharan S
author
Talay, Susanne R
department
Department of Medical Microbiology, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
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
The FbaB-type fibronectin-binding protein of Streptococcus pyogenes promotes specific invasion into endothelial cells.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/213571/1/Amelung%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/213571/7/Amelung%20et%20al_final.pdf.txt
File
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oai:repository.helmholtz-hzi.de:10033/2148502019-08-30T11:27:46Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Härtel, Tobias
author
Klein, Matthias
author
Koedel, Uwe
author
Rohde, Manfred
author
Petruschka, Lothar
author
Hammerschmidt, Sven
department
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
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
Impact of glutamine transporters on pneumococcal fitness under infection-related conditions.
Article
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https://hzi.openrepository.com/bitstream/10033/214850/1/H%c3%a4rtel%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2162492019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Pati, Amrita
author
Gronow, Sabine
author
Zeytun, Ahmet
author
Lapidus, Alla
author
Nolan, Matt
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Detter, John C
author
Brambilla, Evelyne
author
Rohde, Manfred
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lucas, Susan
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
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URL
https://hzi.openrepository.com/bitstream/10033/216249/1/pati%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2162692019-08-30T11:26:13Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Pitluck, Sam
author
Sikorski, Johannes
author
Zeytun, Ahmet
author
Lapidus, Alla
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Detter, John C
author
Brambilla, Evelyne
author
Djao, Oliver Duplex Ngatchou
author
Rohde, Manfred
author
Spring, Stefan
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Land, Miriam
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
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
URL
https://hzi.openrepository.com/bitstream/10033/216269/1/pitluck%20at%20al_final.pdf
File
MD5
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pitluck at al_final.pdf
URL
https://hzi.openrepository.com/bitstream/10033/216269/8/pitluck%20at%20al_final.pdf.txt
File
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pitluck at al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/2169902019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Daligault, Hajnalka
author
Lapidus, Alla
author
Zeytun, Ahmet
author
Nolan, Matt
author
Lucas, Susan
author
Del Rio, Tijana Glavina
author
Tice, Hope
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Huntemann, Marcel
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Rohde, Manfred
author
Verbarg, Susanne
author
Göker, Markus
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Woyke, Tanja
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
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
URL
https://hzi.openrepository.com/bitstream/10033/216990/1/daligault%20et%20al_final.pdf
File
MD5
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URL
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oai:repository.helmholtz-hzi.de:10033/2169922019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Abt, Birte
author
Teshima, Hazuki
author
Lucas, Susan
author
Lapidus, Alla
author
Del Rio, Tijana Glavina
author
Nolan, Matt
author
Tice, Hope
author
Cheng, Jan-Fang
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Pati, Amrita
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Rohde, Manfred
author
Göker, Markus
author
Tindall, Brian J
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Klenk, Hans-Peter
author
Kyrpides, Nikos C
2012-03-29T09:19:29Z
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
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https://hzi.openrepository.com/bitstream/10033/216992/1/abt%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2169932019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Sikorski, Johannes
author
Teshima, Hazuki
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Huntemann, Marcel
author
Mavromatis, Konstantinos
author
Ovchinikova, Galina
author
Pati, Amrita
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Ngatchou-Djao, Olivier D
author
Rohde, Manfred
author
Pukall, Rüdiger
author
Spring, Stefan
author
Abt, Birte
author
Göker, Markus
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Eisen, Jonathan A
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lapidus, Alla
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
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https://hzi.openrepository.com/bitstream/10033/216993/1/sikorski%20at%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2396512020-08-31T20:17:26Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Lang, Elke
author
Teshima, Hazuki
author
Lucas, Susan
author
Lapidus, Alla
author
Hammon, Nancy
author
Deshpande, Shweta
author
Nolan, Matt
author
Cheng, Jan-Fang
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Mikhailova, Natalia
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Pati, Amrita
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Brambilla, Evelyne-Marie
author
Kopitz, Markus
author
Rohde, Manfred
author
Göker, Markus
author
Tindall, Brian J
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Klenk, Hans-Peter
author
Kyrpides, Nikos C
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
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URL
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oai:repository.helmholtz-hzi.de:10033/2169892019-08-30T11:37:44Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Pagani, Ioanna
author
Lapidus, Alla
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Chertkov, Olga
author
Davenport, Karen
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Mavromatis, Konstantinos
author
Ivanova, Natalia
author
Mikhailova, Natalia
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Detter, John C
author
Brambilla, Evelyne
author
Kannan, K Palani
author
Djao, Olivier D Ngatchou
author
Rohde, Manfred
author
Pukall, Rüdiger
author
Spring, Stefan
author
Göker, Markus
author
Sikorski, Johannes
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
2012-03-29T07:48:10Z
2011
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
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URL
https://hzi.openrepository.com/bitstream/10033/216989/1/pagani%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2169962019-08-30T11:25:11Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Gronow, Sabine
author
Munk, Christine
author
Lapidus, Alla
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Brambilla, Evelyne
author
Rohde, Manfred
author
Göker, Markus
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
2012-03-29T10:57:42Z
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
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URL
https://hzi.openrepository.com/bitstream/10033/216996/1/gronow%20et%20al_final.pdf
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MD5
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URL
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oai:repository.helmholtz-hzi.de:10033/2170092019-08-30T11:33:57Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Anderson, Iain
author
Sikorski, Johannes
author
Zeytun, Ahmet
author
Nolan, Matt
author
Lapidus, Alla
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Huntemann, Marcel
author
Mavromatis, Konstantinos
author
Ovchinikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Ngatchou-Djao, Olivier D
author
Rohde, Manfred
author
Tindall, Brian J
author
Göker, Markus
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Klenk, Hans-Peter
author
Kyrpides, Nikos C
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
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URL
https://hzi.openrepository.com/bitstream/10033/217009/1/anderson%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2170102019-08-30T11:34:22Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Han, Cliff
author
Mwirichia, Romano
author
Chertkov, Olga
author
Held, Brittany
author
Lapidus, Alla
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Goodwin, Lynne
author
Pitluck, Sam
author
Huntemann, Marcel
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Pagani, Ioanna
author
Mavromatis, Konstantinos
author
Ovchinikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Rohde, Manfred
author
Spring, Stefan
author
Sikorski, Johannes
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Detter, John C
2012-03-29T11:44:32Z
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
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URL
https://hzi.openrepository.com/bitstream/10033/217010/1/han%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2207512019-08-30T11:35:14Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Göker, Markus
author
Teshima, Hazuki
author
Lapidus, Alla
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Huntemann, Marcel
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Pagani, Ioanna
author
Mavromatis, Konstantinos
author
Ovchinikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Rohde, Manfred
author
Spring, Stefan
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
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
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URL
https://hzi.openrepository.com/bitstream/10033/220751/1/g%c3%b6ker%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2207532019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Anderson, Iain
author
Göker, Markus
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Huntemann, Marcel
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Pagani, Ioanna
author
Mavromatis, Konstantinos
author
Ovchinikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Huber, Harald
author
Yasawong, Montri
author
Rohde, Manfred
author
Spring, Stefan
author
Abt, Birte
author
Sikorski, Johannes
author
Wirth, Reinhard
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lapidus, Alla
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
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URL
https://hzi.openrepository.com/bitstream/10033/220753/1/anderson-g%c3%b6ker%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2207722019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Huntemann, Marcel
author
Lu, Megan
author
Nolan, Matt
author
Lapidus, Alla
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Ovchinikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Jeffries, Cynthia D
author
Detter, John C
author
Brambilla, Evelyne-Marie
author
Rohde, Manfred
author
Spring, Stefan
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Mavromatis, Konstantinos
2012-04-26T10:33:16Z
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
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URL
https://hzi.openrepository.com/bitstream/10033/220772/1/huntemann%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2218122019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Munk, A Christine
author
Lapidus, Alla
author
Lucas, Susan
author
Nolan, Matt
author
Tice, Hope
author
Cheng, Jan-Fang
author
Del Rio, Tijana Glavina
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Huntemann, Marcel
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Tapia, Roxanne
author
Han, Cliff
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Brettin, Thomas
author
Yasawong, Montri
author
Brambilla, Evelyne-Marie
author
Rohde, Manfred
author
Sikorski, Johannes
author
Göker, Markus
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
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
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URL
https://hzi.openrepository.com/bitstream/10033/221812/1/munk%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2207762019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Han, Cliff
author
Gronow, Sabine
author
Teshima, Hazuki
author
Lapidus, Alla
author
Nolan, Matt
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Zeytun, Ahmed
author
Tapia, Roxanne
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pagani, Ioanna
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Huntemann, Marcel
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Rohde, Manfred
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Detter, John C
2012-04-26T10:49:10Z
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
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
URL
https://hzi.openrepository.com/bitstream/10033/220776/1/han-gronow%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2207802019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Ivanova, Natalia
author
Rohde, Christine
author
Munk, Christine
author
Nolan, Matt
author
Lucas, Susan
author
Del Rio, Tijana Glavina
author
Tice, Hope
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxane
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Brambilla, Evelyne
author
Rohde, Manfred
author
Göker, Markus
author
Tindall, Brian J
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lapidus, Alla
2012-04-26T11:27:49Z
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
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URL
https://hzi.openrepository.com/bitstream/10033/220780/1/ivanova%20et%20al_final.pdf
File
MD5
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URL
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ivanova et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/2256792019-08-30T11:35:39Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Chang, Yun-Juan
author
Pukall, Rüdiger
author
Saunders, Elizabeth
author
Lapidus, Alla
author
Copeland, Alex
author
Nolan, Matt
author
Glavina Del Rio, Tijana
author
Lucas, Susan
author
Chen, Feng
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Detter, John C
author
Bruce, David
author
Goodwin, Lynne
author
Pitluck, Sam
author
Mikhailova, Natalia
author
Liolios, Konstantinos
author
Pati, Amrita
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Jeffries, Cynthia D
author
Brettin, Thomas
author
Rohde, Manfred
author
Göker, Markus
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
2012-05-24T11:32:42Z
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
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
URL
https://hzi.openrepository.com/bitstream/10033/225679/1/chang%20et%20al_final.pdf
File
MD5
3c044afb9cf8575a5dbac488be150f14
4078507
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URL
https://hzi.openrepository.com/bitstream/10033/225679/8/chang%20et%20al_final.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/2256742019-08-30T11:36:05Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Sikorski, Johannes
author
Lapidus, Alla
author
Chertkov, Olga
author
Lucas, Susan
author
Copeland, Alex
author
Glavina Del Rio, Tijana
author
Nolan, Matt
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Brambilla, Evelyne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Bruce, David
author
Detter, Chris
author
Tapia, Roxanne
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Rohde, Manfred
author
Göker, Markus
author
Spring, Stefan
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
2012-05-24T10:53:58Z
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
Tk9OLUVYQ0xVU0lWRSBESVNUUklCVVRJT04gTElDRU5TRQoKQnkgc2lnbmluZyBhbmQgc3VibWl0dGluZyB0aGlzIGxpY2Vuc2UsIHlvdSAodGhlIGF1dGhvcihzKSBvciBjb3B5cmlnaHQKb3duZXIpIGdyYW50cyB0byBIZWxtaG9sdHogWmVudHJ1bSBm77+9ciBJbmZla3Rpb25zZm9yc2NodW5nIFJlcG9zaXRvcnkgKEhaSSkgdGhlIG5vbi1leGNsdXNpdmUgcmlnaHQgdG8gcmVwcm9kdWNlLAp0cmFuc2xhdGUgKGFzIGRlZmluZWQgYmVsb3cpLCBhbmQvb3IgZGlzdHJpYnV0ZSB5b3VyIHN1Ym1pc3Npb24gKGluY2x1ZGluZwp0aGUgYWJzdHJhY3QpIHdvcmxkd2lkZSBpbiBwcmludCBhbmQgZWxlY3Ryb25pYyBmb3JtYXQgYW5kIGluIGFueSBtZWRpdW0sCmluY2x1ZGluZyBidXQgbm90IGxpbWl0ZWQgdG8gYXVkaW8gb3IgdmlkZW8uCgpZb3UgYWdyZWUgdGhhdCBIWkkgbWF5LCB3aXRob3V0IGNoYW5naW5nIHRoZSBjb250ZW50LCB0cmFuc2xhdGUgdGhlCnN1Ym1pc3Npb24gdG8gYW55IG1lZGl1bSBvciBmb3JtYXQgZm9yIHRoZSBwdXJwb3NlIG9mIHByZXNlcnZhdGlvbi4KCllvdSBhbHNvIGFncmVlIHRoYXQgSFpJIG1heSBrZWVwIG1vcmUgdGhhbiBvbmUgY29weSBvZiB0aGlzIHN1Ym1pc3Npb24gZm9yCnB1cnBvc2VzIG9mIHNlY3VyaXR5LCBiYWNrLXVwIGFuZCBwcmVzZXJ2YXRpb24uCgpZb3UgcmVwcmVzZW50IHRoYXQgdGhlIHN1Ym1pc3Npb24gaXMgeW91ciBvcmlnaW5hbCB3b3JrLCBhbmQgdGhhdCB5b3UgaGF2ZQp0aGUgcmlnaHQgdG8gZ3JhbnQgdGhlIHJpZ2h0cyBjb250YWluZWQgaW4gdGhpcyBsaWNlbnNlLiBZb3UgYWxzbyByZXByZXNlbnQKdGhhdCB5b3VyIHN1Ym1pc3Npb24gZG9lcyBub3QsIHRvIHRoZSBiZXN0IG9mIHlvdXIga25vd2xlZGdlLCBpbmZyaW5nZSB1cG9uCmFueW9uZSdzIGNvcHlyaWdodC4KCklmIHRoZSBzdWJtaXNzaW9uIGNvbnRhaW5zIG1hdGVyaWFsIGZvciB3aGljaCB5b3UgZG8gbm90IGhvbGQgY29weXJpZ2h0LAp5b3UgcmVwcmVzZW50IHRoYXQgeW91IGhhdmUgb2J0YWluZWQgdGhlIHVucmVzdHJpY3RlZCBwZXJtaXNzaW9uIG9mIHRoZQpjb3B5cmlnaHQgb3duZXIgdG8gZ3JhbnQgSFpJIHRoZSByaWdodHMgcmVxdWlyZWQgYnkgdGhpcyBsaWNlbnNlLCBhbmQgdGhhdApzdWNoIHRoaXJkLXBhcnR5IG93bmVkIG1hdGVyaWFsIGlzIGNsZWFybHkgaWRlbnRpZmllZCBhbmQgYWNrbm93bGVkZ2VkCndpdGhpbiB0aGUgdGV4dCBvciBjb250ZW50IG9mIHRoZSBzdWJtaXNzaW9uLgoKSUYgVEhFIFNVQk1JU1NJT04gSVMgQkFTRUQgVVBPTiBXT1JLIFRIQVQgSEFTIEJFRU4gU1BPTlNPUkVEIE9SIFNVUFBPUlRFRApCWSBBTiBBR0VOQ1kgT1IgT1JHQU5JWkFUSU9OIE9USEVSIFRIQU4gSFpJLCBZT1UgUkVQUkVTRU5UIFRIQVQgWU9VIEhBVkUKRlVMRklMTEVEIEFOWSBSSUdIVCBPRiBSRVZJRVcgT1IgT1RIRVIgT0JMSUdBVElPTlMgUkVRVUlSRUQgQlkgU1VDSApDT05UUkFDVCBPUiBBR1JFRU1FTlQuCgpIWkkgd2lsbCBjbGVhcmx5IGlkZW50aWZ5IHlvdXIgbmFtZShzKSBhcyB0aGUgYXV0aG9yKHMpIG9yIG93bmVyKHMpIG9mIHRoZQpzdWJtaXNzaW9uLCBhbmQgd2lsbCBub3QgbWFrZSBhbnkgYWx0ZXJhdGlvbiwgb3RoZXIgdGhhbiBhcyBhbGxvd2VkIGJ5IHRoaXMKbGljZW5zZSwgdG8geW91ciBzdWJtaXNzaW9uLgo=
URL
https://hzi.openrepository.com/bitstream/10033/225674/1/sikorski-lapidus%20et%20al_final.pdf
File
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URL
https://hzi.openrepository.com/bitstream/10033/225674/8/sikorski-lapidus%20et%20al_final.pdf.txt
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sikorski-lapidus et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/2268332019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Göker, Markus
author
Held, Brittany
author
Lapidus, Alla
author
Nolan, Matt
author
Spring, Stefan
author
Yasawong, Montri
author
Lucas, Susan
author
Glavina Del Rio, Tijana
author
Tice, Hope
author
Cheng, Jan-Fang
author
Goodwin, Lynne
author
Tapia, Roxanne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Brambilla, Evelyne
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Brettin, Thomas
author
Detter, John C
author
Han, Cliff
author
Rohde, Manfred
author
Sikorski, Johannes
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
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
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URL
https://hzi.openrepository.com/bitstream/10033/226833/1/g%c3%b6ker-held%20et%20al_final.pdf
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göker-held et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/2268512019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Tindall, Brian J
author
Sikorski, Johannes
author
Lucas, Susan
author
Goltsman, Eugene
author
Copeland, Alex
author
Glavina Del Rio, Tijana
author
Nolan, Matt
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Ovchinnikova, Galina
author
Pati, Amrita
author
Fähnrich, Regine
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Rohde, Manfred
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lapidus, Alla
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
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URL
https://hzi.openrepository.com/bitstream/10033/226851/1/tindall%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2268342019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Sikorski, Johannes
author
Tindall, Brian J
author
Lowry, Stephen
author
Lucas, Susan
author
Nolan, Matt
author
Copeland, Alex
author
Glavina Del Rio, Tijana
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Rohde, Manfred
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lapidus, Alla
2012-05-31T10:22:11Z
2010
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
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
URL
https://hzi.openrepository.com/bitstream/10033/226834/1/sikorski-tindall%20et%20al_final.pdf
File
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URL
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sikorski-tindall et al_final.pdf.txt
oai:repository.helmholtz-hzi.de:10033/2268112019-08-30T11:36:04Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Chertkov, Olga
author
Sikorski, Johannes
author
Brambilla, Evelyne
author
Lapidus, Alla
author
Copeland, Alex
author
Glavina Del Rio, Tijana
author
Nolan, Matt
author
Lucas, Susan
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Detter, John C
author
Bruce, David
author
Tapia, Roxanne
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Ovchinnikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Spring, Stefan
author
Rohde, Manfred
author
Göker, Markus
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
2012-05-31T08:50:25Z
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
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URL
https://hzi.openrepository.com/bitstream/10033/226811/1/chertkov%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2268322019-08-30T11:36:32Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Kiss, Hajnalka
author
Lang, Elke
author
Lapidus, Alla
author
Copeland, Alex
author
Nolan, Matt
author
Glavina Del Rio, Tijana
author
Chen, Feng
author
Lucas, Susan
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Pati, Amrita
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Detter, John C
author
Brettin, Thomas
author
Spring, Stefan
author
Rohde, Manfred
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
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
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URL
https://hzi.openrepository.com/bitstream/10033/226832/1/kiss%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2268352019-08-30T11:36:59Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Labutti, Kurt
author
Mayilraj, Shanmugam
author
Clum, Alicia
author
Lucas, Susan
author
Glavina Del Rio, Tijana
author
Nolan, Matt
author
Tice, Hope
author
Cheng, Jan-Fang
author
Pitluck, Sam
author
Liolios, Konstantinos
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Mikhailova, Natalia
author
Pati, Amrita
author
Goodwin, Lynne
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Chang, Yun-Juan
author
Jeffries, Cynthia D
author
Rohde, Manfred
author
Spring, Stefan
author
Göker, Markus
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Kyrpides, Nikos C
author
Klenk, Hans-Peter
author
Lapidus, Alla
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
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
URL
https://hzi.openrepository.com/bitstream/10033/226835/1/labutti%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2268722019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Liolios, Konstantinos
author
Sikorski, Johannes
author
Lu, Meagan
author
Nolan, Matt
author
Lapidus, Alla
author
Lucas, Susan
author
Hammon, Nancy
author
Deshpande, Shweta
author
Cheng, Jan-Fang
author
Tapia, Roxanne
author
Han, Cliff
author
Goodwin, Lynne
author
Pitluck, Sam
author
Huntemann, Marcel
author
Ivanova, Natalia
author
Pagani, Ioanna
author
Mavromatis, Konstantinos
author
Ovchinikova, Galina
author
Pati, Amrita
author
Chen, Amy
author
Palaniappan, Krishna
author
Land, Miriam
author
Hauser, Loren
author
Brambilla, Evelyne-Marie
author
Kotsyurbenko, Oleg
author
Rohde, Manfred
author
Tindall, Brian J
author
Abt, Birte
author
Göker, Markus
author
Detter, John C
author
Woyke, Tanja
author
Bristow, James
author
Eisen, Jonathan A
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Klenk, Hans-Peter
author
Kyrpides, Nikos C
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
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URL
https://hzi.openrepository.com/bitstream/10033/226872/1/liolios%20et%20al_final.pdf
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oai:repository.helmholtz-hzi.de:10033/2370522019-08-30T11:37:00Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Klenk, Hans-Peter
author
Lapidus, Alla
author
Chertkov, Olga
author
Copeland, Alex
author
Del Rio, Tijana Glavina
author
Nolan, Matt
author
Lucas, Susan
author
Chen, Feng
author
Tice, Hope
author
Cheng, Jan-Fang
author
Han, Cliff
author
Bruce, David
author
Goodwin, Lynne
author
Pitluck, Sam
author
Pati, Amrita
author
Ivanova, Natalia
author
Mavromatis, Konstantinos
author
Daum, Chris
author
Chen, Amy
author
Palaniappan, Krishna
author
Chang, Yun-Juan
author
Land, Miriam
author
Hauser, Loren
author
Jeffries, Cynthia D
author
Detter, John C
author
Rohde, Manfred
author
Abt, Birte
author
Pukall, Rüdiger
author
Göker, Markus
author
Bristow, James
author
Markowitz, Victor
author
Hugenholtz, Philip
author
Eisen, Jonathan A
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
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URL
https://hzi.openrepository.com/bitstream/10033/237052/1/Klenk%20et%20al_final.pdf
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URL
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oai:repository.helmholtz-hzi.de:10033/2276752019-08-30T11:36:59Zcom_10033_6815com_10033_6814col_10033_6886
Helmholtz Zentrum für Infektionsforschung Repository
author
Reissmann, Silvana
author
Gillen, Christine M
author
Fulde, Marcus
author
Bergmann, René
author
Nerlich, Andreas
author
Rajkumari, Reena
author
Brahmadathan, Kootallur N
author
Chhatwal, Gursharan S
author
Nitsche-Schmitz, D Patric
department
Department of Microbial Pathogenesis, Helmholtz Centre for Infection Research, Braunschweig, Germany.
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
Region specific and worldwide distribution of collagen-binding M proteins with PARF motifs among human pathogenic streptococcal isolates.
Article
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