2.50
Hdl Handle:
http://hdl.handle.net/10033/556926
Title:
An internal thioester in a pathogen surface protein mediates covalent host binding.
Authors:
Walden, Miriam; Edwards, John M; Dziewulska, Aleksandra M; Bergmann, Rene; Saalbach, Gerhard; Kan, Su-Yin; Miller, Ona K; Weckener, Miriam; Jackson, Rosemary J; Shirran, Sally L; Botting, Catherine H; Florence, Gordon J; Rohde, Manfred ( 0000-0003-0522-3580 ) ; Banfield, Mark J; Schwarz-Linek, Ulrich
Abstract:
To cause disease and persist in a host, pathogenic and commensal microbes must adhere to tissues. Colonization and infection depend on specific molecular interactions at the host-microbe interface that involve microbial surface proteins, or adhesins. To date, adhesins are only known to bind to host receptors non-covalently. Here we show that the streptococcal surface protein SfbI mediates covalent interaction with the host protein fibrinogen using an unusual internal thioester bond as a 'chemical harpoon'. This cross-linking reaction allows bacterial attachment to fibrin and SfbI binding to human cells in a model of inflammation. Thioester-containing domains are unexpectedly prevalent in Gram-positive bacteria, including many clinically relevant pathogens. Our findings support bacterial-encoded covalent binding as a new molecular principle in host-microbe interactions. This represents an as yet unexploited target to treat bacterial infection and may also offer novel opportunities for engineering beneficial interactions.
Affiliation:
Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.
Citation:
An internal thioester in a pathogen surface protein mediates covalent host binding. 2015, 4: Elife
Journal:
eLife
Issue Date:
2015
URI:
http://hdl.handle.net/10033/556926
DOI:
10.7554/eLife.06638
PubMed ID:
26032562
Type:
Article
Language:
en
ISSN:
2050-084X
Appears in Collections:
publications of the central unit for microscopy (ZEIM)

Full metadata record

DC FieldValue Language
dc.contributor.authorWalden, Miriamen
dc.contributor.authorEdwards, John Men
dc.contributor.authorDziewulska, Aleksandra Men
dc.contributor.authorBergmann, Reneen
dc.contributor.authorSaalbach, Gerharden
dc.contributor.authorKan, Su-Yinen
dc.contributor.authorMiller, Ona Ken
dc.contributor.authorWeckener, Miriamen
dc.contributor.authorJackson, Rosemary Jen
dc.contributor.authorShirran, Sally Len
dc.contributor.authorBotting, Catherine Hen
dc.contributor.authorFlorence, Gordon Jen
dc.contributor.authorRohde, Manfreden
dc.contributor.authorBanfield, Mark Jen
dc.contributor.authorSchwarz-Linek, Ulrichen
dc.date.accessioned2015-06-15T14:10:13Zen
dc.date.available2015-06-15T14:10:13Zen
dc.date.issued2015en
dc.identifier.citationAn internal thioester in a pathogen surface protein mediates covalent host binding. 2015, 4: Elifeen
dc.identifier.issn2050-084Xen
dc.identifier.pmid26032562en
dc.identifier.doi10.7554/eLife.06638en
dc.identifier.urihttp://hdl.handle.net/10033/556926en
dc.description.abstractTo cause disease and persist in a host, pathogenic and commensal microbes must adhere to tissues. Colonization and infection depend on specific molecular interactions at the host-microbe interface that involve microbial surface proteins, or adhesins. To date, adhesins are only known to bind to host receptors non-covalently. Here we show that the streptococcal surface protein SfbI mediates covalent interaction with the host protein fibrinogen using an unusual internal thioester bond as a 'chemical harpoon'. This cross-linking reaction allows bacterial attachment to fibrin and SfbI binding to human cells in a model of inflammation. Thioester-containing domains are unexpectedly prevalent in Gram-positive bacteria, including many clinically relevant pathogens. Our findings support bacterial-encoded covalent binding as a new molecular principle in host-microbe interactions. This represents an as yet unexploited target to treat bacterial infection and may also offer novel opportunities for engineering beneficial interactions.en
dc.language.isoenen
dc.titleAn internal thioester in a pathogen surface protein mediates covalent host binding.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.en
dc.identifier.journaleLifeen

Related articles on PubMed

This item is licensed under a Creative Commons License
Creative Commons
All Items in HZI are protected by copyright, with all rights reserved, unless otherwise indicated.