2.50
Hdl Handle:
http://hdl.handle.net/10033/142010
Title:
Cooperative binding and activation of fibronectin by a bacterial surface protein.
Authors:
Marjenberg, Zoe R; Ellis, Ian R; Hagan, Robert M; Prabhakaran, Sabitha; Höök, Magnus; Talay, Susanne R; Potts, Jennifer R; Staunton, David; Schwarz-Linek, Ulrich
Abstract:
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.
Affiliation:
Biomedical Sciences Research Complex, University of St. Andrews, St. Andrews KY16 9ST, Scotland, United Kingdom.
Citation:
Cooperative binding and activation of fibronectin by a bacterial surface protein. 2011, 286 (3):1884-94 J. Biol. Chem.
Journal:
The Journal of biological chemistry
Issue Date:
21-Jan-2011
URI:
http://hdl.handle.net/10033/142010
DOI:
10.1074/jbc.M110.183053
PubMed ID:
21059652
Type:
Article
Language:
en
ISSN:
1083-351X
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorMarjenberg, Zoe Ren
dc.contributor.authorEllis, Ian Ren
dc.contributor.authorHagan, Robert Men
dc.contributor.authorPrabhakaran, Sabithaen
dc.contributor.authorHöök, Magnusen
dc.contributor.authorTalay, Susanne Ren
dc.contributor.authorPotts, Jennifer Ren
dc.contributor.authorStaunton, Daviden
dc.contributor.authorSchwarz-Linek, Ulrichen
dc.date.accessioned2011-09-09T08:48:51Z-
dc.date.available2011-09-09T08:48:51Z-
dc.date.issued2011-01-21-
dc.identifier.citationCooperative binding and activation of fibronectin by a bacterial surface protein. 2011, 286 (3):1884-94 J. Biol. Chem.en
dc.identifier.issn1083-351X-
dc.identifier.pmid21059652-
dc.identifier.doi10.1074/jbc.M110.183053-
dc.identifier.urihttp://hdl.handle.net/10033/142010-
dc.description.abstractIntegrin-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
dc.language.isoenen
dc.subject.meshAdhesins, Bacterialen
dc.subject.meshBinding Sitesen
dc.subject.meshCells, Cultureden
dc.subject.meshFibroblastsen
dc.subject.meshFibronectinsen
dc.subject.meshHumansen
dc.subject.meshProtein Bindingen
dc.subject.meshStreptococcus pyogenesen
dc.titleCooperative binding and activation of fibronectin by a bacterial surface protein.en
dc.typeArticleen
dc.contributor.departmentBiomedical Sciences Research Complex, University of St. Andrews, St. Andrews KY16 9ST, Scotland, United Kingdom.en
dc.identifier.journalThe Journal of biological chemistryen

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