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dc.contributor.authorMarjenberg, Zoe R
dc.contributor.authorEllis, Ian R
dc.contributor.authorHagan, Robert M
dc.contributor.authorPrabhakaran, Sabitha
dc.contributor.authorHöök, Magnus
dc.contributor.authorTalay, Susanne R
dc.contributor.authorPotts, Jennifer R
dc.contributor.authorStaunton, David
dc.contributor.authorSchwarz-Linek, Ulrich
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.
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
refterms.dateFOA2018-06-12T22:16:51Z
html.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.


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