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J Biol Chem. 2011 Jan 21;286(3):1884-94. doi: 10.1074/jbc.M110.183053. Epub 2010 Nov 8.

Cooperative binding and activation of fibronectin by a bacterial surface protein.

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1
Biomedical Sciences Research Complex, University of St. Andrews, St. Andrews KY16 9ST, Scotland, United Kingdom.

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.

PMID:
21059652
PMCID:
PMC3023484
DOI:
10.1074/jbc.M110.183053
[Indexed for MEDLINE]
Free PMC Article
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