Loading...
Cooperative binding and activation of fibronectin by a bacterial surface protein.
Marjenberg, Zoe R Ellis, Ian R Hagan, Robert M Prabhakaran, Sabitha Höök, Magnus Talay, Susanne R Potts, Jennifer R Staunton, David Schwarz-Linek, Ulrich
Marjenberg, Zoe R
Ellis, Ian R
Hagan, Robert M
Prabhakaran, Sabitha
Höök, Magnus
Talay, Susanne R
Potts, Jennifer R
Staunton, David
Schwarz-Linek, Ulrich
Citations
Altmetric:
Advisors
Editors
Other Contributors
Issue Date
2011-01-21
Submitted date
Files
Loading...
original manuscript
Adobe PDF, 2.24 MB
Other Titles
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.
Citation
Cooperative binding and activation of fibronectin by a bacterial surface protein. 2011, 286 (3):1884-94 J. Biol. Chem.
Publisher
PubMed ID
PubMed Central ID
Additional Links
Embedded video
Type
Article
Language
en
Description
Series/Report no.
ISSN
1083-351X