Unknown

Dataset Information

0

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


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.

SUBMITTER: Marjenberg ZR 

PROVIDER: S-EPMC3023484 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Marjenberg Zoe R ZR   Ellis Ian R IR   Hagan Robert M RM   Prabhakaran Sabitha S   Höök Magnus M   Talay Susanne R SR   Potts Jennifer R JR   Staunton David D   Schwarz-Linek Ulrich U  

The Journal of biological chemistry 20101108 3


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  ...[more]

Similar Datasets

| S-EPMC3262099 | biostudies-literature
| S-EPMC5448106 | biostudies-literature
| S-EPMC96575 | biostudies-literature
| S-EPMC98132 | biostudies-literature
| S-EPMC3682544 | biostudies-literature
| S-EPMC115982 | biostudies-literature
| S-EPMC7587433 | biostudies-literature
| S-EPMC1594942 | biostudies-literature
| S-EPMC2894786 | biostudies-literature
| S-EPMC4683274 | biostudies-literature