Whitewood, Austin J 
ORCID: 0000-0002-8255-8248, Singh, Abhimanyu K ORCID: 0000-0002-9998-020X, Brown, David G and Goult, Benjamin T ORCID: 0000-0002-3438-2807
(2018)
Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex.
FEBS letters, 592 (10).
pp. 1751-1760.
|
PDF
Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex.pdf - Open Access published version Download (1MB) | Preview |
Abstract
Vinculin is a central component of mechanosensitive adhesive complexes that form between cells and the extracellular matrix. A myriad of infectious agents mimic vinculin binding sites (VBS), enabling them to hijack the adhesion machinery and facilitate cellular entry. Here, we report the structural and biochemical characterisation of VBS from the chlamydial virulence factor TarP. Whilst the affinities of isolated VBS peptides from TarP and talin for vinculin are similar, their behaviour in larger fragments is markedly different. In talin, VBS are cryptic and require mechanical activation to bind vinculin, whereas the TarP VBS are located in disordered regions, and so are constitutively active. We demonstrate that the TarP VBS can uncouple talin:vinculin complexes, which may lead to adhesion destabilisation.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Chlamydia, Bacterial Proteins, Talin, Vinculin, Virulence Factors, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Molecular Mimicry, Amino Acid Sequence, Protein Conformation, Protein Binding, Sequence Homology, Amino Acid, Models, Molecular |
| Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 13 Mar 2024 09:55 |
| Last Modified: | 13 Mar 2024 09:55 |
| DOI: | 10.1002/1873-3468.13074 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3179320 |
Dimensions
Dimensions
