Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex

Whitewood, Austin and Singh, Abhimanyu K and Brown, David G. and Goult, Benjamin T (2018) Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex. FEBS Letters, 592 (10). pp. 1751-1760. ISSN 0014-5793. (doi:https://doi.org/10.1002/1873-3468.13074) (Full text available)

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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 a 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: talin, vinculin, chlamydia, adhesion, molecular mimicry, crystallography
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Ben Goult
Date Deposited: 01 May 2018 12:46 UTC
Last Modified: 01 Jun 2018 08:39 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/66883 (The current URI for this page, for reference purposes)
Goult, Benjamin T: https://orcid.org/0000-0002-3438-2807
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