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

DOI: 10.1002/1873-3468.13074 DOI Help

Authors: Austin Whitewood (University of Kent) , Abhimanyu K. Singh (University of Kent) , David G. Brown (University of Kent) , Benjamin T. Goult (University of Kent)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: April 2018
Diamond Proposal Number(s): 15075

Open Access Open Access

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.

Journal Keywords: talin; vinculin; chlamydia; adhesion; molecular mimicry; crystallography

Diamond Keywords: Chlamydia; Bacteria

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Added On: 01/05/2018 09:21


Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)