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A myriad of infectious agents mimic vinculin binding sites (<jats:styled-content style=\"fixed-case\">VBS<\/jats:styled-content>), enabling them to hijack the adhesion machinery and facilitate cellular entry. Here, we report the structural and biochemical characterisation of <jats:styled-content style=\"fixed-case\">VBS<\/jats:styled-content> from the chlamydial virulence factor TarP. Whilst the affinities of isolated <jats:styled-content style=\"fixed-case\">VBS<\/jats:styled-content> peptides from TarP and talin for vinculin are similar, their behaviour in larger fragments is markedly different. In talin, <jats:styled-content style=\"fixed-case\">VBS<\/jats:styled-content> are cryptic and require mechanical activation to bind vinculin, whereas the TarP <jats:styled-content style=\"fixed-case\">VBS<\/jats:styled-content> are located in disordered regions, and so are constitutively active. We demonstrate that the TarP <jats:styled-content style=\"fixed-case\">VBS<\/jats:styled-content> can uncouple talin:vinculin complexes, which may lead to adhesion destabilisation.<\/jats:p>","DOI":"10.1002\/1873-3468.13074","type":"journal-article","created":{"date-parts":[[2018,4,30]],"date-time":"2018-04-30T22:15:13Z","timestamp":1525126513000},"page":"1751-1760","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Chlamydial virulence factor TarP mimics talin to disrupt the talin\u2010vinculin complex"],"prefix":"10.1002","volume":"592","author":[{"given":"Austin J.","family":"Whitewood","sequence":"first","affiliation":[{"name":"School of Biosciences University of Kent Canterbury UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abhimanyu K.","family":"Singh","sequence":"additional","affiliation":[{"name":"School of Biosciences University of Kent Canterbury 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