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Using nuclear magnetic resonance experiments, we identified residues on the \u03b21\u2010strand of <jats:italic>Brucella<\/jats:italic> VirB8 that undergo chemical shift changes in the presence of VirB10. Bacterial two\u2010hybrid experiments confirm the importance of the \u03b21\u2010strand, whereas phage display experiments suggest that the \u03b12\u2010helix of VirB8 may also contribute to the interaction with VirB10. Conjugation assays using the VirB8 homolog TraE as a model show that several residues on the \u03b21\u2010strand of TraE are important for T4SS function. Together, our results suggest that the \u03b21\u2010strand of VirB8\u2010like proteins is essential for their interaction with VirB10 in the T4SS complex.<\/jats:p>","DOI":"10.1002\/1873-3468.12770","type":"journal-article","created":{"date-parts":[[2017,8,2]],"date-time":"2017-08-02T09:58:25Z","timestamp":1501667905000},"page":"2491-2500","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["The type IV secretion system core component VirB8 interacts via the \u03b21\u2010strand with VirB10"],"prefix":"10.1002","volume":"591","author":[{"given":"Mahzad","family":"Sharifahmadian","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Medicine Faculty of Medicine Universit\u00e9 de Montr\u00e9al QC Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ingrid U.","family":"Nlend","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Medicine 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