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It was previously shown that the presence of the bile salts glycocholate and taurocholate in the small intestine causes dimerization of the transmembrane transcription factor TcpP by inducing intermolecular disulphide bonds in the TcpP periplasmic domain. In this study, they further investigated the mechanism of how taurocholate affects <jats:italic>V. cholerae<\/jats:italic> virulence determinants. <jats:italic>In vitro<\/jats:italic> assay of TcpP oxidation by VcDsbA showed that VcDsbA induced TcpP dimerization in the presence of taurocholate. Taurocholate bound to VcDsbA with a <jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub> of 40\u2009\u00b1\u20092.5 \u03bcM, and also bound other Dsb proteins, including EcDsbA, EcDsbC and VcDsbC. Taurocholate inhibited VcDsbA reductase activity without affecting VcDsbA secondary structure or thermostability. VcDsbA and its substrates were more extensively reduced in the presence of taurocholate, as compared with their redox state in the absence of taurocholate. The data presented here not only provide new insights into the mechanism by which bile salts induce <jats:italic>V. cholerae<\/jats:italic> virulence but also suggest a means by which to develop inhibitors against DsbA.<\/jats:p>","DOI":"10.1111\/mmi.13497","type":"journal-article","created":{"date-parts":[[2016,9,9]],"date-time":"2016-09-09T21:17:47Z","timestamp":1473455867000},"page":"909-924","source":"Crossref","is-referenced-by-count":30,"title":["Redox pathway sensing bile salts activates virulence gene expression in <i><scp>V<\/scp>ibrio cholerae<\/i>"],"prefix":"10.1111","volume":"102","author":[{"given":"Yuanyuan","family":"Xue","sequence":"first","affiliation":[{"name":"College of Animal Science &amp; Technology, China\u2010Australia Joint\u2010Laboratory for Animal Health Big Data Analytics, Zhejiang Provincial Engineering Laboratory for Animal Health Inspection &amp; Internet Technology, Zhejiang A&amp;F University Lin'an 311300 Zhejiang Province 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