{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T05:30:03Z","timestamp":1792647003090,"version":"4.5.0"},"reference-count":94,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2013,10,16]],"date-time":"2013-10-16T00:00:00Z","timestamp":1381881600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2013,11]]},"abstract":"Summary<\/jats:title>Enterotoxigenic E<\/jats:styled-content>scherichia coli<\/jats:italic> (ETEC<\/jats:styled-content>) colonize the human gut, causing severe cholera\u2010like diarrhoea. ETEC<\/jats:styled-content> utilize a diverse array of pili and fimbriae for host colonization, including the T<\/jats:styled-content>ype IVb<\/jats:styled-content> pilus CFA<\/jats:styled-content>\/III<\/jats:styled-content>. The CFA<\/jats:styled-content>\/III<\/jats:styled-content> pilus machinery is encoded on the cof<\/jats:italic><\/jats:styled-content> operon, which is similar in gene sequence and synteny to the tcp<\/jats:italic><\/jats:styled-content> operon that encodes another T<\/jats:styled-content>ype IVb<\/jats:styled-content> pilus, the V<\/jats:styled-content>ibrio cholerae<\/jats:italic> toxin co\u2010regulated pilus (TCP<\/jats:styled-content>). Both pilus operons possess a syntenic gene encoding a protein of unknown function. In V<\/jats:styled-content>.\u2009cholerae<\/jats:italic>, this protein, TcpF<\/jats:styled-content>, is a critical colonization factor secreted by the TCP<\/jats:styled-content> apparatus. Here we show that the corresponding ETEC<\/jats:styled-content> protein, CofJ<\/jats:styled-content>, is a soluble protein secreted via the CFA<\/jats:styled-content>\/III<\/jats:styled-content> apparatus. We present a 2.6 \u00c5 resolution crystal structure of CofJ<\/jats:styled-content>, revealing a large \u03b2\u2010sandwich protein that bears no sequence or structural homology to TcpF<\/jats:styled-content>. CofJ<\/jats:styled-content> has a cluster of exposed hydrophobic side\u2010chains at one end and structural homology to the pore\u2010forming proteins perfringolysin O<\/jats:styled-content> and \u03b1\u2010haemolysin. CofJ<\/jats:styled-content> binds to lipid vesicles and epithelial cells, suggesting a role in membrane attachment during ETEC<\/jats:styled-content> colonization.<\/jats:p>","DOI":"10.1111\/mmi.12407","type":"journal-article","created":{"date-parts":[[2013,10,11]],"date-time":"2013-10-11T22:10:02Z","timestamp":1381529402000},"page":"898-918","source":"Crossref","is-referenced-by-count":20,"title":["Structure and secretion of CofJ<\/scp>, a putative colonization factor of enterotoxigenic E<\/scp>scherichia coli<\/i>"],"prefix":"10.1111","volume":"90","author":[{"given":"Alex S. 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