{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T22:54:31Z","timestamp":1791327271124,"version":"4.3.1"},"reference-count":66,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2013,10,20]],"date-time":"2013-10-20T00:00:00Z","timestamp":1382227200000},"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":[[2013,12]]},"abstract":"Summary<\/jats:title>Autotransporter (AT<\/jats:styled-content>) proteins are a broad class of virulence factors from Gram\u2010negative pathogens. AT<\/jats:styled-content> outer membrane (OM<\/jats:styled-content>) secretion appears simple in many regards, yet the mechanism that enables transport of the central AT<\/jats:styled-content> \u2018passenger\u2019 across the OM<\/jats:styled-content> remains unclear. OM<\/jats:styled-content> secretion efficiency for two AT<\/jats:styled-content> passengers is enhanced by a \u223c\u200920\u2009kDa stable core at the C<\/jats:styled-content>\u2010terminus of the passenger, but studies on a broader range of AT<\/jats:styled-content> proteins are needed in order to determine whether a stability difference between the passenger N<\/jats:styled-content>\u2010 and C<\/jats:styled-content>\u2010terminus represents a truly common mechanistic feature. Y<\/jats:styled-content>ersinia pestis<\/jats:italic>\u2005YapV<\/jats:styled-content> is homologous to S<\/jats:styled-content>higella flexneri<\/jats:italic>\u2005IcsA<\/jats:styled-content>, and like IcsA<\/jats:styled-content>, YapV<\/jats:styled-content> recruits mammalian neural W<\/jats:styled-content>iskott\u2013A<\/jats:styled-content>ldrich syndrome protein (N<\/jats:styled-content>\u2010WASP<\/jats:styled-content>). In vitro<\/jats:italic>, the purified YapV<\/jats:styled-content> passenger is functional and rich in \u03b2\u2010sheet structure, but lacks a \u223c\u200920\u2009kDa C<\/jats:styled-content>\u2010terminal stable core. However, the N<\/jats:styled-content>\u2010terminal 49 residues of the YapV<\/jats:styled-content> passenger globally destabilize the entire YapV<\/jats:styled-content> passenger, enhancing its OM<\/jats:styled-content> secretion efficiency. These results indicate that the contributions of AT<\/jats:styled-content> passenger sequences to OM<\/jats:styled-content> secretion efficiency extend beyond a C<\/jats:styled-content>\u2010terminal stable core, and highlight a role of the passenger N<\/jats:styled-content>\u2010terminus in reducing passenger stability in order to facilitate OM<\/jats:styled-content> secretion of some AT<\/jats:styled-content> proteins.<\/jats:p>","DOI":"10.1111\/mmi.12414","type":"journal-article","created":{"date-parts":[[2013,10,12]],"date-time":"2013-10-12T02:37:14Z","timestamp":1381545434000},"page":"1028-1045","source":"Crossref","is-referenced-by-count":21,"title":["An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C<\/scp>\u2010terminal stable core"],"prefix":"10.1111","volume":"90","author":[{"given":"Richard N.","family":"Besingi","sequence":"first","affiliation":[{"name":"Department of Chemistry & Biochemistry University of Notre Dame Notre Dame IN 46556 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie L.","family":"Chaney","sequence":"additional","affiliation":[{"name":"Department of Chemistry & Biochemistry University of Notre Dame Notre Dame IN 46556 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia L.","family":"Clark","sequence":"additional","affiliation":[{"name":"Department of Chemistry & Biochemistry University of Notre Dame Notre Dame IN 46556 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