{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:08:18Z","timestamp":1790518098228,"version":"4.1.0"},"reference-count":59,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2018,10,26]],"date-time":"2018-10-26T00:00:00Z","timestamp":1540512000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100005440","name":"Center for Scientific Review","doi-asserted-by":"publisher","award":["NIAID AI133570"],"award-info":[{"award-number":["NIAID AI133570"]}],"id":[{"id":"10.13039\/100005440","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2019,1]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Ail, a multifunctional outer membrane protein of <jats:italic>Yersinia pestis<\/jats:italic>, confers cell binding, Yop delivery and serum resistance activities. Resistance to complement proteins in serum is critical for the survival of <jats:italic>Y. pestis <\/jats:italic>during the septicemic stage of plague infections. Bacteria employ a variety of tactics to evade the complement system, including recruitment of complement regulatory factors, such as factor H, C4b\u2010binding protein (C4BP) and vitronectin (Vn). <jats:italic>Y. pestis <\/jats:italic>Ail interacts with the regulatory factors Vn and C4BP, and Ail homologs from <jats:italic>Y. enterocolitica <\/jats:italic>and <jats:italic>Y. pseudotuberculosis <\/jats:italic>recruit factor H. Using co\u2010sedimentation assays, we demonstrate that two surface\u2010exposed amino acids, F80 and F130, are required for the interaction of <jats:italic>Y. pestis <\/jats:italic>Ail with Vn, factor H and C4BP. However, although Ail\u2010F80A\/F130A fails to interact with these complement regulatory proteins, it still confers 10,000\u2010fold more serum resistance than a \u0394<jats:italic>ail <\/jats:italic>strain and prevents C9 polymerization, potentially by directly interfering with MAC assembly. Using site\u2010directed mutagenesis, we further defined this additional mechanism of complement evasion conferred by Ail. Finally, we find that at <jats:italic>Y. pestis<\/jats:italic> concentrations reflective of early\u2010stage septicemic plague, Ail weakly recruits Vn and fails to recruit factor H, suggesting that this alternative mechanism of serum resistance may be essential during plague infection.<\/jats:p>","DOI":"10.1111\/mmi.14140","type":"journal-article","created":{"date-parts":[[2018,9,27]],"date-time":"2018-09-27T13:04:46Z","timestamp":1538053486000},"page":"82-95","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":34,"title":["Ail provides multiple mechanisms of serum resistance to <i>Yersinia pestis<\/i>"],"prefix":"10.1111","volume":"111","author":[{"given":"Joshua J.","family":"Thomson","sequence":"first","affiliation":[{"name":"Division of Integrated Biomedical Sciences University of Detroit Mercy School of Dentistry Detroit MI USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah 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