{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:48:08Z","timestamp":1791276488614,"version":"4.1.0"},"reference-count":32,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2014,1,13]],"date-time":"2014-01-13T00:00:00Z","timestamp":1389571200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[2014,3]]},"abstract":"The outer membrane protein A<\/jats:styled-content>il of Y<\/jats:styled-content>ersinia pestis<\/jats:italic> mediates several virulence functions, including serum resistance. Here, we demonstrate that A<\/jats:styled-content>il binds C<\/jats:styled-content>4b\u2010binding protein (C<\/jats:styled-content>4BP<\/jats:styled-content>), the primary fluid\u2010phase regulator of the classical and lectin pathways. Non\u2010covalent binding of C<\/jats:styled-content>4 and C<\/jats:styled-content>4b to A<\/jats:styled-content>il was also observed. C<\/jats:styled-content>4BP<\/jats:styled-content> bound to A<\/jats:styled-content>il can act as a cofactor to the serine protease factor I (fI) in the cleavage of fluid\u2010phase C<\/jats:styled-content>4b. Employing a panel of C<\/jats:styled-content>4BP<\/jats:styled-content> alpha\u2010chain mutants, we observed that the absence of complement control protein domain 6 and 8 reduced binding to Ail. Immunoblot analysis of normal human serum (NHS<\/jats:styled-content>)\u2010treated bacteria revealed minimal C<\/jats:styled-content>4b alpha\u2019\u2010chain complexes with bacterial outer membrane targets. Addition of the anti\u2010C<\/jats:styled-content>4BP<\/jats:styled-content> monoclonal antibody MK<\/jats:styled-content>104 to NHS<\/jats:styled-content> restored C<\/jats:styled-content>4b\u2010alpha\u2019 chain target complexes, suggesting that C<\/jats:styled-content>4b binds covalently to targets on the Y. pestis<\/jats:italic> surface. C4b bound to A<\/jats:styled-content>il noncovalently was also cleaved in a C<\/jats:styled-content>4BP<\/jats:styled-content> and fI\u2010dependent manner, leaving the C<\/jats:styled-content>4c fragment bound to A<\/jats:styled-content>il. MK<\/jats:styled-content>104 also prevented the cleavage of noncovalently bound C<\/jats:styled-content>4b. Collectively, these data suggest that when C<\/jats:styled-content>4BP<\/jats:styled-content> is bound to A<\/jats:styled-content>il, fI can cleave and inactivate C<\/jats:styled-content>4b that has bound covalently to bacterial surface structures as well as C<\/jats:styled-content>4b bound noncovalently to A<\/jats:styled-content>il.<\/jats:p>","DOI":"10.1002\/eji.201343552","type":"journal-article","created":{"date-parts":[[2013,12,2]],"date-time":"2013-12-02T09:47:00Z","timestamp":1385977620000},"page":"742-751","source":"Crossref","is-referenced-by-count":32,"title":["Yersinia pestis<\/i>A<\/scp>il recruitment of C<\/scp>4b\u2010binding protein leads to factor I\u2010mediated inactivation of covalently and noncovalently bound C<\/scp>4b"],"prefix":"10.1002","volume":"44","author":[{"given":"Derek K.","family":"Ho","sequence":"first","affiliation":[{"name":"Immunobiology Program, Department of Bacteriology and Immunology Haartman Institute, University of Helsinki Helsinki Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikael","family":"Skurnik","sequence":"additional","affiliation":[{"name":"Immunobiology Program, Department of Bacteriology and Immunology Haartman Institute, University of Helsinki Helsinki Finland"},{"name":"HUSLAB Helsinki University Central Hospital Helsinki Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna M.","family":"Blom","sequence":"additional","affiliation":[{"name":"Division of Medical Protein Chemistry Lund University Department of Laboratory Medicine Malm\u00f6 Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seppo","family":"Meri","sequence":"additional","affiliation":[{"name":"Immunobiology Program, Department of Bacteriology and Immunology Haartman Institute, University of Helsinki Helsinki Finland"},{"name":"HUSLAB Helsinki University Central Hospital Helsinki 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