{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:07:52Z","timestamp":1790518072892,"version":"4.1.0"},"reference-count":63,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2011,11,4]],"date-time":"2011-11-04T00:00:00Z","timestamp":1320364800000},"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":[[2011,12]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Complement evasion is an important survival strategy of <jats:italic>Neisseria meningitidis<\/jats:italic> (Nm) during colonization and infection. Previously, we have shown that Nm Opc binds to serum vitronectin to inhibit complement\u2010mediated killing. In this study, we demonstrate meningococcal interactions with vitronectin via a novel adhesin, Msf (meningococcal surface fibril, previously NhhA or Hsf). As with Opc, Msf binds preferentially to activated vitronectin (aVn), engaging at its N\u2010terminal region but the C\u2010terminal heparin binding domain may also participate. However, unlike Opc, the latter binding is not heparin\u2010mediated. By binding to aVn, Msf or Opc can impart serum resistance, which is further increased in coexpressers, a phenomenon dependent on serum aVn concentrations. The survival fitness of aVn\u2010binding derivatives was evident from mixed population studies, in which <jats:italic>msf\/opc<\/jats:italic> mutants were preferentially depleted. In addition, using vitronectin peptides to block Msf\u2013aVn interactions, aVn\u2010induced inhibition of lytic C5b\u20109 formation and of serum killing could be reversed. As Msf\u2010encoding gene is ubiquitous in the meningococcal strains examined and is expressed <jats:italic>in vivo<\/jats:italic>, serum resistance via Msf may be of significance to meningococcal pathogenesis. The data imply that vitronectin binding may be an important strategy for the <jats:italic>in vivo<\/jats:italic> survival of Nm for which the bacterium has evolved redundant mechanisms.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07876.x","type":"journal-article","created":{"date-parts":[[2011,11,4]],"date-time":"2011-11-04T10:13:38Z","timestamp":1320401618000},"page":"1129-1149","source":"Crossref","is-referenced-by-count":48,"title":["Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance"],"prefix":"10.1111","volume":"82","author":[{"given":"Natalie J.","family":"Griffiths","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Darryl 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