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The molecular mechanism by which <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009bavariensis<\/jats:italic> overcomes innate immunity, in particular, complement remains elusive. In contrast to other serum\u2010resistant spirochetes, none of the <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009bavariensis<\/jats:italic> isolates investigated bound complement regulators of the alternative (<jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content>) and classical pathway (<jats:styled-content style=\"fixed-case\">CP<\/jats:styled-content>) or proteolytically inactivated complement components. Focusing on outer surface proteins <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>66 and <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>71, we demonstrated that both molecules either inhibit <jats:styled-content style=\"fixed-case\">AP<\/jats:styled-content>, <jats:styled-content style=\"fixed-case\">CP<\/jats:styled-content> and terminal pathway (<jats:styled-content style=\"fixed-case\">TP<\/jats:styled-content>) activation, or block activation of the <jats:styled-content style=\"fixed-case\">CP<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">TP<\/jats:styled-content> respectively. Both molecules bind complement components <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>7, <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>8 and <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>9, and thereby prevent assembly of the terminal complement complex. This inhibitory activity was confirmed by the introduction of the <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>66 and <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>71 encoding genes into a serum\u2010sensitive <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009garinii<\/jats:italic> strain. Transformed spirochetes producing either <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>66 or <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>71 overcome complement\u2010mediated killing, thus indicating that both proteins independently facilitate serum resistance of <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009bavariensis<\/jats:italic>. The generation of <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>\u2010terminally truncated proteins as well as a chimeric <jats:styled-content style=\"fixed-case\">BGA<\/jats:styled-content>71 protein lead to the localization of the complement\u2010interacting binding site within the <jats:styled-content style=\"fixed-case\">N<\/jats:styled-content>\u2010terminus. Collectively, our data reveal a novel immune evasion strategy of <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009bavariensis<\/jats:italic> that is directed against the activation of the <jats:styled-content style=\"fixed-case\">TP<\/jats:styled-content>.<\/jats:p>","DOI":"10.1111\/mmi.13239","type":"journal-article","created":{"date-parts":[[2015,10,5]],"date-time":"2015-10-05T11:30:44Z","timestamp":1444044644000},"page":"407-424","source":"Crossref","is-referenced-by-count":55,"title":["BGA66 and BGA71 facilitate complement resistance of <i>Borrelia bavariensis<\/i> by inhibiting assembly of the membrane attack complex"],"prefix":"10.1111","volume":"99","author":[{"given":"Claudia","family":"Hammerschmidt","sequence":"first","affiliation":[{"name":"Institute of Medical Microbiology and Infection Control University Hospital of Frankfurt  Frankfurt 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