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Previous studies indicate that a putative lipoprotein, <jats:styled-content style=\"fixed-case\">BBA<\/jats:styled-content>33, is produced in an <jats:styled-content style=\"fixed-case\">RpoS<\/jats:styled-content>\u2010dependent manner under conditions that mimic the mammalian component of the borrelial lifecycle. However, the significance and function for <jats:styled-content style=\"fixed-case\">BBA<\/jats:styled-content>33 is not known. Given its linkage to the <jats:styled-content style=\"fixed-case\">BosR\/Rrp2\u2010RpoN\u2010RpoS<\/jats:styled-content> regulatory cascade, we hypothesized that <jats:styled-content style=\"fixed-case\">BBA<\/jats:styled-content>33 facilitates <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009burgdorferi<\/jats:italic> infection in the mammalian host. The deletion of <jats:italic>bba33<\/jats:italic> eliminated <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content><jats:italic>.\u2009burgdorferi<\/jats:italic> infectivity in <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>3<jats:styled-content style=\"fixed-case\">H<\/jats:styled-content> mice, which was rescued by genetic complementation with intact <jats:italic>bba33<\/jats:italic>. With regard to function, a combinatorial peptide approach, coupled with subsequent <jats:italic>in vitro<\/jats:italic> binding assays, indicated that <jats:styled-content style=\"fixed-case\">BBA<\/jats:styled-content>33 binds to collagen type <jats:styled-content style=\"fixed-case\">VI<\/jats:styled-content> and, to a lesser extent, collagen type <jats:styled-content style=\"fixed-case\">IV<\/jats:styled-content>. Whole cell binding assays demonstrated <jats:styled-content style=\"fixed-case\">BBA<\/jats:styled-content>33\u2010dependent binding to human collagen type <jats:styled-content style=\"fixed-case\">VI<\/jats:styled-content>. Taken together, these results suggest that <jats:styled-content style=\"fixed-case\">BBA<\/jats:styled-content>33 interacts with collagenous structures and may function as an adhesin in a process that is required to prevent bacterial clearance.<\/jats:p>","DOI":"10.1111\/mmi.12921","type":"journal-article","created":{"date-parts":[[2015,1,6]],"date-time":"2015-01-06T07:13:45Z","timestamp":1420528425000},"page":"68-83","source":"Crossref","is-referenced-by-count":21,"title":["The <scp>BBA<\/scp>33 lipoprotein binds collagen and impacts <scp><i>B<\/i><\/scp><i>orrelia burgdorferi<\/i> pathogenesis"],"prefix":"10.1111","volume":"96","author":[{"given":"Hui","family":"Zhi","sequence":"first","affiliation":[{"name":"Department of Microbial Pathogenesis and Immunology College of Medicine Texas A&amp;M Health Science Center  Bryan TX 77807 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eric H.","family":"Weening","sequence":"additional","affiliation":[{"name":"Department of Microbial Pathogenesis and Immunology College of Medicine Texas A&amp;M Health Science Center  Bryan TX 77807 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elena Magda","family":"Barbu","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases The University of Texas M. 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