{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T07:10:10Z","timestamp":1780384210689,"version":"3.54.1"},"reference-count":62,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2011,12,11]],"date-time":"2011-12-11T00:00:00Z","timestamp":1323561600000},"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":[[2012,1]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>The etiological agent of Lyme disease, <jats:italic>Borrelia burgdorferi<\/jats:italic>, is transmitted by ticks of the <jats:italic>Ixodes<\/jats:italic> genus and, if untreated, can cause significant morbidity in affected individuals. Recent reports have shown that polyunsaturated fatty acids in the <jats:italic>B.\u2003burgdorferi<\/jats:italic> cell envelope are potential targets for oxidative damage, which can be lethal. How <jats:italic>B.\u2003burgdorferi<\/jats:italic> responds to this assault is not known. Herein we report evidence that <jats:italic>bb0646<\/jats:italic> codes for a lipase that is located within the <jats:italic>bosR<\/jats:italic> operon and that has specificity for both saturated and polyunsaturated fatty acids. Specifically, strains harbouring mutated copies of the lipase, either in the form of an insertionally inactivated construct or site\u2010directed mutations within the active site, demonstrated attenuated lipolytic and haemolytic phenotypes when compared with the isogenic parent and <jats:italic>trans\u2010<\/jats:italic>complements. <jats:italic>In vivo<\/jats:italic> analysis showed that while the <jats:italic>bb0646<\/jats:italic> mutant remains infectious, the spirochaetal load is significantly lower than both the isogenic parent and the complemented mutant strains. Taken together, these data demonstrate that BB0646 is a broad substrate specific lipase that contributes to lipolytic and haemolytic activity <jats:italic>in vitro<\/jats:italic> and is required for optimal <jats:italic>B.\u2003burgdorferi<\/jats:italic> infection.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07932.x","type":"journal-article","created":{"date-parts":[[2011,12,12]],"date-time":"2011-12-12T05:25:30Z","timestamp":1323667530000},"page":"319-334","source":"Crossref","is-referenced-by-count":16,"title":["The BB0646 protein demonstrates lipase and haemolytic activity associated with <i>Borrelia burgdorferi<\/i>, the aetiological agent of Lyme disease"],"prefix":"10.1111","volume":"83","author":[{"given":"Dana K.","family":"Shaw","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jenny A.","family":"Hyde","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jon 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