{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T21:09:27Z","timestamp":1791148167071,"version":"4.1.0"},"reference-count":65,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"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":[[2006,9]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p> <jats:italic>Borrelia burgdorferi<\/jats:italic>, the aetiological agent of Lyme disease, employs sophisticated means to survive in diverse mammalian hosts. Recent studies demonstrated that acquisition of complement regulators factor H and factor H\u2010like protein\u20101 (FHL\u20101) allows spirochetes to resist complement\u2010mediated killing. Serum\u2010resistant <jats:italic>B.\u2003burgdorferi<\/jats:italic> express up to five distinct complement regulator\u2010acquiring surface proteins (CRASPs) that bind factor H and\/or FHL\u20101. In this study we have identified and characterized one of those <jats:italic>B.\u2003burgdorferi<\/jats:italic> proteins, named BbCRASP\u20102. BbCRASP\u20102 is distinct from the four previously identified factor H\/FHL\u20101\u2010binding CRASPs of <jats:italic>B.\u2003burgdorferi<\/jats:italic> strains. The single copy of the gene encoding BbCRASP\u20102, <jats:italic>cspZ<\/jats:italic>, is located on the linear plasmid lp28\u20103. BbCRASP\u20102 is highly divergent from the factor H\/FHL\u20101\u2010binding protein BbCRASP\u20101 and from members of the factor H\u2010binding Erp (OspE\/F\u2010related) protein family. Peptide mapping analysis revealed that the factor H\/FHL\u20101 binding site is discontinuous and it was found that C\u2010terminal truncations abrogate factor H and FHL\u20101 binding. The predominant BbCRASP\u20102 binding site of both host complement regulators was mapped to the short consensus repeat 7 (SCR 7). Factor H and FHL\u20101 bound to BbCRASP\u20102 maintain cofactor activity for factor I\u2010mediated C3b inactivation and accelerate the decay of the C3 convertase. Expression of BbCRASP\u20102 in serum\u2010sensitive <jats:italic>B.\u2003burgdorferi<\/jats:italic> mutant B313 increased resistance to complement\u2010mediated lysis. The characterization of BbCRASP\u20102 now provides a complete picture of the three diverse complement regulator\u2010binding protein families of <jats:italic>B.\u2003burgdorferi<\/jats:italic> yielding new insights into the pathogenesis of Lyme disease.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2006.05318.x","type":"journal-article","created":{"date-parts":[[2006,8,2]],"date-time":"2006-08-02T14:14:46Z","timestamp":1154528086000},"page":"1220-1236","source":"Crossref","is-referenced-by-count":139,"title":["Functional characterization of BbCRASP\u20102, a distinct outer membrane protein of <i>Borrelia burgdorferi<\/i> that binds host complement regulators factor H and FHL\u20101"],"prefix":"10.1111","volume":"61","author":[{"given":"Kristina","family":"Hartmann","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carsten","family":"Corvey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Skerka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Kirschfink","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Karas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Volker","family":"Brade","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer 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