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Here, we extend our analyses to the contribution of CRASP-4 in mediating complement resistance of<jats:italic>B. burgdorferi<\/jats:italic>and its interaction with human complement regulators. CRASP-4 (also known as ErpC) was immobilized onto magnetic beads and used to capture proteins from human serum. Following Western blotting, factor H (CFH), CFH-related protein 1 (CFHR1), CFHR2, and CFHR5 were identified as ligands of CRASP-4. To analyze the impact of native CRASP-4 on mediating survival of serum-sensitive cells in human serum, a<jats:italic>B. garinii<\/jats:italic>strain was generated that ectopically expresses CRASP-4. CRASP-4-producing bacteria bound CFHR1, CFHR2, and CFHR5 but not CFH. In addition, transformed spirochetes deposited significant amounts of lethal complement components on their surface and were susceptible to human serum, thus indicating that CRASP-4 plays a subordinate role in complement resistance of<jats:italic>B. burgdorferi<\/jats:italic>.<\/jats:p>","DOI":"10.1155\/2012\/349657","type":"journal-article","created":{"date-parts":[[2012,1,30]],"date-time":"2012-01-30T21:00:26Z","timestamp":1327957226000},"page":"1-12","source":"Crossref","is-referenced-by-count":33,"title":["Contribution of the Infection-Associated Complement Regulator-Acquiring Surface Protein 4 (ErpC) to Complement Resistance of<i>Borrelia burgdorferi<\/i>"],"prefix":"10.1155","volume":"2012","author":[{"given":"Claudia","family":"Hammerschmidt","sequence":"first","affiliation":[{"name":"Institute of Medical Microbiology and Infection Control, Frankfurt University Hospital, Paul-Ehrlich-Stra\u00dfe 40, 60596 Frankfurt, 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