Contribution of the Infection-Associated Complement Regulator-Acquiring Surface Protein 4 (ErpC) to Complement Resistance of<i>Borrelia burgdorferi</i>
-
- Claudia Hammerschmidt
- Institute of Medical Microbiology and Infection Control, Frankfurt University Hospital, Paul-Ehrlich-Straße 40, 60596 Frankfurt, Germany
-
- Teresia Hallström
- Department of Infection Biology, Leibniz Institute for Natural Products Research and Infection Biology, Beutenbergstraße 11a, 07745 Jena, Germany
-
- Christine Skerka
- Department of Infection Biology, Leibniz Institute for Natural Products Research and Infection Biology, Beutenbergstraße 11a, 07745 Jena, Germany
-
- Reinhard Wallich
- Institute of Immunology, University of Heidelberg, Im Neuenheimer Feld 305, 69120 Heidelberg, Germany
-
- Brian Stevenson
- Department of Microbiology, Immunology and Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY 40536, USA
-
- Peter F. Zipfel
- Department of Infection Biology, Leibniz Institute for Natural Products Research and Infection Biology, Beutenbergstraße 11a, 07745 Jena, Germany
-
- Peter Kraiczy
- Institute of Medical Microbiology and Infection Control, Frankfurt University Hospital, Paul-Ehrlich-Straße 40, 60596 Frankfurt, Germany
説明
<jats:p><jats:italic>Borrelia burgdorferi</jats:italic>evades complement-mediated killing by interacting with complement regulators through distinct complement regulator-acquiring surface proteins (CRASPs). 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>
収録刊行物
-
- Clinical and Developmental Immunology
-
Clinical and Developmental Immunology 2012 1-12, 2012
Wiley
