Open AccessThe OspE-Related Proteins Inhibit Complement Deposition and Enhance Serum Resistance of Borrelia burgdorferi , the Lyme Disease Spirochete
Author(s) -
Melisha R. Kenedy,
Darrin R. Akins
Publication year - 2011
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.01274-10
Subject(s) - borrelia burgdorferi , biology , complement system , microbiology and biotechnology , mutant , strain (injury) , lyme disease , alternative complement pathway , virology , immunology , antibody , gene , genetics , anatomy
Borrelia burgdorferi , the Lyme disease spirochete, binds the host complement inhibitors factor H (FH) and FH-like protein 1 (FHL-1). Binding of FH/FHL-1 by theB. burgdorferi proteins CspA and the OspE-related proteins is thought to enhance resistance to serum-mediated killing. While previous reports have shown that CspA confers serum resistance inB. burgdorferi , it is unclear whether the OspE-related proteins are relevant inB. burgdorferi serum resistance when OspE is expressed on the borrelial surface. To assess the role of the OspE-related proteins, we overexpressed them in a serum-sensitive CspA mutant strain. OspE overexpression enhanced serum resistance of the CspA-deficient organisms. Furthermore, FH was more efficiently bound to theB. burgdorferi surface when OspE was overexpressed. Deposition of complement components C3 and C5b-9 (the membrane attack complex), however, was reduced on the surface of the OspE-overexpressing strain compared to that on the CspA mutant strain. These data demonstrate that OspE proteins expressed on the surface ofB. burgdorferi bind FH and protect the organism from complement deposition and subsequent serum-mediated destruction.