Open AccessCharacterization of a unique borreliacidal epitope on the outer surface protein C of Borrelia burgdorferi
Author(s) -
Yang Xiaohua,
Li Yang,
Dunn John J.,
Luft Benjamin J.
Publication year - 2006
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2006.00122.x
Subject(s) - borrelia burgdorferi , epitope , biology , monoclonal antibody , spirochaetaceae , peptide sequence , antigen , amino acid , borrelia , epitope mapping , microbiology and biotechnology , western blot , peptide , antibody , virology , biochemistry , immunology , gene
The outer surface protein C (OspC) of the Lyme disease agent, Borrelia burgdorferi , is an immunoprotective antigen in laboratory models of infection. However, to understand its protective effects, it is important to identify the key epitopes of this protein. We produced a borreliacidal anti‐OspC monoclonal antibody specific to the B31 strain and identified its binding site. The specificity of MAb 16.22 was determined by Western blot reactivity using OspC derived from different Borrelia isolates which had varying amino acid sequences. Comparison of the OspC sequences and binding data suggested that MAb 16.22 binds to amino acids 133–147 of the OspC protein. To test this hypothesis, we synthesized a 15‐amino acid peptide containing the target sequence and, using competition enzyme‐linked immunosorbent assay (ELISA), we found that this peptide included the epitope of MAb 16.22. In addition, we determined that MAb 16.22 is able to kill of B . burgdorferi in a complement‐independent fashion.