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Characterization of an anti‐ Borrelia burgdorferi OspA conformational epitope by limited proteolysis of monoclonal antibody‐bound antigen and mass spectrometricpeptide mapping
Author(s) -
Legros Vèronique,
JolivetReynaud Colette,
BattailPoirot Nicole,
SaintPierre Christine,
Forest Eric
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.5.1002
Subject(s) - borrelia burgdorferi , epitope , conformational epitope , monoclonal antibody , borrelia , epitope mapping , antigen , biology , lyme disease , antibody , linear epitope , virology , immune system , microbiology and biotechnology , immunology
Lyme borreliosis is a multisystem disorder caused by the spirochete Borrelia burgdorferi that is transmitted to humans by the tick Ixodes dammini. The immune response against the 31 kDa OspA, which is one of the most abundant B. burgdorferi proteins, appears to be critical in preventing infection and tissue inflammation. Detailed knowledge of the immunological and molecular characteristics of the OspA protein is important for the development of reliable diagnostic assays. In this study, we characterized a new conformational epitope present within the middle part of B. burgdorferi OspA. Our approach used enzymatic proteolyses of the immune complex followed by mass spectrometric identification of the peptides bound to the antibody. It appears to be one of the first reports on the characterization of a discontinuous epitope using mass spectrometry.