
A murine IgG1 monoclonal antibody thatbinds specifically to outer surface protein A of Lyme disease spirochete Borrelia burgdorferi
Author(s) -
Abolhassani Mohsen,
Pavia Charles S.,
Dunn John J.,
Chiao J.W.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06185.x
Subject(s) - borrelia burgdorferi , microbiology and biotechnology , epitope , lyme disease , biology , monoclonal antibody , spirochaetaceae , treponema , virology , borrelia , antigen , antibody , immunology , syphilis , human immunodeficiency virus (hiv)
A murine monoclonal antibody, designated MA‐2G9, directed against outer surface protein A (OspA) of the Lyme disease spirochete, Borrelia burgdorferi , has been produced. Antibody MA‐2G9, IgG1 subclass, was purified by affinity chromatography on protein G Sepharose column and used for purification of OspA antigen from Borrelia burgdorferi cell lysate. Epitope specificity was studied by Western immunoblotting, using several strains of B. burgdorferi and non‐Lyme disease bacteria such as Treponema pallidum and B. hermsii . The MA‐2G9 monoclonal antibody reacted specifically with recombinant OspA aas well as with native OspA in sonicated B. burgdorferi strains. No reaction was observed with T. pallidum, Escherichia coli, Staphylococcus aureus and B. hermsii lysates. The MA‐2G9 antibody also recognized the denatured form of OspA indicating that it is directed against sequential epitope and not conformational epitope.