Premium
Carboxyl terminus of the 34 kDa protein of Mycobacterium paratuberculosis shares homologous B‐cell epitopes with Mycobacterium avium and Mycobacterium intracellulare
Author(s) -
Malamo M.,
Okazaki K.,
Sakoda Y.,
Kida H.
Publication year - 2007
Publication title -
veterinary record
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.261
H-Index - 99
eISSN - 2042-7670
pISSN - 0042-4900
DOI - 10.1136/vr.161.25.853
Subject(s) - epitope , paratuberculosis , polyclonal antibodies , monoclonal antibody , mycobacterium , recombinant dna , microbiology and biotechnology , biology , antibody , mycobacterium smegmatis , virology , mycobacterium bovis , antigen , mycobacterium tuberculosis , bacteria , biochemistry , immunology , gene , tuberculosis , medicine , genetics , pathology
Monoclonal antibodies (mAbs) against a recombinant carboxyl terminus of the 34 kDa protein of Mycobacterium paratuberculosis were produced in mice. Two of the mAbs cross‐reacted with Mycobacterium avium and Mycobacterium intracellulare in both an elisa and immunoblot. The recombinant protein also reacted with polyclonal sera produced in rabbits against all three mycobacteria, indicating the presence of cross‐reactive epitopes in the protein. To determine the reactivity of cattle sera against epitopes recognised by the mAbs, competition assays between bovine sera and the mAbs were carried out. Two mAbs were significantly inhibited by sera from cattle that were naturally infected with M paratuberculosis . The results indicate that epitopes on the carboxyl terminus of the 34 kDa protein common to M paratuberculosis , M avium and M intracellulare readily induce antibody production in naturally infected cattle. These epitopes reduce the diagnostic specificity of the carboxyl terminus of the 34 kDa protein, which was originally thought to contain only M paratuberculosis ‐specific epitopes.