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Composition and Immunological Properties of the Protein Fraction of A36, a Major Antigen Complex of Mycobacterium paratuberculosis
Author(s) -
KESEL M.,
GILOT P.,
COENE M.,
COCITO C.
Publication year - 1992
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1992.tb03092.x
Subject(s) - paratuberculosis , epitope , antigen , virology , biology , mycobacterium bovis , serology , immunodominance , microbiology and biotechnology , mycobacterium , immune system , antiserum , antibody , tuberculosis , immunology , bacteria , mycobacterium tuberculosis , medicine , genetics , pathology
TMA (thermostable macromolecular antigens) are major mycobactcrial complexes present in all mycobticteria. We have purified A36, the TMA complex of M. paratuberculosis , the etiological agent of paratuberculosis (Johne's disease), and shown by the immune electron microscopy approach its presentation at the cell surface. The immunodominance of the A36 complex in Johne's disease was suggested by comparative ELISA analysis of infected bovine sera, using either A36 or M. paratuberculosis total soluble sonicate as antigens. The cross‐reactivity of TMA complexes from diifcrcnt tnycobacteria was evaluated by immunocn/ymometri c measurements. Percentage of shared epifopes was high tor the couple M. paratuberculosis‐ M. avium . and somewhat lower for the couple M. paratuberculosis and M. bovis Immunological kinship between M. paratuberculosis and M. leprae was suggested by the finding that oul of eleven anti‐ M. lepraemonoclonals , four cross‐reacted with A36 proteins. The specificiiy missing al the level of the whole A36 complex was sought at the level of its protein components. Comparative immunoblot analysis of electrophoresed A36 proteins indicated three of them to contain epitopes not shared by M. bovis proteins, and one of them to contain epitopes specific wilh respect lo M. avium, M. bovis and M. phlei. The latter component, a 34‐kDa protein, could be an ideal reagent for a serological tesi for, Johne's disease, being immunodominant in infected cattle and endowed with species‐specific epitopes.