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The analysis of host immunity to mycobacteria and the development of discriminatory diagnostic reagents relies on the characterization of conserved and species-specific mycobacterial antigens. In this report, we have characterized theMycobacterium avium homolog of the highly immunogenicM. leprae 35-kDa protein. The genes encoding these two proteins were well conserved, having 82% DNA identity and 90% identity at the amino acid level. Moreover both proteins, purified from the fast-growing hostM. smegmatis , formed multimeric complexes of around 1000 kDa in size and were antigenically related as assessed through their recognition by antibodies and T cells fromM. leprae -infected individuals. The 35-kDa protein exhibited significant sequence identity with proteins fromStreptomyces griseus and the cyanobacteriumSynechoccocus sp. strain PCC 7942 that are up-regulated under conditions of nutrient deprivation. The 67% amino acid identity between theM. avium 35-kDa protein and SrpI ofSynechoccocus was spread across the sequences of both proteins, while the homologous regions of the 35-kDa protein and the P3 sporulation protein ofS. griseus were interrupted in the P3 protein by a divergent central region. Assessment by PCR demonstrated that the gene encoding theM. avium 35-kDa protein was present in all 30M. avium clinical isolates tested but absent fromM. intracellulare ,M. tuberculosis , orM. bovis BCG. Mice infected withM. avium , but notM. bovis BCG, developed specific immunoglobulin G antibodies to the 35-kDa protein, consistent with the observation that tuberculosis patients do not recognize the antigen. Strong delayed-type hypersensitivity was elicited by the protein in guinea pigs sensitized withM. avium.

Molecular and Immunological Analyses of the Mycobacterium avium Homolog of the Immunodominant Mycobacterium leprae 35-Kilodalton Protein