[The isolation and testing of syngeneic anti-idiotypic antibodies against antimycobacterial monoclonal antibodies].

Fifteen monoclonal antibodies (MAb) were obtained to cell walls (CW) of M. bovinus-8, two of them were limited specific against human and bovine mycobacteria. One MAb reacted in immunoblotting with a protein having molecular mass of 19.1 kDa. It was also found that all MAb bind with the antigen determinants of mycobacterial proteins. The competitive enzyme immunoassay (EIA) helped reveal that the antigenic determinants "recognized" by two MAb are located in the same area despite the fact that one reacted in immunoblotting with a denatured protein and the other "recognized" only a native antigen in EIA. The syngeneic antiidiotypic (anti-ID) immune response was induced by these MAb in BALB/c mice. The EIA showed the binding of anti-ID-antibodies isolated from mice serum both MAb inducing their synthesis and to antimycobacterial serum antibodies of caws with tuberculosis. Data suggesting a similarity existing between the mycobacterial antigen and anti-ID-antibodies were also obtained in the blast transformation reaction: in M. bovinus antigen stimulation of 8 mice lymph node cells sensitized by anti-ID-antibodies and in the reverse situation when the cells sensitive to KC M. bovinus-8 proliferated in response to stimulation by anti-ID-antibodies.