Elicitation and immunological characterization of monoclonal anti-idiotypic antibodies reactive with the ligand binding sites of monoclonal kinin antibodies.

Ten monoclonal anti-idiotypic antibodies (mAB2s) were obtained from fusions of myeloma cells, X63/Ag8.653, and splenocytes from mice immunized with one of two monoclonal kinin antibodies (mAB1s). The interactions of these mAB2s, with four different mAB1s, which have similar kinin binding specificities, was examined. Five of the ten mAB2s cross-reacted with similar affinities, with all four mAB1s. In addition, these five mAB2s were able to inhibit biotinylated-kallidin binding to the mAB1s. This indicated that these mAB2s interact with the mAB1s at, or near, their ligand binding sites. These immunological results are consistent with these five mAB2s being "internal image" beta type anti-idiotypic antibodies.