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Molecular analysis of anti‐idiotypic monoclonal antibodies in the HLA‐DR antigenic system

The structural organization of anti‐idiotypic (id) antibodies has been investigated mostly in haptenic systems. No information is available about the structural characteristics of anti‐id antibodies in major histocompatibility complex (MHC) antigenic systems, although these data may contribute to our understanding of the molecular basis of their functional role in the immune response. Therefore, we have determined the nucleotide and derived amino acid sequence of the VH and VL regions of the anti‐id monoclonal antibodies (mAb) F5‐444, F5‐830, F5‐963, F5‐1126, F5‐1336 and F5‐1419, which had been elicited with the syngeneic anti‐HLA‐DR1, 4, w14, w8, 9 mAb AC1.59. The six anti‐id mAb are heterogenous in their VH and VL region gene usage. This structural heterogeneity is not correlated with their target specificity and with their ability to elicit anti‐HLA‐DR antibodies. The latter characteristic is markedly influenced by a limited number of amino acid substitutions, since mAb F5‐444, which induces anti‐HLA‐DR antibodies, differs only in two residues in complementarity‐determining regions and in five residues in framework regions from mAb F5‐1126, which does not induce anti‐HLA‐DR antibodies.