The FASEB Journal, Vol 7, 437-444, Copyright © 1993 by The Federation of American Societies for Experimental Biology

REVIEWS

Idiotypes: structure and immunogenicity

NS Greenspan and CA Bona
Institute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106.

Idiotopes are markers on the variable domains of antigen-specific immunological receptors recognized by anti-idiotypic antibodies or T cells. Therefore, a given antibody or T cell receptor can be identified on the basis of a characteristic idiotypic pattern. The structural correlates for idiotopes on antibodies have been studied by competitive binding assays, electron microscopy, site-directed mutagenesis, and X- ray crystallography. Immunoglobulin idiotopes, recognized by antiidiotypic antibodies, can involve amino acid residues from several hypervariable or framework regions and from either or both of the heavy and light chain variable domains. Recent studies suggest that it may be possible to exploit structural knowledge of idiotopes and anti- idiotopes for the design of new ligands for immunological or other cell surface receptors. In one instance, it has been possible to use the inferred structural features of an anti-idiotope, which mimics a viral protein, to design a small organic molecule with functional properties approximating those of the antigen and the native anti-idiotope. An alternative strategy being explored for creating new vaccines or therapeutic agents involves engineering an amino acid sequence, corresponding to a segment of a selected nominal antigen, into an immunoglobulin variable domain.

This article has been cited by other articles:

				D. M. Belnap, N. R. Watts, J. F. Conway, N. Cheng, S. J. Stahl, P. T. Wingfield, and A. C. Steven Diversity of core antigen epitopes of hepatitis B virus PNAS, September 16, 2003; 100(19): 10884 - 10889. [Abstract] [Full Text] [PDF]