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This article examines the mimicry of biological receptors by immuno globulin idiotypes. This mimicry is usually defined empirically by the interaction of antiidiotypic antibodies with epitopes of these receptors. We begin with a definition of the theoretical base and operational terms used in this analysis. For clarity, precise distinctions in terms of specificity and function are made between the different subclasses of antiidiotypic antibodies. Next, we present an overview of the most defined examples of idiotypic mimicry. These systems are to be distinguished from those that regulate lymphocyte function by interaction of antiidiotypic antibodies with lymphocyte antigen receptors. For discussions of these effects we refer the reader to several excellent recent reviews that summarize the roles of antiidiotypic antibodies in the regulation of lymphocyte function, acti vation, and ontogeny (1-3). The majority of examples of receptor mimicry are relatively new, and their focus is thus far biased toward the phenomenological and practical use of antiidiotypes as research tools (4, 5). Certainly, the application of antiidiotypic antibodies as specific receptor probes has unique advantages over more conventional ligand-based methodologies. Perhaps most useful is the discovery that antiidiotypes that bind receptors may be generated in the absence of either purified
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1986
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