Anti‐idiotypic antibodies: biological function and structural studies

Abstract

Under a variety of circumstances antibodies can be elicited against the variable region of other antibody molecules (anti-idotypic antibodies, anti-ids). Some of the antibodies are directed against the binding sites of the eliciting antibodies. Of particular interest are the antibodies that recognize epitopes of the original antibody that are in contact with antigen. Antibodies of this kind have been produced and used in a variety of situations including attempts at using them as therapeutic agents. In recent years structural data at the atomic level have emerged for anti-idiotypic antibodies from X-ray diffraction studies. These studies provided structural basis for molecular mimicry of anti-ids. For a large globular antigen (lysozyme), where epitope is noncontinuguous, molecular mimicry is not present at the atomic level. In this case, idiotopes are largely composed of CDR residues, but framework residues are also used. For an epitope that is sequence-specific (anti-FIPV system), molecular mimicry appears to be present as evidenced by the sequence homology between the CDR loops of the anti-id and the epitope of the original antigen. In the case of a small hormone antigen (angiotensin II), an internal image of the eliciting antigen appears to be represented in a single CDR loop of the antiiodiotypic antibody.