Antigen mimicry by anti-idiotypic antibodies: study of interactions between complementary surfaces in macromolecules.
Anti-idiotypic antibodies were obtained from New Zealand White rabbits injected with affinity-purified rabbit anti-TrpR antibodies. In gel mobility shift studies, such immunoglobulin preparations were shown to contain one or more species able to form specific complexes with DNA molecules bearing a trp operator. In competitive ELISA assays, the binding of anti-idiotypic antibodies to operator-bearing DNA was reversed by TrpR. The demonstration that the immune repertoire contains information for operator-specific DNA-binding proteins may be relevant to the etiology of certain autoimmune diseases.
Yang
W
W
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-1153, USA.
Somerville
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RL
D000818:Animals; D000888:Antibodies, Anti-Idiotypic / Q000737:chemistry*; D000937:Antigen-Antibody Reactions; D000941:Antigens / Q000737:chemistry* / Q000276:immunology*; D001426:Bacterial Proteins / Q000276:immunology; D004247:DNA / Q000737:chemistry / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods; D011817:Rabbits; D012097:Repressor Proteins / Q000276:immunology*; D014364:Tryptophan; D029968:Escherichia coli Proteins
D000888:Antibodies, Anti-Idiotypic; D000941:Antigens; D001426:Bacterial Proteins; D004247:DNA; D012097:Repressor Proteins; D014364:Tryptophan; C027190:TRPR protein, E coli; D029968:Escherichia coli Proteins