IRBP from bovine retina is poorly uveitogenic in guinea pigs and is identical to A-antigen.
Retinal interphotoreceptor retinoid-binding protein (IRBP) is a potent uveitogen in Lewis rats, producing experimental autoimmune uveitis (EAU) reproducibly at doses lower than those of S-antigen (S-Ag). In contrast, IRBP was found to be poorly uveitogenic in three strains of guinea pigs, inducing only minor changes in a small proportion of these animals. On the other hand, S-Ag was found to induce EAU in the majority of immunized guinea pigs, with changes more severe than those induced by IRBP. Unlike the difference in their uveitogenicity, IRBP and S-Ag induced similar levels of specific immune responses in the immunized guinea pigs. The poor uveitogenicity of IRBP in guinea pigs resembles that of A-antigen (A-Ag). The two proteins are also similar in other features and were found in this study to be antigenically identical. It is proposed that IRBP and A-Ag are one and the same protein.
D000818:Animals; D000917:Antibody Formation / Q000187:drug effects; D000941:Antigens / Q000276:immunology; D019393:Arrestin; D001327:Autoimmune Diseases / Q000139:chemically induced* / Q000276:immunology; D002417:Cattle; D005136:Eye Proteins / Q000276:immunology; D005260:Female; D006168:Guinea Pigs; D007114:Immunization; D008297:Male; D010786:Photoreceptor Cells / Q000187:drug effects; D012177:Retinol-Binding Proteins / Q000494:pharmacology*; D014605:Uveitis / Q000139:chemically induced* / Q000276:immunology; D000099214:Retinol-Binding Proteins, Interstitial
D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D012177:Retinol-Binding Proteins; D000099214:Retinol-Binding Proteins, Interstitial