MOLELCULAR BIOLOGY OF PHOTOPIGMENTS

我们已经研究了它的结构、功能、进化和 视网膜S抗原(48K蛋白)及其免疫原性部位的研究 吉恩。人、牛和牛的完整氨基酸序列 用部分蛋白测定小鼠视网膜S抗原 测序和cDNA测序。S抗原的编码序列 来自人、牛和小鼠视网膜的cDNA 大约80%的相似性。相反，非编码序列 这些DNA中最多只有30%的相似性。这个 人、牛和牛S抗原的多肽序列分析 小鼠的视网膜也非常相似(-83%)。的免疫原性部位 对牛S抗原和两株单抗进行了测定 抗体结合部位(表位)和两个葡萄膜致病部位 (命名为M和K)使用20种不同的化学合成 寡肽。EAU诱导所需的最小大小为 也下定决心。M肽为12个氨基酸，K肽为20个氨基酸 酸味很长。这些小肽含有所有必需的 诱导EAU的信息。还观察到了EAU 刘易斯的T细胞淋巴细胞适应性转移后 以前接种过M肽的大鼠，表明 M诱导的实验性自身免疫性葡萄膜炎(EAU) 也有T细胞介导的自身免疫反应。临床和临床 M肽诱导的EAU的组织病理学特征 与用土生土长的S抗原培育的病毒相似。M12号公路 S的多肽-人和小鼠的抗原具有相同的 序列与牛S抗原的序列一致。检索NBRF数据 Bank未发现S抗原之间广泛的序列同源性 和其他蛋白质，尽管一些序列相似性是 在阿尔法转导蛋白上表现明显。有趣的是，其中包括 百日咳毒素作用下的ADP核糖化位点和 磷酸结合位点数。

We have investigated the structure, function, evolution and immunogenic sites of the retinal S-antigen (48 K protein) and its gene. The complete amino acid sequences of human, bovine and murine retinal S-antigen have been determined by partial protein sequencing and cDNA sequencing. Coding sequences of S-antigen cDNAs from human, bovine and murine retinas have approximately 80% similarity. In contrast, noncoding sequences of these cDNAs have at most only 30% similarity. The polypeptide sequences of S-antigen from human, bovine and murine retinas are also very similar (-83%). Immunogenic sites of bovine S-antigen were determined, as were two monoclonal antibody binding sites (epitopes) and two uveitopathogenic sites (named M and K) using 20 different chemically synthesized oligopeptides. The minimum size required for EAU induction was also determined. M peptide was 12 and K peptide was 20 amino acids long. These small peptides contain all the necessary information for the induction of EAU. EAU was also observed following the adaptive transfer of T cell lymphocytes from Lewis rats which were previously immunized with M peptide, indicating that experimental autoimmune uveitis (EAU) induced by M was also a T cell mediated autoimmune response. The clinical and histopathologic features of EAU induced with M peptide were similar to those developed with native S-antigen. The M12 peptide of S-antigen from humans and mice has an identical sequence to that of bovine S-antigen. Searching the NBRF data bank revealed no extensive sequence homology between S-antigen and other proteins, although some sequence similarity was apparent with alpha-transducin. Interestingly, these include the sites subject to ADP-ribosylation by petussis toxin and the phosphoryl binding sites.