Shinohara T, Donoso L, Wistow G, Dietzschold B, Craft C, Tao R
Laboratory of Molecular and Developmental Biology, National Eye Institute, Bethesda, MD.
Jpn J Ophthalmol. 1987;31(2):197-206.
cDNA clones for bovine retinal S-antigen (48K protein) have been isolated and sequenced. Secondary structure prediction for the deduced amino acid sequence suggest that the protein has predominantly beta-conformation with a helical region at the C-terminus. Local regions of sequence similarity with alpha-transducin have been observed, including the sites subject to ADP-ribosylation by pertussis and cholera toxins. Thirty-nine tryptic peptides and ten CNBr peptides of native S-antigen were purified and partially sequenced, showing good agreement with the sequence deduced from the cDNA analysis. The locations of two monoclonal epitopes have been determined by different methods. Furthermore, one synthetic peptide corresponding to the determined amino acid sequence was found to be highly pathogenic for the induction of experimental autoimmune uveitis (EAU). Native S-antigen has further been shown to be glycosylated, which has implications for its antigenicity.
已分离并测序了牛视网膜S抗原（48K蛋白）的cDNA克隆。对推导的氨基酸序列进行二级结构预测表明，该蛋白主要具有β构象，C端有一个螺旋区域。已观察到与α-转导蛋白的局部序列相似性区域，包括百日咳毒素和霍乱毒素进行ADP-核糖基化修饰的位点。纯化了天然S抗原的39个胰蛋白酶肽段和10个溴化氰肽段并进行了部分测序，结果与cDNA分析推导的序列高度一致。已通过不同方法确定了两个单克隆表位的位置。此外，发现一个与确定的氨基酸序列相对应的合成肽对诱导实验性自身免疫性葡萄膜炎（EAU）具有高度致病性。进一步证明天然S抗原是糖基化的，这对其抗原性有影响。
