Kraus W, Ohyama K, Snyder D S, Beachey E H
Veterans Administration Medical Center, Memphis, Tennessee.
J Exp Med. 1989 Feb 1;169(2):481-92. doi: 10.1084/jem.169.2.481.
The crossreactivity of antibodies against a renal autoimmune epitope of Streptococcus pyogenes M protein with glomerular mesangial cells was investigated. The antibodies directed against the amino acid sequence Ile-Arg-Leu-Arg of the nephritogenic type 1 M protein reacted in a fibrillar pattern with mesangial cells cultured from isolated glomeruli. In Western blots of urea-extracted mesangial proteins, the antibodies reacted with a 56-kD protein. Monoclonal and polyclonal antibodies identified the 56-kD mesangial protein as vimentin. Two synthetic peptides of human vimentin containing the sequence Arg-Leu-Arg reacted with the autoimmune antibodies raised against a streptococcal M protein peptide. These results provide evidence that the intermediate filament protein vimentin shares autoimmune epitopes with streptococcal M protein.
研究了抗化脓性链球菌M蛋白肾脏自身免疫表位的抗体与肾小球系膜细胞的交叉反应性。针对致肾炎1型M蛋白氨基酸序列Ile-Arg-Leu-Arg的抗体,与从分离的肾小球培养的系膜细胞呈纤维状反应。在尿素提取的系膜蛋白的蛋白质印迹法中,该抗体与一种56-kD蛋白发生反应。单克隆抗体和多克隆抗体将56-kD系膜蛋白鉴定为波形蛋白。两条含序列Arg-Leu-Arg的人波形蛋白合成肽,与针对链球菌M蛋白肽产生的自身免疫抗体发生反应。这些结果证明中间丝蛋白波形蛋白与链球菌M蛋白共享自身免疫表位。