Clayson E T, Compans R W
Department of Microbiology, University of Alabama, Birmingham 35294.
J Virol. 1989 Mar;63(3):1095-100. doi: 10.1128/JVI.63.3.1095-1100.1989.
The nature of the simian virus 40 (SV40) receptor on the surfaces of Vero C1008 cells was investigated by a virus binding assay. The optimum pH for SV40 binding to cell surfaces was found to be at 6.5; however, there was little difference in SV40 binding in the range between pH 4.5 and 7.3. The treatment of cell surfaces with several proteases or with an enzyme specific for O-linked carbohydrates significantly reduced virus binding, suggesting that the receptor for SV40 contains protein and O-linked carbohydrates. Treatment of cell monolayers with octyl glucoside removed virus-binding activity from cell surfaces. Recovery of virus-binding activity by octyl glucoside-treated cells took 2.5 h and was inhibited by cycloheximide or tunicamycin. Four polypeptides with molecular weights of 90,000, 58,000, 54,000, and 30,000 were immunoprecipitated from virus-protein complexes derived from octyl glucoside extract solutions and therefore may be components of the SV40 receptor. Competition experiments between SV40 and polyomavirus revealed that these two viruses do not share the same receptor on Vero C1008 cells.
通过病毒结合试验研究了非洲绿猴肾细胞（Vero C1008）表面猿猴病毒40（SV40）受体的性质。发现SV40与细胞表面结合的最适pH值为6.5；然而，在pH 4.5至7.3范围内，SV40的结合几乎没有差异。用几种蛋白酶或对O-连接碳水化合物具有特异性的酶处理细胞表面，可显著降低病毒结合，这表明SV40的受体含有蛋白质和O-连接碳水化合物。用辛基葡糖苷处理细胞单层可去除细胞表面的病毒结合活性。辛基葡糖苷处理的细胞恢复病毒结合活性需要2.5小时，并且受到环己酰亚胺或衣霉素的抑制。从辛基葡糖苷提取物溶液衍生的病毒-蛋白质复合物中免疫沉淀出分子量分别为90,000、58,000、54,000和30,000的四种多肽，因此它们可能是SV40受体的组成成分。SV40和多瘤病毒之间的竞争实验表明，这两种病毒在Vero C1008细胞上不共享相同的受体。
