Coulson B S, Fowler K J, White J R, Cotton R G
Arch Virol. 1987;93(3-4):199-211. doi: 10.1007/BF01310974.
Monoclonal antibodies were derived to a human rotavirus purified from stools. Three of the antibodies immunoprecipitated the rotavirus outer capsid glycoprotein gp 34 and were non-neutralizing. These antibodies reacted by enzyme immunoassay with cultivable rotaviruses showing the "long" RNA electropherotype but were inefficient as detectors of "long" RNA pattern rotaviruses in stools. Treatment of SA 11 rotavirus with 7.5 micrograms/ml porcine trypsin for 30 minutes at 37 degrees C irreversibly reduced binding of the antibodies to SA 11 rotavirus in enzyme immunoassays by 50 per cent. Binding was abolished in the presence of rotavirus-negative faecal extracts. These results indicate that non-neutralizing sites on gp 34 of rotaviruses can vary with RNA electropherotype and serotype, and that levels of trypsin currently in use to assist growth of rotaviruses in cell culture may alter the serological profile of the viruses.
针对从粪便中纯化出的人轮状病毒制备了单克隆抗体。其中三种抗体可免疫沉淀轮状病毒外衣壳糖蛋白gp 34，且无中和作用。这些抗体通过酶免疫测定法与显示“长”RNA电泳型的可培养轮状病毒发生反应，但作为粪便中“长”RNA型轮状病毒的检测试剂效率不高。在37℃下用7.5微克/毫升猪胰蛋白酶处理SA 11轮状病毒30分钟，在酶免疫测定中，抗体与SA 11轮状病毒的结合不可逆地减少了50%。在轮状病毒阴性粪便提取物存在的情况下，结合被消除。这些结果表明，轮状病毒gp 34上的非中和位点可能随RNA电泳型和血清型而变化，并且目前用于辅助轮状病毒在细胞培养中生长的胰蛋白酶水平可能会改变病毒的血清学特征。
