Sato T, Kitaoka S, Suzuki H, Konno T, Ishida N
Med Microbiol Immunol. 1987;176(2):65-73. doi: 10.1007/BF00200676.
In view of the fact that trypsin enhances the infectivity of human rotavirus and decreases its hemagglutination, the trypsin-mediated structural modification of the viral polypeptides was analysed, using the KUN strain, a cultivable human rotavirus isolate, grown in the absence of trypsin. A major polypeptide sensitive to trypsin treatment was Vp4 with a molecular weight of 80,000, being cleaved into three polypeptides with molecular weights of 54,000 (P54), 30,000 (P30), and 24,000 (P24). Vp4 was also sensitive to chymotrypsin treatment, generating cleavage products different from those obtained with trypsin.
鉴于胰蛋白酶可增强人轮状病毒的感染性并降低其血凝作用,我们使用在无胰蛋白酶条件下培养的可培养人轮状病毒分离株KUN株,分析了胰蛋白酶介导的病毒多肽结构修饰。对胰蛋白酶处理敏感的一种主要多肽是分子量为80,000的Vp4,它被切割成分子量分别为54,000(P54)、30,000(P30)和24,000(P24)的三种多肽。Vp4对胰凝乳蛋白酶处理也敏感,产生的切割产物与用胰蛋白酶获得的不同。