Varela R, Martínez-Costas J, Mallo M, Benavente J
Departamento de Bioquímica y Biologia Molecular, Facultad de Farmacia, Santiago de Compostela, Spain.
J Virol. 1996 May;70(5):2974-81. doi: 10.1128/JVI.70.5.2974-2981.1996.
Avian reovirus S1133 specifies at least 10 primary translation products, eight of which are present in the viral particle and two of which are nonstructural proteins. In the work presented here, we studied the covalent modifications undergone by these translation products in the infected cell. The structural polypeptide mu2 was shown to be intracellularly modified by both myristoylation and proteolysis. The site-specific cleavage of mu2 yielded a large carboxy-terminal fragment and a myristoylated approximately 5,500-Mr peptide corresponding to the amino terminus. Both mu2 and its cleavage products were found to be structural components of the reovirion. Most avian reovirus proteins were found to be glycosylated and to have a blocking group at the amino terminus. In contrast to the mammalian reovirus system, none of the avian reovirus polypeptides was found to incorporate phosphorus during infection. Our results add to current understanding of the similarities and differences between avian and mammalian reoviruses.
禽呼肠孤病毒S1133至少可产生10种初级翻译产物，其中8种存在于病毒粒子中，另外2种是非结构蛋白。在本文所述的研究中，我们研究了这些翻译产物在受感染细胞中发生的共价修饰。结构多肽μ2被证明在细胞内会发生肉豆蔻酰化和蛋白水解修饰。μ2的位点特异性切割产生了一个大的羧基末端片段和一个对应于氨基末端的肉豆蔻酰化的约5500道尔顿的肽段。μ2及其切割产物均被发现是呼肠孤病毒粒子的结构成分。大多数禽呼肠孤病毒蛋白都被发现发生了糖基化，并且在氨基末端有一个封闭基团。与哺乳动物呼肠孤病毒系统不同，在感染过程中未发现禽呼肠孤病毒多肽结合磷。我们的结果增进了目前对禽呼肠孤病毒和哺乳动物呼肠孤病毒异同的理解。
