Kedl R, Schmechel S, Schiff L
Department of Microbiology, University of Minnesota, Minneapolis 55455.
J Virol. 1995 Jan;69(1):552-9. doi: 10.1128/JVI.69.1.552-559.1995.
The reovirus sigma 3 protein is a major outer capsid protein that may function to regulate translation within infected cells. To facilitate the understanding of sigma 3 structure and functions and the evolution of mammalian reoviruses, we sequenced cDNA copies of the S4 genes from 10 serotype 3 and 3 serotype 1 reovirus field isolates and compared these sequences with sequences of prototypic strains of the three reovirus serotypes. We found that the sigma 3 proteins are highly conserved: the two longest conserved regions contain motifs proposed to function in binding zinc and double-stranded RNA. We used the 16 viral isolates to investigate the hypothesis that structural interactions between sigma 3 and the cell attachment protein, sigma 1, constrain their evolution and to identify a determinant within sigma 3 that is in close proximity to the sigma 1 hemagglutination site.
呼肠孤病毒σ3蛋白是一种主要的外衣壳蛋白,可能在受感染细胞内发挥调节翻译的作用。为了便于理解σ3的结构和功能以及哺乳动物呼肠孤病毒的进化,我们对10株3型和3株1型呼肠孤病毒野外分离株的S4基因的cDNA拷贝进行了测序,并将这些序列与三种呼肠孤病毒血清型原型株的序列进行了比较。我们发现σ3蛋白高度保守:两个最长的保守区域包含被认为在结合锌和双链RNA中起作用的基序。我们使用这16株病毒分离株来研究σ3与细胞附着蛋白σ1之间的结构相互作用限制它们进化的假说,并确定σ3中与σ1血凝素位点紧密相邻的一个决定因素。