Coombs K M
Department of Medical Microbiology and Infectious Diseases, University of Manitoba, Winnipeg, Manitoba, Canada.
J Virol. 1996 Jul;70(7):4237-45. doi: 10.1128/JVI.70.7.4237-4245.1996.
A newly identified temperature-sensitive mutant whose defect was mapped to the reovirus M1 gene (minor core protein mu2) was studied to better understand the functions of this virion protein. Sequence determination of the Ml gene of this mutant (tsH11.2) revealed a predicted methionine-to-threonine alteration at amino acid 399 and a change from proline to histidine at amino acid 414. The mutant made normal amounts of single-stranded RNA, both in in vitro transcriptase assays and in infected cells, and normal amounts of progeny viral protein at early times in a restrictive infection. However, tsH11.2 produced neither detectable progeny protein nor double-stranded RNA at late times in a restrictive infection. These studies indicate that mu2 plays a role in the conversion of reovirus mRNA to progeny double-stranded RNA.
为了更好地理解呼肠孤病毒核心蛋白μ2的功能,对一个新鉴定出的温度敏感突变体进行了研究,该突变体的缺陷被定位到呼肠孤病毒M1基因(次要核心蛋白μ2)。对该突变体(tsH11.2)的M1基因进行测序,结果显示在氨基酸399处预测有蛋氨酸到苏氨酸的改变,在氨基酸414处脯氨酸变为组氨酸。在体外转录酶分析和感染细胞中,该突变体产生的单链RNA量正常,并且在限制性感染的早期产生的子代病毒蛋白量也正常。然而,在限制性感染后期,tsH11.2既没有产生可检测到的子代蛋白,也没有产生双链RNA。这些研究表明,μ2在呼肠孤病毒mRNA转化为子代双链RNA的过程中发挥作用。