Celluzzi C N, Farber F E
Department of Microbiology, University of New Hampshire, Durham 03824.
Acta Virol. 1990 Dec;34(6):497-507.
Two herpes simplex virus type 1 (HSV-1) temperature-sensitive (ts) mutants with defects in the gene for the major capsid protein, ICP5, were examined for their effects on virion capsid assembly. Polyacrylamide gel electrophoresis revealed that both mutants were able to synthesize wild-type (WT) levels of ICP5 at the nonpermissive temperature. However, the 53 kD capsid protein disappeared concomitant with the appearance of a new, 51 kD species. These results, taken together with ultrastructural and immunological analyses indicate that the processing and assembly of capsid proteins, DNA packaging and thermal stability of HSV-1 virions are dependent upon functional ICP5.
研究了两个单纯疱疹病毒1型（HSV-1）温度敏感（ts）突变体，它们在主要衣壳蛋白ICP5的基因上存在缺陷，以检测它们对病毒粒子衣壳组装的影响。聚丙烯酰胺凝胶电泳显示，两个突变体在非允许温度下都能够合成野生型（WT）水平的ICP5。然而，53 kD的衣壳蛋白消失，同时出现了一种新的51 kD蛋白。这些结果，结合超微结构和免疫学分析表明，HSV-1病毒粒子的衣壳蛋白加工和组装、DNA包装以及热稳定性都依赖于功能性的ICP5。
