人巨细胞病毒衣壳中最小衣壳蛋白的三维定位
Three-dimensional localization of the smallest capsid protein in the human cytomegalovirus capsid.
作者信息
Yu Xuekui, Shah Sanket, Atanasov Ivo, Lo Pierrette, Liu Fenyong, Britt William J, Zhou Z Hong
机构信息
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin St., MSB 2.280, Houston, TX 77030, USA.
出版信息
J Virol. 2005 Jan;79(2):1327-32. doi: 10.1128/JVI.79.2.1327-1332.2005.
Abstract
The smallest capsid proteins (SCPs) of the human herpesviruses differ substantially in size and sequence and are thought to impart some unique aspects of infection to their respective viruses. We used electron cryomicroscopy and antibody labeling to show that the 8-kDa SCP of human cytomegalovirus is attached only to major capsid protein subunits of the hexons, not the pentons. Thus, the SCPs of different herpesviruses illustrate that a protein can evolve significantly in sequence, structure, and function, while preserving its role in the architecture of the virus by binding to a specific partner in a specific oligomeric state.
摘要
人类疱疹病毒的最小衣壳蛋白（SCPs）在大小和序列上有很大差异，并且被认为赋予了各自病毒感染的一些独特方面。我们使用电子冷冻显微镜和抗体标记来表明，人巨细胞病毒的8 kDa SCP仅附着于六邻体的主要衣壳蛋白亚基，而非五邻体。因此，不同疱疹病毒的SCP表明，一种蛋白质可以在序列、结构和功能上发生显著进化，同时通过以特定寡聚状态与特定伴侣结合来保留其在病毒结构中的作用。
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