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A 9 angstroms single particle reconstruction from CCD captured images on a 200 kV electron cryomicroscope.通过在200 kV冷冻电子显微镜上使用电荷耦合器件（CCD）捕获的图像进行的9埃单颗粒重建。
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Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution.通过电子冷冻显微镜在亚纳米分辨率下确定二十面体病毒结构。
Adv Protein Chem. 2003;64:93-124. doi: 10.1016/s0065-3233(03)01003-9.
3
Three-dimensional localization of pORF65 in Kaposi's sarcoma-associated herpesvirus capsid.卡波西肉瘤相关疱疹病毒衣壳中pORF65的三维定位
J Virol. 2003 Apr;77(7):4291-7. doi: 10.1128/jvi.77.7.4291-4297.2003.
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Structure of the herpesvirus major capsid protein.疱疹病毒主要衣壳蛋白的结构
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5
The interaction between the major capsid protein and the smallest capsid protein of human cytomegalovirus is dependent on two linear sequences in the smallest capsid protein.人巨细胞病毒主要衣壳蛋白与最小衣壳蛋白之间的相互作用取决于最小衣壳蛋白中的两个线性序列。
J Virol. 2003 Feb;77(4):2730-5. doi: 10.1128/jvi.77.4.2730-2735.2003.
6
Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids.单纯疱疹病毒1型VP26与衣壳相互作用所需的残基。
J Virol. 2003 Jan;77(1):391-404. doi: 10.1128/jvi.77.1.391-404.2003.
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IMIRS: a high-resolution 3D reconstruction package integrated with a relational image database.IMIRS：一个与关系型图像数据库集成的高分辨率三维重建软件包。
J Struct Biol. 2002 Mar;137(3):292-304. doi: 10.1016/s1047-8477(02)00014-x.
8
The pattern of tegument-capsid interaction in the herpes simplex virus type 1 virion is not influenced by the small hexon-associated protein VP26.1型单纯疱疹病毒病毒粒子中包膜-衣壳的相互作用模式不受小六邻体相关蛋白VP26的影响。
J Virol. 2001 Dec;75(23):11863-7. doi: 10.1128/JVI.75.23.11863-11867.2001.
9
Genetic evidence of an essential role for cytomegalovirus small capsid protein in viral growth.巨细胞病毒小衣壳蛋白在病毒生长中起关键作用的遗传学证据。
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10
Three-dimensional structure of the human herpesvirus 8 capsid.人类疱疹病毒8型衣壳的三维结构。
J Virol. 2000 Oct;74(20):9646-54. doi: 10.1128/jvi.74.20.9646-9654.2000.

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.

DOI:10.1128/JVI.79.2.1327-1332.2005
PMID:15613360
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC538561/
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。