Steven A C, Roberts C R, Hay J, Bisher M E, Pun T, Trus B L
J Virol. 1986 Feb;57(2):578-84. doi: 10.1128/JVI.57.2.578-584.1986.
The structures of the hexavalent capsomers of herpes simplex virus type 2 were analyzed by negative staining electron microscopy of capsomer patches derived from partially disrupted nucleocapsids. Optimally computer-averaged images were formed for each of the three classes of capsomer distinguished by their respective positions on the surface of the icosahedral capsid with a triangulation number of 16; in projection, each capsomer exhibited unequivocal sixfold symmetry. According to correspondence analysis of our set of capsomer images, no significant structural differences were detected among the three classes of capsomers, as visualized under these conditions. Taking into account information from images of freeze-dried, platinum-shadowed nucleocapsid fragments, it was established that each hexavalent capsomer is a hexamer of the 155-kilodalton major capsid protein. The capsomer has the form of a sixfold hollow cone approximately 12 nm in diameter and approximately 15 nm in depth, whose axial channel tapers in width from the outside towards the inner capsid surface.
通过对部分破坏的核衣壳衍生的衣壳粒贴片进行负染色电子显微镜分析，研究了2型单纯疱疹病毒六价衣壳粒的结构。对于二十面体衣壳表面上具有三角剖分数16的三类衣壳粒中的每一类，都形成了最佳的计算机平均图像；在投影中，每个衣壳粒都呈现出明确的六重对称性。根据我们这组衣壳粒图像的对应分析，在这些条件下观察到的三类衣壳粒之间未检测到明显的结构差异。考虑到来自冻干、铂阴影核衣壳片段图像的信息，确定每个六价衣壳粒是155千道尔顿主要衣壳蛋白的六聚体。衣壳粒呈六重空心圆锥体形式，直径约12纳米，深度约15纳米，其轴向通道宽度从外部向内衣壳表面逐渐变窄。
