RECONSTRUCTION OF THE 3-DIMENSIONAL STRUCTURE OF SIMIAN VIRUS-40 AND VISUALIZATION OF THE CHROMATIN CORE
RECONSTRUCTION OF THE 3-DIMENSIONAL STRUCTURE OF SIMIAN VIRUS-40 AND VISUALIZATION OF THE CHROMATIN CORE
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DOI：
10.1073/pnas.85.2.422
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发表时间：
1988-01-01
影响因子：
11.1
通讯作者：
BINA, M
中科院分区：
文献类型：
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作者：
BAKER, TS;DRAK, J;BINA, M
通过对猴病毒40（SV 40）冷冻水化样品的电子显微照片进行图像分析，重建了病毒衣壳和核组蛋白核心的三维结构。72个突出的衣壳单位，包括T = 7D二十面体表面晶格的衣壳被清楚地解决。五价和六价壳粒都出现五聚体亚结构，表明壳中的键合特异性不是准等价的。SV40病毒粒子衣壳的结构与多瘤空衣壳的结构有显著的相似性。这一结果表明：（i）六价衣壳的五聚体亚结构也存在于病毒体中，（ii）衣壳晶格中72个五聚体的排列可能是整个帕波瓦病毒家族的特征。SV 40重建的中心显示了与核组蛋白核心相对应的电子密度。这个密度是模糊的，表明微型染色体不是以与衣壳对称性匹配的二十面体对称性组织的。可视化的病毒粒子染色质提供了一个基础，调用新的模型，为更高层次的结构的crossidated微型染色体。
The three-dimensional structure of the capsid and the nucleohistone core of simian virus 40 (SV40) has been reconstructed by image analysis of electron micrographs of frozen hydrated samples. The 72 prominent capsomere units that comprise the T = 7d icosahedral surface lattice of the capsid are clearly resolved. Both the pentavalent and hexavalent capsomeres appear with pentameric substructure, indicating that bonding specificity in the shell is not quasi-equivalent. There is a remarkable similarily between the structure of the SV40 virion capsid and the structure reported for the polyoma empty capsid. This result established that (i) the unexpected pentameric substructure of the hexavalent capsomeres is also present in virions and (ii) the arrangement of the 72 pentamers in the capsid lattice may be a characteristic feature of the entire papova family of viruses. The center of the SV40 reconstruction reveals electron density corresponding to the nucleohistone core. This density is smeared, suggesting that the minichromosome is not organized with icosahedral symmetry matching the capsid symmetry. The visualization of the virion chromatin provides a basis for invoking new models for the higher order structure of the encapsidated minichromosome.