Morphological variants of Sindbis virus produced by a mutation in the capsid protein
Morphological variants of Sindbis virus produced by a mutation in the capsid protein
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DOI：
10.1016/s0042-6822(02)00034-x
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发表时间：
2003-03-01
期刊：
影响因子：
3.7
通讯作者：
Brown, DT
中科院分区：
文献类型：
--
作者：
Ferreira, D;Hernandez, R;Brown, DT
辛德比斯病毒是一种由RNA、蛋白质和脂质组成的复杂的集合体。病毒被组织成两个嵌套的T=4二十面体蛋白质壳，它们之间夹着一个脂质双层。病毒RNA驻留在内部蛋白质壳内。内层蛋白质壳通过与外层蛋白质的接触附着到外层蛋白质壳上，外层蛋白质穿透脂质双层。以下手稿中提供的数据表明，衣壳蛋白的突变可以导致病毒结构蛋白组装成不同三角数的二十面体。对于这些形态变体，计算的三角化数遵循序列T=4、9、16、25和36。它们都属于Caspar和Klug(1962)预测的二十碳六面体的P=1类。这些数据支持他们的假设，即通过改变五重轴插入点之间的距离，将形成二十面体家族。这种衣壳蛋白缺陷还导致大量衣壳蛋白被合并到蛋白质和RNA的大的细胞质聚集体中。这些观察结果支持这样的模型，即预先形成的核衣壳的几何形状将病毒膜蛋白的组装组织成相同配置的结构，并反对认为膜糖蛋白的组装指导核衣壳组装的模型。(C)2003年埃尔塞维尔科学公司(美国)。版权所有。
Sindbis virus is a complex aggregate of RNA, protein and lipid. The virus is organized as two nested T = 4 icosahedral protein shells between which is sandwiched a lipid bilayer. The virus RNA resides within the inner protein shell. The inner protein shell is attached to the outer protein shell through contacts to proteins in the outer shell, which penetrate the lipid bilayer. The data presented in the following manuscript show that mutations in the capsid protein can result in the assembly of the virus structural proteins into icosahedra of different triangulation numbers. The triangulation numbers calculated, for these morphological variants, follow the sequence T = 4, 9, 16, 25 and 36. All fall into the class P = 1 of icosadeltahedra as was predicted by Caspar and Klug (1962). The data support their hypothesis that families of icosahedra would be developed by altering the distance between the points of insertion of the five-fold axis. This capsid protein defect also results in the incorporation of much of the capsid protein, into large cytoplasmic aggregates of protein and RNA. These observations support models suggesting that the geometry of a pre-formed nucleocapsid organizes the assembly of the virus membrane proteins into a structure of identical configuration and argues against models suggesting that assembly of the membrane glycoproteins directs the assembly of the nucleocapsid. (C) 2003 Elsevier Science (USA). All rights reserved.