Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles
Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles
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DOI：
10.1128/jvi.78.15.8078-8084.2004
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发表时间：
2004-08-01
影响因子：
5.4
通讯作者：
Heinz, FX
中科院分区：
文献类型：
--
作者：
Kiermayr, S;Kofler, RM;Heinz, FX
黄病毒有一个球形衣壳，由单个衣壳蛋白的多个拷贝组成，与病毒包膜不同，黄病毒显然没有二十面体结构。到目前为止，试图从纯化的病毒粒子中分离出不同的颗粒衣壳和可溶形式的衣壳蛋白，以及在体外组装衣壳样颗粒，基本上都是不成功的。本文描述了从蜱传脑炎（TBE）病毒中分离出的核衣壳及其在高盐处理下分解成衣壳蛋白二聚体的过程。纯化的衣壳蛋白二聚体与体外转录的病毒RNA结合，可以在体外组装成衣壳样颗粒。当使用单链DNA寡核苷酸时，也可以获得颗粒结构。这些数据表明二聚体衣壳蛋白在黄病毒的组装过程中起着基本的构建块的作用。
Flaviviruses have a spherical capsid that is composed of multiple copies of a single capsid protein and, in contrast to the viral envelope, apparently does not have an icosahedral structure. So far, attempts to isolate distinct particulate capsids and soluble forms of the capsid protein from purified virions as well as to assemble capsid-like particles in vitro have been largely unsuccessful. Here we describe the isolation of nucleocapsids from tick-borne encephalitis (TBE) virus and their disintegration into a capsid protein dimer by high-salt treatment. Purified capsid protein dimers could be assembled in vitro into capsid-like particles when combined with in vitro transcribed viral RNA. Particulate structures could also be obtained when single-stranded DNA oligonucleotides were used. These data suggest that the dimeric capsid protein functions as a basic building block in the assembly process of flaviviruses.