Near-atomic structure of a giant virus
Near-atomic structure of a giant virus
复制标题
DOI：
10.1038/s41467-019-08319-6
复制
发表时间：
2019-01-23
影响因子：
16.6
通讯作者：
Rossmann, Michael G.
中科院分区：
文献类型：
--
作者：
Fang, Qianglin;Zhu, Dongjie;Rossmann, Michael G.
尽管核胞质大DNA病毒（NCLDVs）是感染许多真核宿主的最大病毒群之一，但这些病毒的近原子分辨率结构仍然未知。本文描述了小球藻草履虫病毒1 （PBCV-1）的一个3.5埃分辨率的二十面体平均衣壳结构。该结构由5040个主衣壳蛋白拷贝，60个penton蛋白拷贝和1800个次要衣壳蛋白组成，其中有13种不同的类型。次要的衣壳蛋白在外衣壳下面形成六角形网络，通过将邻近的衣壳体结合在一起来稳定衣壳。病毒衣壳的大小是由一个卷尺决定的，一个小的衣壳蛋白在病毒粒子中有60个拷贝。在其他NCLDVs中也存在类似于tape-measure蛋白和其他一些次要衣壳蛋白的同源物。因此，类似的衣壳组装途径可能被其他NCLDVs使用。
Although the nucleocytoplasmic large DNA viruses (NCLDVs) are one of the largest group of viruses that infect many eukaryotic hosts, the near-atomic resolution structures of these viruses have remained unknown. Here we describe a 3.5 angstrom resolution icosahedrally averaged capsid structure of Paramecium bursaria chlorella virus 1 (PBCV-1). This structure consists of 5040 copies of the major capsid protein, 60 copies of the penton protein and 1800 minor capsid proteins of which there are 13 different types. The minor capsid proteins form a hexagonal network below the outer capsid shell, stabilizing the capsid by binding neighboring capsomers together. The size of the viral capsid is determined by a tape-measure, minor capsid protein of which there are 60 copies in the virion. Homologs of the tape-measure protein and some of the other minor capsid proteins exist in other NCLDVs. Thus, a similar capsid assembly pathway might be used by other NCLDVs.