A Physical Link between the Pseudorabies Virus Capsid and the Nuclear Egress Complex
A Physical Link between the Pseudorabies Virus Capsid and the Nuclear Egress Complex
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DOI：
10.1128/jvi.05614-11
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发表时间：
2011-11-01
影响因子：
5.4
通讯作者：
Smith, Gregory A.
中科院分区：
文献类型：
--
作者：
Leelawong, Mindy;Guo, Dongsheng;Smith, Gregory A.
组装后，疱疹病毒衣壳通过在内核膜处出芽而离开细胞核。该过程需要两种高度保守的病毒蛋白：pUL31 和 pUL34。在本报告中，我们证明伪狂犬病病毒核出口复合物的 pUL31 成分是一种条件衣壳结合蛋白，在没有 pUL34 的情况下会被暴露。通过荧光显微镜和纯化核内衣壳的蛋白质印迹分析证实了 pUL31 和衣壳之间的相互作用。测试了三种病毒蛋白介导 pUL31-衣壳相互作用的能力：次要衣壳蛋白 pUL25、门户蛋白 pUL6 和终止酶亚基 pUL33。尽管核出口需要每种蛋白质，但 pUL31-衣壳相互作用不需要这些病毒蛋白质。这些发现提供了第一个正式证据，证明疱疹病毒核出口复合物与衣壳相互作用，并对含有 DNA 的衣壳如何选择性地针对核出口产生影响。
Following their assembly, herpesvirus capsids exit the nucleus by budding at the inner nuclear membrane. Two highly conserved viral proteins are required for this process, pUL31 and pUL34. In this report, we demonstrate that the pUL31 component of the pseudorabies virus nuclear egress complex is a conditional capsid-binding protein that is unmasked in the absence of pUL34. The interaction between pUL31 and capsids was confirmed through fluorescence microscopy and Western blot analysis of purified intranuclear capsids. Three viral proteins were tested for their abilities to mediate the pUL31-capsid interaction: the minor capsid protein pUL25, the portal protein pUL6, and the terminase subunit pUL33. Despite the requirement for each protein in nuclear egress, none of these viral proteins were required for the pUL31-capsid interaction. These findings provide the first formal evidence that a herpesvirus nuclear egress complex interacts with capsids and have implications for how DNA-containing capsids are selectively targeted for nuclear egress.