Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave., Morton 3-603, Chicago, IL 60611, USA.
J Virol. 2011 Nov;85(22):11675-84. doi: 10.1128/JVI.05614-11. Epub 2011 Aug 31.
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.
疱疹病毒衣壳组装完成后,通过在内核膜出芽离开细胞核。这一过程需要两种高度保守的病毒蛋白,pUL31 和 pUL34。在本报告中,我们证明了伪狂犬病病毒核出芽复合物中的 pUL31 成分是一种条件性衣壳结合蛋白,在没有 pUL34 的情况下会暴露出来。通过荧光显微镜和纯化的核内衣壳的 Western blot 分析证实了 pUL31 和衣壳之间的相互作用。我们测试了三种病毒蛋白的能力,以确定它们是否能介导 pUL31-衣壳的相互作用:次要衣壳蛋白 pUL25、衣壳蛋白 pUL6 和末端酶亚基 pUL33。尽管这些蛋白都需要在核出芽过程中发挥作用,但它们都不是 pUL31-衣壳相互作用所必需的。这些发现首次提供了正式的证据,证明疱疹病毒核出芽复合物与衣壳相互作用,这对于 DNA 衣壳如何被选择性地靶向核出芽具有重要意义。