Everett R D, Maul G G, Orr A, Elliott M
MRC Virology Unit, Glasgow, UK.
J Gen Virol. 1995 Apr;76 ( Pt 4):791-8. doi: 10.1099/0022-1317-76-4-791.
Herpes simplex virus type 1 (HSV-1) immediate early protein Vmw110 (also known as ICP0) is required for the fully efficient expression of viral genes during onset of lytic growth and for normal reactivation from latency. Both Vmw110 and the cellular protein PML are members of the RING finger family of zinc binding domain proteins, a family which includes an increasing number of examples from a wide evolutionary range. The function of the RING finger domain is unknown, and the question arises whether the RING finger (like several other examples of conserved domains) fulfils similar functions in these diverse proteins. Another link between Vmw110 and PML is that at early times of HSV-1 infection Vmw110 migrates to distinct nuclear structures which contain the PML protein. In order to test the possibility that PML and Vmw110, or their RING finger domains, fulfill similar functions, we have constructed recombinant viruses that express either intact PML, or a chimeric Vmw110 protein which contains the PML RING finger in place of its own. The results indicate that the PML and Vmw110 RING fingers are not functionally interchangeable, and that PML is not a cellular functional counterpart of Vmw110.
单纯疱疹病毒1型（HSV-1）的立即早期蛋白Vmw110（也称为ICP0）在裂解生长开始期间病毒基因的完全有效表达以及从潜伏期的正常重新激活中是必需的。Vmw110和细胞蛋白PML都是锌结合结构域蛋白的RING指家族成员，该家族包括来自广泛进化范围的越来越多的例子。RING指结构域的功能尚不清楚，问题在于RING指（与其他一些保守结构域的例子一样）在这些不同的蛋白质中是否履行相似的功能。Vmw110和PML之间的另一个联系是，在HSV-1感染的早期，Vmw110迁移到含有PML蛋白的不同核结构中。为了测试PML和Vmw110或它们的RING指结构域履行相似功能的可能性，我们构建了表达完整PML或含有PML RING指以取代其自身RING指的嵌合Vmw110蛋白的重组病毒。结果表明，PML和Vmw110的RING指在功能上不可互换，并且PML不是Vmw110的细胞功能对应物。
