Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Schlossgarten 4, 91054 Erlangen, Germany; E-Mail:
Viruses. 2009 Dec;1(3):1240-64. doi: 10.3390/v1031240. Epub 2009 Dec 15.
In recent studies we and others have identified the cellular proteins PML, hDaxx, and Sp100, which form a subnuclear structure known as nuclear domain 10 (ND10) or PML nuclear bodies (PML-NBs), as host restriction factors that counteract herpesviral infections by inhibiting viral replication at different stages. The antiviral function of ND10, however, is antagonized by viral regulatory proteins (e.g., ICP0 of herpes simplex virus; IE1 of human cytomegalovirus) which induce either a modification or disruption of ND10. This review will summarize the current knowledge on how viral replication is inhibited by ND10 proteins. Furthermore, herpesviral strategies to defeat this host defense mechanism are discussed.
在最近的研究中，我们和其他人已经确定了细胞蛋白 PML、hDaxx 和 Sp100，它们形成了一个核内结构，称为核域 10（ND10）或 PML 核体（PML-NBs），作为宿主限制因子，通过在不同阶段抑制病毒复制来抵抗疱疹病毒感染。然而，ND10 的抗病毒功能受到病毒调节蛋白（例如单纯疱疹病毒的 ICP0；人巨细胞病毒的 IE1）的拮抗，这些调节蛋白诱导 ND10 的修饰或破坏。这篇综述将总结目前关于 ND10 蛋白如何抑制病毒复制的知识。此外，还讨论了疱疹病毒战胜这种宿主防御机制的策略。
