Genome Integrity and Structural Biology Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
Open Biol. 2021 Jun;11(6):210011. doi: 10.1098/rsob.210011. Epub 2021 Jun 9.
Herpes simplex virus type 1 (HSV-1) is one of the nine herpesviruses that infect humans. HSV-1 encodes seven proteins to replicate its genome in the hijacked human cell. Among these are the herpes virus DNA helicase and primase that are essential components of its replication machinery. In the HSV-1 replisome, the helicase-primase complex is composed of three components including UL5 (helicase), UL52 (primase) and UL8 (non-catalytic subunit). UL5 and UL52 subunits are functionally interdependent, and the UL8 component is required for the coordination of UL5 and UL52 activities proceeding in opposite directions with respect to the viral replication fork. Anti-viral compounds currently under development target the functions of UL5 and UL52. Here, we review the structural and functional properties of the UL5/UL8/UL52 complex and highlight the gaps in knowledge to be filled to facilitate molecular characterization of the structure and function of the helicase-primase complex for development of alternative anti-viral treatments.
单纯疱疹病毒 1 型（HSV-1）是感染人类的九种疱疹病毒之一。HSV-1 编码七种蛋白质，以在被劫持的人类细胞中复制其基因组。其中包括疱疹病毒 DNA 解旋酶和引发酶，它们是其复制机制的重要组成部分。在 HSV-1 复制体中，解旋酶-引发酶复合物由三个成分组成，包括 UL5（解旋酶）、UL52（引发酶）和 UL8（非催化亚基）。UL5 和 UL52 亚基在功能上是相互依赖的，UL8 成分对于协调相对于病毒复制叉以相反方向进行的 UL5 和 UL52 活性是必需的。目前正在开发的抗病毒化合物针对 UL5 和 UL52 的功能。在这里，我们回顾了 UL5/UL8/UL52 复合物的结构和功能特性，并强调了为促进解旋酶-引发酶复合物的结构和功能的分子表征以开发替代抗病毒治疗方法而需要填补的知识空白。
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