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 解旋酶和引物酶，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-引物复合物由 UL5（解旋酶）、UL52（引物酶）和 UL8（非催化亚基）三种成分组成。UL5 和 UL52 亚基在功能上是相互依赖的，并且 UL8 组件是协调 UL5 和 UL52 活动在病毒复制叉相反方向上进行的必要条件。目前正在开发的抗病毒化合物针对 UL5 和 UL52 的功能。这里，