The three-component helicase/primase complex of herpes simplex virus-1

被引：18

作者：

Bermek, Oya ^{[1
]}

Williams, R. Scott ^{[1
]}

机构：

[1] NIEHS, Genome Integr & Struct Biol Lab, US Dept HHS, NIH, POB 12233, Res Triangle Pk, NC 27709 USA

来源：

OPEN BIOLOGY | 2021年 / 11卷 / 06期

基金：

美国国家卫生研究院;

关键词：

herpesvirus DNA replication; helicase; primase; anti-viral drug; CYTOMEGALOVIRUS DNA-POLYMERASE; PRIMASE INHIBITOR; ANTIVIRAL ACTIVITY; PROTEIN-STRUCTURE; CRYSTAL-STRUCTURE; PRIMER SYNTHESIS; BINDING PROTEIN; UL8; PROTEIN; C-TERMINUS; INTRACELLULAR-LOCALIZATION;

D O I：

10.1098/rsob.210011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页数：13

共 133 条

[1] Crystal structure of the cytomegalovirus DNA polymerase subunit UL44 in complex with the C terminus from the catalytic subunit - Differences in structure and function relative to unliganded UL44 [J].