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The three-component helicase/primase complex of herpes simplex virus-1.
| Content Provider | Europe PMC |
|---|---|
| Author | Bermek, Oya Williams, R. Scott |
| Copyright Year | 2021 |
| Abstract | 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. |
| Journal | Open Biology |
| Volume Number | 11 |
| PubMed Central reference number | PMC8187027 |
| Issue Number | 6 |
| PubMed reference number | 34102080 |
| e-ISSN | 20462441 |
| DOI | 10.1098/rsob.210011 |
| Language | English |
| Publisher | The Royal Society |
| Publisher Date | 2021-06-09 |
| Access Restriction | Open |
| Rights License | Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. © 2021 The Authors. |
| Subject Keyword | herpesvirus DNA replication helicase primase anti-viral drug |
| Content Type | Text |
| Resource Type | Article |
| Subject | Immunology Biochemistry, Genetics and Molecular Biology Neuroscience |