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Herpes Simplex Virus Helicase–Primase Complex (HSV Helicase-Primase)
- Target
- HSV Helicase-Primase
- Molecular classification
- Enzyme, Helicase, Primase, Multi-protein complex
01
Overview
The herpes simplex virus (HSV) helicase–primase complex is a multi-protein enzyme essential for viral DNA replication. It comprises the UL5 (helicase), UL52 (primase), and UL8 (non-catalytic) subunits. This complex unwinds double-stranded DNA and synthesizes RNA primers necessary for DNA synthesis. It is a validated antiviral target, with inhibitors like pritelivir demonstrating efficacy against HSV infections, including acyclovir-resistant strains. Resistance mutations often map to specific residues in the catalytic domains of UL5 and UL52. Targeting this complex offers an alternative strategy against drug-resistant strains by blocking essential steps upstream in genome processing.
- Other names
- HSV helicase-primaseUL5-UL52-UL8 complexHSV DNA replication complex
02
Mechanism of action
Inhibition of helicase and/or primase activity, thereby blocking viral DNA replication.
03
Biological functions
DNA replicationDNA unwindingRNA primer synthesis
04
Disease associations
InfectionHerpes simplex virus infection
05
Safety considerations
Potential for drug resistance (mutations in UL5 and UL52)Specificity for different herpesvirus subtypes (alpha vs. beta vs. gamma)
06
Interacting drugs
Pritelivir
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