ArticleThe Journal of biological chemistry2014
UL52 primase interactions in the herpes simplex virus 1 helicase-primase are affected by antiviral compounds and mutations causing drug resistance.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Structural and mechanistic insights into the herpes simplex virus type 1 helicase-primase primosome.Cell discovery · 2025Article
- Structural and mechanistic insights into herpesvirus helicase-primase and its therapeutic inhibitors.Nature microbiology · 2025Article
- Structural basis of herpesvirus helicase-primase inhibition by pritelivir and amenamevir.Science advances · 2025Article
- Ophthalmic Solutions with a Broad Antiviral Action: Evaluation of Their Potential against Ocular Herpetic Infections.Microorganisms · 2022Article
- Characteristics of Helicase-Primase Inhibitor Amenamevir-Resistant Herpes Simplex Virus.Antimicrobial agents and chemotherapy · 2021Article
- The three-component helicase/primase complex of herpes simplex virus-1.Open biology · 2021Review
- Development and evaluation of a host-targeted antiviral that abrogates herpes simplex virus replication through modulation of arginine-associated metabolic pathways.Antiviral research · 2016Article
- Comparative Genomics of Herpesviridae Family to Look for Potential Signatures of Human Infecting Strains.International journal of genomics · 2016Article
- DNA replication catalyzed by herpes simplex virus type 1 proteins reveals trombone loops at the fork.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpes simplex virus 1 (HSV-1) UL5/8/52 helicase-primase complex is required for DNA unwinding at the replication fork and synthesis of primers during virus replication, and it has become a promising novel target for antiviral therapy. Using molecular cloning, we have identified three separate domains of UL52. Co-immunoprecipitation experiments in extracts from cells transiently expressing HA-tagged UL5, FLAG-UL8, and enhanced GFP-tagged UL52 domains revealed that the N-terminal domain of UL52 primase binds UL5 helicase and the middle domain interacts with the UL8 accessory protein. In addition, an interaction between the single strand DNA-binding protein ICP8 and the UL52 middle domain was observed. The complex between UL5 and UL52 was stabilized by the antiviral compound BAY 54-6322, and mutations providing resistance to the drug obliterate this effect. Our results also suggest a mechanism for accommodating conformational strain resulting from movement of UL5 and UL52 in opposite directions on the lagging strand template, and they identify molecular complexes that can be further examined by structural biology techniques to resolve the mechanism of primer synthesis during herpesvirus replication. Finally, they help to explain the mechanism of action of a novel class of antiviral compounds currently being evaluated in clinical trials.
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