ArticleNature communications2021
Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
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- Design of the Inhibitors for Pseudorabies Virus Replication by Reinforcement Learning from HSV-1 DNA Polymerase Inhibitors.ACS omega · 2025Article
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- Discovery of Broad-Spectrum Herpes Antiviral Oxazolidinone Amide Derivatives and Their Structure-Activity Relationships.ACS medicinal chemistry letters · 2024Article
- Dynamics of the Herpes simplex virus DNA polymerase holoenzyme during DNA synthesis and proof-reading revealed by Cryo-EM.Nucleic acids research · 2024Article
- Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus.PLoS pathogens · 2024Article
- Antimicrobial and antiviral evaluation of compounds fromRSC advances · 2023Article
- RETRACTED: Design and Synthesis of Novel 5-((3-(Trifluoromethyl)piperidin-1-yl)sulfonyl)indoline-2,3-dione Derivatives as Promising Antiviral Agents: In Vitro, In Silico, and Structure-Activity Relationship Studies.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Mutations in the monkeypox virus replication complex: Potential contributing factors to the 2022 outbreak.Journal of autoimmunity · 2022Article
- Complete and Prolonged Inhibition of Herpes Simplex Virus Type 1 Infection In Vitro by CRISPR/Cas9 and CRISPR/CasX Systems.International journal of molecular sciences · 2022Article
- Potential therapeutic targets for Mpox: the evidence to date.Expert opinion on therapeutic targetsArticle
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All herpesviruses encode a conserved DNA polymerase that is required for viral genome replication and serves as an important therapeutic target. Currently available herpesvirus therapies include nucleoside and non-nucleoside inhibitors (NNI) that target the DNA-bound state of herpesvirus polymerase and block replication. Here we report the ternary complex crystal structure of Herpes Simplex Virus 1 DNA polymerase bound to DNA and a 4-oxo-dihydroquinoline NNI, PNU-183792 (PNU), at 3.5 Å resolution. PNU bound at the polymerase active site, displacing the template strand and inducing a conformational shift of the fingers domain into an open state. These results demonstrate that PNU inhibits replication by blocking association of dNTP and stalling the enzyme in a catalytically incompetent conformation, ultimately acting as a nucleotide competing inhibitor (NCI). Sequence conservation of the NCI binding pocket further explains broad-spectrum activity while a direct interaction between PNU and residue V823 rationalizes why mutations at this position result in loss of inhibition.
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