ArticleScience advances2023
Structural basis for the assembly of the DNA polymerase holoenzyme from a monkeypox virus variant.
Article in Science advances, 2023. 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, 24 citations in OpenAlex.
- An integrated review of monkeypox: from pathogen and epidemiology to diagnostics, control, and challenges.Emerging microbes & infections · 2026Review
- Article
- Structure-based multi-pocket virtual screening identifies FDA-approved candidate compounds targeting MPXV thymidylate kinase.Frontiers in cellular and infection microbiology · 2026Article
- Article
- Inhibition of monkeypox polymerase holoenzyme and methyltransferase using bioactive compounds of black tea: a computational approach.Scientific reports · 2025Article
- Mpox: disease manifestations and therapeutic development.Journal of virology · 2025Review
- Computational screening of antiviral candidates for Monkeypox virus DNA polymerase and A42R protein.PLoS neglected tropical diseases · 2025Article
- Structural basis of DNA replication fidelity of the Mpox virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Mpox Virus and its ocular surface manifestations.The ocular surface · 2024Review
- Structural and functional insights into the helicase protein E5 of Mpox virus.Cell discovery · 2024Article
- Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus.PLoS pathogens · 2024Article
- Missing subunits of Mpox replication complex: Possible impact on structural organization.The Journal of infection · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ongoing global pandemic caused by a variant of the monkeypox (or mpox) virus (MPXV) has prompted widespread concern. The MPXV DNA polymerase holoenzyme, consisting of F8, A22, and E4, is vital for replicating the viral genome and represents a crucial target for the development of antiviral drugs. However, the assembly and working mechanism for the DNA polymerase holoenzyme of MPXV remains elusive. Here, we present the cryo-electron microscopy (cryo-EM) structure of the DNA polymerase holoenzyme at an overall resolution of 3.5 Å. Unexpectedly, the holoenzyme is assembled as a dimer of heterotrimers, of which the extra interface between the thumb domain of F8 and A22 shows a clash between A22 and substrate DNA, suggesting an autoinhibition state. Addition of exogenous double-stranded DNA shifts the hexamer into trimer exposing DNA binding sites, potentially representing a more active state. Our findings provide crucial steps toward developing targeted antiviral therapies for MPXV and related viruses.
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Registered trials
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