ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural basis of DNA replication fidelity of the Mpox virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- An integrated review of monkeypox: from pathogen and epidemiology to diagnostics, control, and challenges.Emerging microbes & infections · 2026Review
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- Monkeypox Virus (MPXV) Transmission Dynamics in Neighboring Countries as a Potential Threat to Kazakhstan.Viruses · 2026Review
- DNA deformability in sequence-dependent capture of E. coli gyrase.Nature communications · 2026Article
- Monkeypox (Mpox), a Resurging Global Public Health Concern: An Updated Outlook Through 2025.Current issues in molecular biology · 2026Review
- Assembly and breakage of head-to-head double hexamer reveals mpox virus E5-catalyzed DNA unwinding initiation.Nature communications · 2025Article
- Genomic variability and immunological aspects involved in response to MPXV infection.Frontiers in pharmacology · 2025Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The Mpox virus (MPXV) is an orthopoxvirus that caused a global outbreak in 2022. The poxvirus DNA polymerase complex is responsible for the replication and integrity of the viral genome; however, the molecular mechanisms underlying DNA replication fidelity are still unclear. In this study, we determined the cryoelectron microscopy (cryo-EM) structures of the MPXV F8-A22-E4 polymerase holoenzyme in its editing state, in complex with mismatched primer-template DNA and DNA containing uracil deoxynucleotide. We showed that the MPXV polymerase has a similar replication-to-edit transition mechanism to proofread the mismatched nucleotides like the B-family DNA polymerases of other species. The unique processivity cofactor A22-E4 undergoes conformational changes in different working states and might affect the proofreading process. Moreover, we elucidated the base excision repair (BER) function of E4 as a uracil-DNA glycosylase and the coupling mechanism of genome replication and BER, characteristic of poxviruses. Our findings greatly enhance our molecular understanding of DNA replication fidelity of orthopoxviruses and will stimulate the development of broad-spectrum antiviral drugs.
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Registered trials
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