ArticleJournal of virology2009
The 3'-to-5' exonuclease activity of vaccinia virus DNA polymerase is essential and plays a role in promoting virus genetic recombination.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 74 citations in OpenAlex.
- Article
- Viral piracy of host RNA phosphatase DUSP11 by avipoxviruses.PLoS pathogens · 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
- Poxvirus A51R Proteins Negatively Regulate Microtubule-Dependent Transport by Kinesin-1.International journal of molecular sciences · 2024Article
- FEAR antiviral response pathway is independent of interferons and countered by poxvirus proteins.Nature microbiology · 2024Article
- Peroxidase-Mimicking Activity of Nanoceria for Label-Free Colorimetric Assay for Exonuclease III Activity.International journal of molecular sciences · 2023Article
- Poxvirus Recombination.Pathogens (Basel, Switzerland) · 2022Review
- Review
- UV Irradiation of Vaccinia Virus-Infected Cells Impairs Cellular Functions, Introduces Lesions into the Viral Genome, and Uncovers Repair Capabilities for the Viral Replication Machinery.Journal of virology · 2022Article
- ADRV 12L: A Ranaviral Putative Rad2 Family Protein Involved in DNA Recombination and Repair.Viruses · 2022Article
- Single 3'-exonuclease-based multifragment DNA assembly method (SENAX).Scientific reports · 2022Article
- Poxviruses Bearing DNA Polymerase Mutations Show Complex Patterns of Cross-Resistance.Biomedicines · 2022Article
- Mechanisms of Coronavirus Genome Stability As Potential Targets for Antiviral Drugs.Herald of the Russian Academy of Sciences · 2022Article
- CRISPR-mediated rapid arming of poxvirus vectors enables facile generation of the novel immunotherapeutic STINGPOX.Frontiers in immunology · 2022Article
- Capripoxviruses, leporipoxviruses, and orthopoxviruses: Occurrences of recombination.Frontiers in microbiology · 2022Review
- Mutation Rates, Mutation Frequencies, and Proofreading-Repair Activities in RNA Virus Genetics.Viruses · 2021Review
- Vaccinia Virus Gene Acquisition through Nonhomologous Recombination.Journal of virology · 2021Article
- The coronavirus proofreading exoribonuclease mediates extensive viral recombination.PLoS pathogens · 2021Article
- When DNA Polymerases Multitask: Functions Beyond Nucleotidyl Transfer.Frontiers in molecular biosciences · 2021Review
- Rapid poxvirus engineering using CRISPR/Cas9 as a selection tool.Communications biology · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poxviruses are subjected to extraordinarily high levels of genetic recombination during infection, although the enzymes catalyzing these reactions have never been identified. However, it is clear that virus-encoded DNA polymerases play some unknown yet critical role in virus recombination. Using a novel, antiviral-drug-based strategy to dissect recombination and replication reactions, we now show that the 3'-to-5' proofreading exonuclease activity of the viral DNA polymerase plays a key role in promoting recombination reactions. Linear DNA substrates were prepared containing the dCMP analog cidofovir (CDV) incorporated into the 3' ends of the molecules. The drug blocked the formation of concatemeric recombinant molecules in vitro in a process that was catalyzed by the proofreading activity of vaccinia virus DNA polymerase. Recombinant formation was also blocked when CDV-containing recombination substrates were transfected into cells infected with wild-type vaccinia virus. These inhibitory effects could be overcome if CDV-containing substrates were transfected into cells infected with CDV-resistant (CDV(r)) viruses, but only when resistance was linked to an A314T substitution mutation mapping within the 3'-to-5' exonuclease domain of the viral polymerase. Viruses encoding a CDV(r) mutation in the polymerase domain still exhibited a CDV-induced recombination deficiency. The A314T substitution also enhanced the enzyme's capacity to excise CDV molecules from the 3' ends of duplex DNA and to recombine these DNAs in vitro, as judged from experiments using purified mutant DNA polymerase. The 3'-to-5' exonuclease activity appears to be an essential virus function, and our results suggest that this might be because poxviruses use it to promote genetic exchange.
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