Evidence map›Paper›PMID 17283339›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression.

Susan Parrish, Wolfgang Resch, Bernard Moss

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

80 citing papers in PubMed, 125 citations in OpenAlex.

  1. Perturbation of RNA homeostasis impairs mitochondrial respiration during poxvirus infection through excess RNA accumulation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Ribosomes in poxvirus infection.Current opinion in virology · 2022
    Review
  14. Review
  15. Apprehending the NADViruses · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Susan ParrishLaboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-3210, USA.
Wolfgang Resch
Bernard Moss
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · US

Funding

Poxvirus Gene Expression and DNA ReplicationZIAAI000307 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MOSS, BERNARD · 2009 to 2025
$14.6M
Regulation Of Virus Gene Expression and DNA ReplicationZ01AI000307 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI MOSS, BERNARD · 1985 to 2008
$2.2M
Intramural NIH HHS
6 · The paper itself

Abstract

Previous studies indicated that the vaccinia virus D10 protein, which is conserved in all sequenced poxviruses, participates in the rapid turnover of host and viral mRNAs. D10 contains a motif present in the family of Nudix/MutT enzymes, a subset of which has been shown to enhance mRNA turnover in eukaryotic cells through cleavage of the 5' cap (m7GpppNm-). Here, we demonstrate that a purified recombinant D10 fusion protein possesses an intrinsic activity that liberates m7GDP from capped RNA substrates. Furthermore, point mutations in the Nudix/MutT motif abolished decapping activity. D10 has a strong affinity for capped RNA substrates (Km approximately 3 nm). RNAs of 24-309 nt were decapped to comparable extents, whereas the cap of a 12-nt RNA was uncleaved. At large molar ratios relative to capped RNA substrate, competitor m7GpppG, m7GTP, or m7GDP inhibited decapping, whereas even higher concentrations of unmethylated analogs did not. High concentrations of uncapped RNA were also inhibitory, suggesting that D10 recognizes its substrate through interaction with both cap and RNA moieties. Thus far, poxviruses represent the only virus family shown to encode a Nudix hydrolase-decapping enzyme. Although it may seem self-destructive for a virus to encode a decapping and a capping enzyme, accelerated mRNA turnover helps eliminate competing host mRNAs and allows stage-specific synthesis of viral proteins.

Indexed as

Gene Expression RegulationBinding SitesGene Expression Regulation, ViralNucleotidasesNudix HydrolasesPoint MutationPyrophosphatasesRecombinant Fusion ProteinsRNA-Binding ProteinsRNA Cap AnalogsRNA CapsSubstrate SpecificityVaccinia virusViral Proteins7-methylguanosine triphosphateD10 protein, vaccinia virusNucleotidasesNudix HydrolasesPyrophosphatasesRecombinant Fusion ProteinsRNA-Binding ProteinsRNA Cap AnalogsRNA CapsViral Proteins

Identifiers

PMID17283339
PMCPMC1793903
OpenAlexW1997971074

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.