Evidence map›Paper›PMID 11238845›Full record

ArticleJournal of virology2001

Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation.

P Najarro, P Traktman, J A Lewis

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

92 citing papers in PubMed, 188 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
  4. Article
  5. A study of flavonoid inhibitors against Monkeypox H1 phosphatase.Journal of enzyme inhibition and medicinal chemistry · 2025
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Pentacyclo-icosan-19'-one compound fromIn silico pharmacology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Characteristics ofFrontiers in cellular and infection microbiology · 2023
    Article
  18. Article
  19. Article
  20. STAT1 and Its Crucial Role in the Control of Viral Infections.International journal of molecular sciences · 2022
    Review

32 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.

P NajarroDepartment of Anatomy & Cell Biology, SUNY Downstate Medical Center, Brooklyn, New York 11203, USA.
P Traktman
J A Lewis
SUNY Downstate Health Sciences University · USMedical College of Wisconsin · US

Funding

INTERFERONS, MITOCHONDRIA AND CELL GROWTHR01GM046977 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI LEWIS, JOHN A · 1992 to 1994
–
NIGMS NIH HHS GM 4697703
6 · The paper itself

Abstract

We have analyzed the effects of vaccinia virus (VV) on gamma interferon (IFN-gamma) signal transduction. Infection of cells with VV 1 to 2 h prior to treatment with IFN-gamma inhibits phosphorylation and nuclear translocation of Stat1 and consequently blocks accumulation of mRNAs normally induced by IFN-gamma. While phosphorylation of other proteins in the IFN-gamma pathway was not affected, activation of Stat1 by other ligand-receptor systems was also blocked by VV. This block of Stat1 activation was dose dependent, and although viral protein synthesis was not required, entry and uncoating of viral cores appear to be needed to block the accumulation of phosphorylated Stat1. These results suggest that a virion component is responsible for the effect. VV virions contain a phosphatase (VH1) that is sensitive to the phosphatase inhibitor Na(3)VO(4) but not to okadaic acid. Addition of Na(3)VO(4) but not okadaic acid restored normal Stat1 phosphorylation levels in VV-infected cells. Moreover, virions containing reduced levels of VH1 were unable to block the IFN-gamma signaling pathway. In vitro studies show that the phosphatase can bind and dephosphorylate Stat1, indicating that this transcription factor can be a substrate for VH1. Our results reveal a novel mechanism by which VV interferes with the onset of host immune responses by blocking the IFN-gamma signal cascade through the dephosphorylating activity of the viral phosphatase VH1.

Indexed as

Signal TransductionAdenosineCell NucleusCyclic N-OxidesCycloheximideDNA-Binding ProteinsHeLa CellsHumansInterferon-gammaPhosphorylationProtein Tyrosine PhosphatasesSTAT1 Transcription FactorTrans-ActivatorsVaccinia virusViral ProteinsVirionAdenosineadenosine N(1)-oxideCyclic N-OxidesCycloheximideDNA-Binding ProteinsInterferon-gammaProtein Tyrosine PhosphatasesSTAT1 protein, humanSTAT1 Transcription FactorTrans-ActivatorsViral Proteins

Identifiers

PMID11238845
PMCPMC114112
OpenAlexW2059453562

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.