Evidence map›Paper›PMID 17005694›Full record

ArticleJournal of virology2006

Double-stranded RNA binding by a heterodimeric complex of murine cytomegalovirus m142 and m143 proteins.

Stephanie J Child, Laura K Hanson, Crystal E Brown, Deanna M Janzen, Adam P Geballe

Abstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 48 citations in OpenAlex.

  1. Antagonism of Protein Kinase R by Large DNA Viruses.Pathogens (Basel, Switzerland) · 2022
    Review
  2. Emerging translation strategies during virus-host interaction.Wiley interdisciplinary reviews. RNA · 2021
    Review
  3. Article
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  15. Viral modulation of programmed necrosis.Current opinion in virology · 2013
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors at 3 institutions in 1 country.

Stephanie J ChildDivision of Human Biology, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue N, MS C2-023, Seattle, WA 98109-1024, USA.
Laura K Hanson
Crystal E Brown
Deanna M Janzen
Adam P Geballe
Fred Hutch Cancer Center · USUniversity of Washington · USEastern Virginia Medical School · US

Funding

TRANSLATIONAL CONTROL OF CYTOMEGALOVIRUS GENE EXPRESSIONR01AI026672 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI GEBALLE, ADAM P. · 1994 to 2017
$6.9M
GENETIC DETERMINANTS OF CYTOMEGALOVIRUS PATHOGENESISR01CA041451 · NCI · EASTERN VIRGINIA MEDICAL SCHOOL · PI CAMPBELL, ANN E · 1992 to 2007
$1.7M
NCI NIH HHS R01 CA041451NCI NIH HHS R01 CA 41451NIAID NIH HHS R01 AI 026672NIAID NIH HHS R01 AI026672
6 · The paper itself

Abstract

In response to viral infection, cells activate a variety of antiviral responses, including several that are triggered by double-stranded (ds) RNA. Among these are the protein kinase R and oligoadenylate synthetase/RNase L pathways, both of which result in the shutoff of protein synthesis. Many viruses, including human cytomegalovirus, encode dsRNA-binding proteins that prevent the activation of these pathways and thereby enable continued protein synthesis and viral replication. We have extended these analyses to another member of the beta subfamily of herpesviruses, murine cytomegalovirus (MCMV), and now report that products of the m142 and m143 genes together bind dsRNA. Coimmunoprecipitation experiments demonstrate that these two proteins interact in infected cells, consistent with their previously reported colocalization. Jointly, but not individually, the proteins rescue replication of a vaccinia virus mutant with a deletion of the dsRNA-binding protein gene E3L (VVDeltaE3L). Like the human cytomegalovirus dsRNA-binding protein genes TRS1 and IRS1, m142 and m143 are members of the US22 gene family. We also found that two other members of the MCMV US22 family, M23 and M24, encode dsRNA-binding proteins, but they do not rescue VVDeltaE3L replication. These results reveal that MCMV, like many other viruses, encodes dsRNA-binding proteins, at least two of which can inhibit dsRNA-activated antiviral pathways. However, unlike other well-studied examples, the MCMV proteins appear to act in a heterodimeric complex.

Indexed as

MuromegalovirusDimerizationGene DeletionImmunoprecipitationProtein BindingRNA-Binding ProteinsRNA, Double-StrandedRNA, ViralVaccinia virusViral ProteinsE3L protein, Vaccinia virusRNA-Binding ProteinsRNA, Double-StrandedRNA, ViralViral Proteins

Identifiers

PMID17005694
PMCPMC1617283
OpenAlexW2108822954

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.