Evidence map›Paper›PMID 22505578›Full record

ArticleNucleic acids research2012

Epstein-Barr virus protein EB2 stimulates cytoplasmic mRNA accumulation by counteracting the deleterious effects of SRp20 on viral mRNAs.

Franceline Juillard, Quentin Bazot, Fabrice Mure, Lionel Tafforeau, Christophe Macri, Chantal Rabourdin-Combe, Vincent Lotteau, Evelyne Manet, Henri Gruffat

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

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  12. Epstein-Barr virus co-opts TFIIH component XPB to specifically activate essential viral lytic promoters.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

9 authors at 3 institutions in 1 country.

Franceline JuillardINSERM U758, Unité de Virologie Humaine, 69364 Lyon, France.
Quentin Bazot
Fabrice Mure
Lionel Tafforeau
Christophe Macri
Chantal Rabourdin-Combe
Vincent Lotteau
Evelyne Manet
Henri Gruffat
Université Claude Bernard Lyon 1 · FRVirologie et Pathologies Humaines · FRImmunologie, Immunopathologie et Chimie Thérapeutique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Epstein-Barr Virus (EBV) protein EB2 (also called Mta, SM and BMLF1), is an essential nuclear protein produced during the replicative cycle of EBV. EB2 is required for the efficient cytoplasmic accumulation of viral mRNAs derived from intronless genes. EB2 is an RNA-binding protein whose expression has been shown to influence RNA stability, splicing, nuclear export and translation. Using a yeast two-hybrid screen, we have identified three SR proteins, SF2/ASF, 9G8 and SRp20, as cellular partners of EB2. Then, by using siRNA to deplete cells of specific SR proteins, we found that SRp20 plays an essential role in the processing of several model mRNAs: the Renilla luciferase reporter mRNA, the human β-globin cDNA transcript and two EBV late mRNAs. These four mRNAs were previously found to be highly dependent on EB2 for their efficient cytoplasmic accumulation. Here, we show that SRp20 depletion results in an increase in the accumulation of these mRNAs, which correlates with an absence of additive effect of EB2, suggesting that EB2 functions by antagonizing SRp20. Moreover, by using RNA-immunoprecipitation assays we found that EB2 enhances the association of SRp20 with the β-globin transcript suggesting that EB2 acts by stabilizing SRp20's labile interactions with the RNA.

Indexed as

beta-GlobinsCell NucleusCytoplasmDown-RegulationHEK293 CellsHeLa CellsHumansLuciferases, RenillaMutationNuclear ProteinsPhosphoproteinsProtein Interaction Domains and MotifsRNA-Binding ProteinsRNA, MessengerRNA, ViralSerine-Arginine Splicing Factorsbeta-GlobinsLuciferases, RenillaNuclear ProteinsPhosphoproteinsRNA-Binding ProteinsRNA, MessengerRNA, ViralSerine-Arginine Splicing FactorsSM protein, Human herpesvirus 4SRSF3 protein, humanTrans-Activators

Identifiers

PMID22505578
PMCPMC3413128
OpenAlexW2154647861

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.