Evidence map›Paper›PMID 30541834›Full record

ArticleJournal of virology2019

Cellular RNA Helicase DHX9 Interacts with the Essential Epstein-Barr Virus (EBV) Protein SM and Restricts EBV Lytic Replication.

Wenmin Fu, Dinesh Verma, Ashlee Burton, Sankar Swaminathan

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

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  12. Pathogenesis of Human Gammaherpesviruses: Recent Advances.Current clinical microbiology reports · 2019
    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

4 authors at 1 institution in 1 country.

Wenmin FuDivision of Infectious Diseases, Department of Medicine, University of Utah School of Medicine, Salt Lake City, Utah, USA.
Dinesh VermaDivision of Infectious Diseases, Department of Medicine, University of Utah School of Medicine, Salt Lake City, Utah, USA.
Ashlee BurtonDivision of Infectious Diseases, Department of Medicine, University of Utah School of Medicine, Salt Lake City, Utah, USA.
Sankar SwaminathanDivision of Infectious Diseases, Department of Medicine, University of Utah School of Medicine, Salt Lake City, Utah, USA sankar.swaminathan@hsc.utah.edu.ORCID 0000-0002-9773-1277
University of Utah · US

Funding

POSTTRANSCRIPTIONAL GENE REGULATION BY EBV SM PROTEINR01CA081133 · NCI · UNIVERSITY OF UTAH · PI SWAMINATHAN, SANKAR · 1999 to 2022
$4.9M
Restriction of Oncogenic Herpesviruses by Host Cell FactorsI01BX002262 · VA · VA SALT LAKE CITY HEALTHCARE SYSTEM · PI SWAMINATHAN, SANKAR · 2015 to 2019
–
BLRD VA I01 BX002262NCI NIH HHS R01 CA081133
6 · The paper itself

Abstract

Epstein-Barr virus (EBV) SM protein is an RNA-binding protein that has multiple posttranscriptional gene regulatory functions essential for EBV lytic replication. In this study, we identified an interaction between SM and DHX9, a DExH-box helicase family member, by mass spectrometry and coimmunoprecipitation. DHX9 participates in many cellular pathways involving RNA, including transcription, processing, transport, and translation. DHX9 enhances virus production or infectivity of a wide variety of DNA and RNA viruses. Surprisingly, an increase in EBV late gene expression and virion production occurred upon knockdown of DHX9. To further characterize the SM-DHX9 interaction, we performed immunofluorescence microscopy of EBV-infected cells and found that DHX9 partially colocalized with SM in nuclear foci during EBV lytic replication. However, the positive effect of DHX9 depletion on EBV lytic gene expression was not confined to SM-dependent genes, indicating that the antiviral effect of DHX9 was not mediated through its effects on SM. DHX9 enhanced activation of innate antiviral pathways comprised of several interferon-stimulated genes that are active against EBV. SM inhibited the transcription-activating function of DHX9, which acts through cAMP response elements (CREs), suggesting that SM may also act to counteract DHX9's antiviral functions during lytic replication.

Indexed as

DEAD-box RNA HelicasesDNA ReplicationDNA, ViralHEK293 CellsHerpesvirus 4, HumanHost-Pathogen InteractionsHumansImmediate-Early ProteinsNeoplasm ProteinsTrans-ActivatorsTranscriptional ActivationTranscription FactorsVirus ReplicationBRLF1 protein, Human herpesvirus 4DEAD-box RNA HelicasesDHX9 protein, humanDNA, ViralImmediate-Early ProteinsNeoplasm ProteinsTrans-ActivatorsTranscription FactorsEpstein-Barr virushelicaseinnate immune responseprotein-protein interactionsRNA processingtranscriptional activationvirus-host interactions

Identifiers

PMID30541834
PMCPMC6364004
OpenAlexW2903693306

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.