Evidence map›Paper›PMID 12186924›Full record

ArticleJournal of virology2002

The Epstein-Barr virus SM protein is functionally similar to ICP27 from herpes simplex virus in viral infections.

Julie L Boyer, Sankar Swaminathan, Saul J Silverstein

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  7. Spironolactone blocks Epstein-Barr virus production by inhibiting EBV SM protein function.Proceedings of the National Academy of Sciences of the United States of America · 2016
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  17. Viral regulation of mRNA export.Journal of virology · 2004
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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

3 authors at 2 institutions in 1 country.

Julie L BoyerDepartment of Microbiology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.
Sankar Swaminathan
Saul J Silverstein
Columbia University · USUniversity of Florida Health · US

Funding

POSTTRANSCRIPTIONAL GENE REGULATION BY EBV SM PROTEINR01CA081133 · NCI · UNIVERSITY OF UTAH · PI SWAMINATHAN, SANKAR · 1999 to 2022
$4.9M
GENETIC AND BIOCHEMICAL STUDIES OF THE HSV IE-O GENER01AI033952 · NIAID · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI SILVERSTEIN, SAUL J · 1994 to 2003
$1.6M
VIRAL MRNA EXPORT MEDIATED BY THE HSV-1 ICP27 PROTEINF32GM020693 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI BOYER, JULIE L · 2000 to 2001
$73k
NCI NIH HHS CA-81133NCI NIH HHS R01 CA081133NIAID NIH HHS AI-33952NIAID NIH HHS R01 AI033952NIGMS NIH HHS 1F32-GM20693NIGMS NIH HHS F32 GM020693
6 · The paper itself

Abstract

The herpes simplex virus type 1 (HSV-1) ICP27 protein is an essential RNA-binding protein that shuttles between the nucleus and cytoplasm to increase the cytoplasmic accumulation of viral late mRNAs. ICP27 homologs have been identified in each of the herpesvirus subfamilies, and accumulating evidence indicates that homologs from the gammaherpesvirus subfamily function similarly to ICP27. In particular, the Epstein-Barr virus (EBV) SM protein posttranscriptionally regulates gene expression, binds RNA in vitro and in vivo, and shuttles between the nucleus and cytoplasm. To determine if these two proteins function through a common mechanism, the ability of EBV SM to complement the growth defect of an HSV-1 ICP27-null virus was examined in a transient-expression assay. ICP27 stimulated the growth of the null mutant more efficiently than did SM, but the ability of SM to compensate for the ICP27 defects suggests conservation of common functions. To assay for complementation in the context of a viral infection, the growth properties of an HSV recombinant expressing SM in an ICP27-null background were analyzed. SM stimulated growth of the recombinant, although this growth was reduced by comparison to that of an ICP27-expressing virus. By contrast, an HSV recombinant expressing an SM mutant allele defective for transactivation activity and nucleocytoplasmic shuttling did not grow at all. These results suggest that SM and ICP27 may regulate gene expression through a common pathway that is evolutionarily conserved in herpesviruses.

Indexed as

AnimalsCell NucleusChlorocebus aethiopsCytoplasmGenetic Complementation TestHerpesvirus 1, HumanHerpesvirus 4, HumanHumansImmediate-Early ProteinsPhosphoproteinsPhylogenySequence Analysis, DNATrans-ActivatorsVero CellsViral Plaque AssayViral ProteinsICP27 protein, human herpesvirus 1Immediate-Early ProteinsPhosphoproteinsSM protein, Human herpesvirus 4Trans-ActivatorsViral Proteins

Identifiers

PMID12186924
PMCPMC136475
OpenAlexW2146311664

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.