Evidence map›Paper›PMID 29925667›Full record

ArticleJournal of virology2018

Multiple Posttranscriptional Strategies To Regulate the Herpes Simplex Virus 1 vhs Endoribonuclease.

Gillian Elliott, Kathleen Pheasant, Katja Ebert-Keel, Julianna Stylianou, Ashley Franklyn, Juliet Jones

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Gillian ElliottSection of Virology, Department of Microbial Sciences, Faculty of Health & Medical Sciences, University of Surrey, Guildford, United Kingdom g.elliott@surrey.ac.uk.
Kathleen PheasantSection of Virology, Department of Microbial Sciences, Faculty of Health & Medical Sciences, University of Surrey, Guildford, United Kingdom.
Katja Ebert-KeelSection of Virology, Department of Microbial Sciences, Faculty of Health & Medical Sciences, University of Surrey, Guildford, United Kingdom.
Julianna StylianouSection of Virology, Faculty of Medicine Building, Imperial College London, London, United Kingdom.
Ashley FranklynSection of Virology, Department of Microbial Sciences, Faculty of Health & Medical Sciences, University of Surrey, Guildford, United Kingdom.
Juliet JonesSection of Virology, Department of Microbial Sciences, Faculty of Health & Medical Sciences, University of Surrey, Guildford, United Kingdom.
University of Surrey · GBImperial College London · GB

Funding

Medical Research Council G0601605Medical Research Council MR/M011607/1
6 · The paper itself

Abstract

The herpes simplex virus 1 (HSV-1) virion host shutoff (vhs) protein is an endoribonuclease that binds to the cellular translation initiation machinery and degrades associated mRNAs, resulting in the shutoff of host protein synthesis. Hence, its unrestrained activity is considered lethal, and it has been proposed that vhs is regulated by two other virus proteins, VP22 and VP16. We have found that during infection, translation of vhs requires VP22 but not the VP22-VP16 complex. Moreover, in the absence of VP22, vhs is not overactive against cellular or viral transcripts. In transfected cells, vhs was also poorly translated, correlating with the aberrant localization of its mRNA. Counterintuitively, vhs mRNA was predominantly nuclear in cells where vhs protein was detected. Likewise, transcripts from cotransfected plasmids were also retained in the same nuclei where vhs mRNA was located, while poly(A) binding protein (PABP) was relocalized to the nucleus in a vhs-dependent manner, implying a general block to mRNA export. Coexpression of VP16 and VP22 rescued the cytoplasmic localization of vhs mRNA but failed to rescue vhs translation. We identified a 230-nucleotide sequence in the 5' region of vhs that blocked its translation and, when transferred to a heterologous green fluorescent protein transcript, reduced translation without altering mRNA levels or localization. We propose that expression of vhs is tightly regulated by a combination of inherent untranslatability and autoinduced nuclear retention of its mRNA that results in a negative feedback loop, with nuclear retention but not translation of vhs mRNA being the target of rescue by the vhs-VP16-VP22 complex.

Indexed as

5' Untranslated RegionsCell NucleusGene Expression Regulation, EnzymologicGene Expression Regulation, ViralHerpes Simplex Virus Protein Vmw65Herpesvirus 1, HumanOpen Reading FramesRibonucleasesRNA Processing, Post-TranscriptionalViral ProteinsViral Structural Proteins5' Untranslated RegionsHerpes Simplex Virus Protein Vmw65herpes simplex virus type 1 protein VP22RibonucleasesViral ProteinsViral Structural Proteinsvirion host shutoff protein, SimplexvirusendoribonucleaseHSV-1PABPvhsVP16VP22

Identifiers

PMID29925667
PMCPMC6096803
OpenAlexW2809527595

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.