Evidence map›Paper›PMID 21775450›Full record

ArticleJournal of virology2011

A functional role for TorsinA in herpes simplex virus 1 nuclear egress.

Martina Maric, Jianqiang Shao, Randi J Ryan, Chun-Shu Wong, Pedro Gonzalez-Alegre, Richard J Roller

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 62 citations in OpenAlex.

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  6. SUN2 Modulates the Propagation of HSV-1.Journal of virology · 2022
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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.

Martina MaricDepartment of Microbiology, The University of Iowa, Iowa City, IA 52242, USA.
Jianqiang Shao
Randi J Ryan
Chun-Shu Wong
Pedro Gonzalez-Alegre
Richard J Roller
University of Iowa · USUniversity of Michigan–Ann Arbor · US

Funding

UL34 AND HERPES SIMPLEX VIRUS INFECTIONR01AI041478 · NIAID · UNIVERSITY OF IOWA · PI ROLLER, RICHARD J · 1999 to 2010
$2.0M
Exploring DYT1 pathogenesis: torsinA and the nuclear envelopeK02NS058450 · NINDS · UNIVERSITY OF IOWA · PI GONZALEZ-ALEGRE, PEDRO · 2007 to 2009
$506k
Novel IRES-specific trans acting factors that modulate EV71 translationR03AI070668 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI LI, MEI-LING · 2006 to 2007
$153k
NIAID NIH HHS AI-70668NIAID NIH HHS R01 AI041478NINDS NIH HHS K02 NS058450NINDS NIH HHS K02NS058450
6 · The paper itself

Abstract

Herpes simplex virus 1 (HSV-1) capsids leave the nucleus by a process of envelopment and de-envelopment at the nuclear envelope (NE) that is accompanied by structural alterations of the NE. As capsids translocate across the NE, transient primary enveloped virions form in the perinuclear space. Here, we provide evidence that torsinA (TA), a ubiquitously expressed ATPase, has a role in HSV-1 nuclear egress. TA resides within the lumen of the endoplasmic reticulum (ER)/NE and functions in maintaining normal NE architecture. We show that perturbation of TA normal function by overexpressing torsinA wild type (TAwt) inhibits HSV-1 production. Ultrastructural analysis of infected cells overexpressing TAwt revealed reduced levels of surface virions in addition to accumulation of novel, double-membrane structures called virus-like vesicles (VLVs). Although mainly found in the cytoplasm, VLVs resemble primary virions in their size, by the appearance of the inner membrane, and by the presence of pUL34, a structural component of primary virions. Collectively, our data suggest a model in which interference of TA normal function by overexpression impairs de-envelopment of the primary virions leading to their accumulation in a cytoplasmic membrane compartment. This implies novel functions for TA at the NE.

Indexed as

Host-Pathogen InteractionsVirus ReplicationCell LineHerpesvirus 1, HumanHumansMicroscopy, Electron, TransmissionMicroscopy, FluorescenceMolecular ChaperonesVirionVirus AssemblyMolecular ChaperonesTOR1A protein, human

Identifiers

PMID21775450
PMCPMC3196446
OpenAlexW2080523738

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.