Evidence map›Paper›PMID 27654296›Full record

ArticleJournal of virology2016

Extragenic Suppression of a Mutation in Herpes Simplex Virus 1 UL34 That Affects Lamina Disruption and Nuclear Egress.

Amber Vu, Chelsea Poyzer, Richard Roller

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2016. 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
1.0field-weighted citation impact, top 22% 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, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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

3 authors at 1 institution in 1 country.

Amber VuDepartment of Microbiology, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa.
Chelsea PoyzerDepartment of Microbiology, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa.
Richard RollerDepartment of Microbiology, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa richard-roller@uiowa.edu.
University of Iowa · US

Funding

RESEARCH TRAINING IN INFECTIOUS DISEASEST32AI007343 · NIAID · UNIVERSITY OF IOWA · PI STAPLETON, JACK T. · 1988 to 2024
$5.0M
Training in Molecular Virology, Viral Pathogenesis and Viral VectorsT32AI007533 · NIAID · UNIVERSITY OF IOWA · PI Stanley Perlman · 1998 to 2026
$2.5M
UL34 AND HERPES SIMPLEX VIRUS INFECTIONR01AI041478 · NIAID · UNIVERSITY OF IOWA · PI ROLLER, RICHARD J · 1999 to 2010
$2.0M
TorsinA and Nuclear Envelope Function in HSV InfectionR21AI099597 · NIAID · UNIVERSITY OF IOWA · PI ROLLER, RICHARD J · 2012 to 2013
$415k
NIAID NIH HHS R01 AI041478NIAID NIH HHS R21 AI099597NIAID NIH HHS T32 AI007343NIAID NIH HHS T32 AI007533
6 · The paper itself

Abstract

Nuclear egress of herpesviruses is accompanied by changes in the architecture of the nuclear membrane and nuclear lamina that are thought to facilitate capsid access to the inner nuclear membrane (INM) and curvature of patches of the INM around the capsid during budding. Here we report the properties of a point mutant of pUL34 (Q163A) that fails to induce gross changes in nuclear architecture or redistribution of lamin A/C. The UL34(Q163A) mutant shows a roughly 100-fold defect in single-step growth, and it forms small plaques. This mutant has a defect in nuclear egress, and furthermore, it fails to disrupt nuclear shape or cause observable displacement of lamin A/C despite retaining the ability to recruit the pUS3 and PKC protein kinases and to mediate phosphorylation of emerin. Extragenic suppressors of the UL34(Q163A) phenotype were isolated, and all of them carry a single mutation of arginine 229 to leucine in UL31. Surprisingly, although this UL31 mutation largely restores virus replication, it does not correct the lamina disruption defect, suggesting that, in Vero cells, changes in nuclear shape and gross displacements of lamin A/C may facilitate but are unnecessary for nuclear egress. IMPORTANCE: Herpesvirus nuclear egress is an essential and conserved process that requires close association of the viral capsid with the inner nuclear membrane and budding of the capsid into that membrane. Access to the nuclear membrane and tight curvature of that membrane are thought to require disruption of the nuclear lamina that underlies the inner nuclear membrane, and consistent with this idea, herpesvirus infection induces biochemical and architectural changes at the nuclear membrane. The significance of the nuclear membrane architectural changes is poorly characterized. The results presented here address that deficiency in our understanding and show that a combination of mutations in two of the viral nuclear egress factors results in a failure to accomplish at least two components of lamina disruption while still allowing relatively efficient viral replication, suggesting that changes in nuclear shape and displacement of lamins are not necessary for herpes simplex virus 1 (HSV-1) nuclear egress.

Indexed as

Point MutationAmino Acid SubstitutionAnimalsCell Nucleus ShapeChlorocebus aethiopsHEK293 CellsHerpesvirus 1, HumanHumansLamin Type AModels, MolecularNuclear EnvelopeNuclear LaminaNuclear ProteinsProtein ConformationVero CellsViral ProteinsLamin Type ANuclear ProteinsUL31 protein, Human herpesvirus 1UL34 protein, Human herpesvirus 1Viral Proteins

Identifiers

PMID27654296
PMCPMC5110175
OpenAlexW2522921974

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.