Evidence map›Paper›PMID 26914506›Full record

ArticleVirology2016

Mutational analysis of varicella-zoster virus (VZV) immediate early protein (IE62) subdomains and their importance in viral replication.

Mohamed I Khalil, Xibing Che, Phillip Sung, Marvin H Sommer, John Hay, Ann M Arvin

Abstract read
In one paragraph

Article in Virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
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  6. Review
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.

Mohamed I KhalilDepartments of Pediatrics and Microbiology & Immunology, Stan ford University School of Medicine, Stanford, CA, United States; Department of Molecular Biology, National Research Centre, El-Buhouth St., Cairo, Egypt. Electronic address: mkhalil2@stanford.edu.
Xibing CheDepartments of Pediatrics and Microbiology & Immunology, Stan ford University School of Medicine, Stanford, CA, United States.
Phillip SungDepartments of Pediatrics and Microbiology & Immunology, Stan ford University School of Medicine, Stanford, CA, United States.
Marvin H SommerDepartments of Pediatrics and Microbiology & Immunology, Stan ford University School of Medicine, Stanford, CA, United States.
John HayDepartment of Microbiology and Immunology, School of Medicine and Biomedical Science, University at Buffalo, Buffalo, NY, United States.
Ann M ArvinDepartments of Pediatrics and Microbiology & Immunology, Stan ford University School of Medicine, Stanford, CA, United States.

Funding

Varicella-Zoster Virus: T Cell/Skin Tropisms &ImmunityR01AI020459 · NIAID · STANFORD UNIVERSITY · PI OLIVER, STEFAN LYNE · 1985 to 2023
$6.4M
Varicella-zoster Virus: Tegument Proteins in PathogenesisR01AI053846 · NIAID · STANFORD UNIVERSITY · PI ARVIN, ANN · 2003 to 2012
$4.1M
Varicella-Zoster Virus: T Cell/Skin Tropisms & ImmunityR37AI020459 · NIAID · STANFORD UNIVERSITY · PI ARVIN, ANN · 2016 to 2020
$2.0M
Structure/Function of Varicella Zoster Virus DNAR01AI018449 · NIAID · U.S. UNIFORMED SERVICES UNIV OF HLTH SCI · PI RUYECHAN, WILLIAM T · 1985 to 2007
$1.8M
Structure/Function of Varicella Zoster Virus DNA.R56AI018449 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI HAY, JOHN I. · 2008 to 2009
$788k
Structure/Function of Varicella Zoster Virus DNAR21AI018449 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI RUYECHAN, WILLIAM T · 2002 to 2002
$304k
NIAID NIH HHS AI018449NIAID NIH HHS AI020459NIAID NIH HHS AI053846NIAID NIH HHS R01 AI018449NIAID NIH HHS R01 AI020459NIAID NIH HHS R01 AI053846NIAID NIH HHS R21 AI018449NIAID NIH HHS R37 AI020459NIAID NIH HHS R56 AI018449
6 · The paper itself

Abstract

VZV IE62 is an essential, immediate-early, tegument protein and consists of five domains. We generated recombinant viruses carrying mutations in the first three IE62 domains and tested their influence on VZV replication kinetics. The mutations in domain I did not affect replication kinetics while domain II mutations, disrupting the DNA binding and dimerization domain (DBD), were lethal for VZV replication. Mutations in domain III of the nuclear localization signal (NLS) and the two phosphorylation sites S686A/S722A resulted in slower growth in early and late infection respectively and were associated with IE62 accumulation in the cytoplasm and nucleus respectively. This study mapped the functional domains of IE62 in context of viral infection, indicating that DNA binding and dimerization domain is essential for VZV replication. In addition, the correct localization of IE62, whether nuclear or cytoplasmic, at different points in the viral life cycle, is important for normal progression of VZV replication.

Indexed as

Cell Line, TumorCell NucleusCytoplasmGene ExpressionGenes, ReporterHerpesvirus 3, HumanHumansImmediate-Early ProteinsLuciferasesMutationNuclear Localization SignalsPhosphorylationProtein Structure, TertiaryReassortant VirusesTrans-ActivatorsViral Envelope ProteinsIE62 protein, Human herpesvirus 3Immediate-Early ProteinsLuciferasesNuclear Localization SignalsTrans-ActivatorsViral Envelope ProteinsDBDDimerizationIE62NLSPutative phosphorylation siteTADVZV

Identifiers

PMID26914506
PMCPMC4826839

What OpenQuestion holds

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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.