(Q36363780)

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Deletion of the herpes simplex virus 1 UL49 gene results in mRNA and protein translation defects that are complemented by secondary mutations in UL41.

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Europe PubMed Central

PMC publication ID

13 August 2017

Deletion of the herpes simplex virus 1 UL49 gene results in mRNA and protein translation defects that are complemented by secondary mutations in UL41. (English)

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Europe PubMed Central

PMC publication ID

13 August 2017

author name string

Ekaette F Mbong

1

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Europe PubMed Central

PMC publication ID

13 August 2017

Lucille Woodley

2

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Europe PubMed Central

PMC publication ID

13 August 2017

Eric Dunkerley

3

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Europe PubMed Central

PMC publication ID

13 August 2017

Jane E Schrimpf

4

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Europe PubMed Central

PMC publication ID

13 August 2017

Lynda A Morrison

5

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Europe PubMed Central

PMC publication ID

13 August 2017

Carol Duffy

6

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Europe PubMed Central

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13 August 2017

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publication date

5 September 2012

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Europe PubMed Central

PMC publication ID

13 August 2017

Journal of Virology

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Europe PubMed Central

PMC publication ID

13 August 2017

86

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Europe PubMed Central

PMC publication ID

13 August 2017

22

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Europe PubMed Central

PMC publication ID

13 August 2017

12351-12361

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Europe PubMed Central

PMC publication ID

13 August 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3486455/fullTextXML

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How to control an infectious bead string: nucleosome-based regulation and targeting of herpesvirus chromatin.

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The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner.

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The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F.

1 reference

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Evidence for translational regulation by the herpes simplex virus virion host shutoff protein

1 reference

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VP22 of herpes simplex virus 1 promotes protein synthesis at late times in infection and accumulation of a subset of viral mRNAs at early times in infection

1 reference

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Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase.

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Interaction of herpes simplex virus RNase with VP16 and VP22 is required for the accumulation of the protein but not for accumulation of mRNA

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The amino terminus of the herpes simplex virus 1 protein Vhs mediates membrane association and tegument incorporation

1 reference

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The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase A

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Characterization of a UL49-null mutant: VP22 of herpes simplex virus type 1 facilitates viral spread in cultured cells and the mouse cornea

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The U(L)41 protein of herpes simplex virus 1 degrades RNA by endonucleolytic cleavage in absence of other cellular or viral proteins

1 reference

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mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A.

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Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H

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A subpopulation of tegument protein vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells

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Construction of an excisable bacterial artificial chromosome containing a full-length infectious clone of herpes simplex virus type 1: viruses reconstituted from the clone exhibit wild-type properties in vitro and in vivo

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mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease

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Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection

1 reference

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The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions

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mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor

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Bovine herpesvirus 1 tegument protein VP22 interacts with histones, and the carboxyl terminus of VP22 is required for nuclear localization

1 reference

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Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions

1 reference

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Assembly of infectious Herpes simplex virus type 1 virions in the absence of full-length VP22.

1 reference

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Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function

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Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles

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The virion host shutoff protein of herpes simplex virus type 1: messenger ribonucleolytic activity in vitro

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Retention of the herpes simplex virus type 1 (HSV-1) UL37 protein on single-stranded DNA columns requires the HSV-1 ICP8 protein

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Isolation of a herpes simplex virus type 1 mutant with a deletion in the virion host shutoff gene and identification of multiple forms of the vhs (UL41) polypeptide.

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VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells

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Herpes simplex virus mutants defective in the virion-associated shutoff of host polypeptide synthesis and exhibiting abnormal synthesis of alpha (immediate early) viral polypeptides

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Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs

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A mutant of herpes simplex virus type 1 exhibits increased stability of immediate-early (alpha) mRNAs

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Control of mRNA stability by the virion host shutoff function of herpes simplex virus

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Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription

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Generation and properties of the glycoprotein E-related 32K/34K/35K and 55K/57K polypeptides encoded by herpes simplex virus type 1.

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The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49

1 reference

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En passant mutagenesis: a two step markerless red recombination system.

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Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli

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Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT.

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Identifiers

10.1128/JVI.01975-12

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

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