Complementation of a herpes simplex virus ICP0 null mutant by varicella-zoster virus ORF61p. Academic Article uri icon

Overview

MeSH

  • Antigens, Nuclear
  • Autoantigens
  • Cell Line, Tumor
  • Genetic Complementation Test
  • Humans
  • Interferon-alpha
  • Mutation
  • Nuclear Proteins
  • Transcription Factors
  • Tumor Suppressor Proteins

MeSH Major

  • Gene Deletion
  • Herpesvirus 3, Human
  • Immediate-Early Proteins
  • Recombination, Genetic
  • Simplexvirus
  • Ubiquitin-Protein Ligases
  • Viral Proteins

abstract

  • The herpes simplex virus (HSV) ICP0 protein acts to overcome intrinsic cellular defenses that repress viral alpha gene expression. In that vein, viruses that have mutations in ICP0's RING finger or are deleted for the gene are sensitive to interferon, as they fail to direct degradation of promyelocytic leukemia protein (PML), a component of host nuclear domain 10s. While varicella-zoster virus is also insensitive to interferon, ORF61p, its ICP0 ortholog, failed to degrade PML. A recombinant virus with each coding region of the gene for ICP0 replaced with sequences encoding ORF61p was constructed. This virus was compared to an ICP0 deletion mutant and wild-type HSV. The recombinant degraded only Sp100 and not PML and grew to higher titers than its ICP0 null parental virus, but it was sensitive to interferon, like the virus from which it was derived. This analysis permitted us to compare the activities of ICP0 and ORF61p in identical backgrounds and revealed distinct biologic roles for these proteins.

publication date

  • October 2009

has subject area

  • Antigens, Nuclear
  • Autoantigens
  • Cell Line, Tumor
  • Gene Deletion
  • Genetic Complementation Test
  • Herpesvirus 3, Human
  • Humans
  • Immediate-Early Proteins
  • Interferon-alpha
  • Mutation
  • Nuclear Proteins
  • Recombination, Genetic
  • Simplexvirus
  • Transcription Factors
  • Tumor Suppressor Proteins
  • Ubiquitin-Protein Ligases
  • Viral Proteins

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2753114

Digital Object Identifier (DOI)

  • 10.1128/JVI.01144-09

PubMed ID

  • 19656893

Additional Document Info

start page

  • 10637

end page

  • 10643

volume

  • 83

number

  • 20