Histone deacetylases 1 and 2 are phosphorylated at novel sites during varicella-zoster virus infection. Academic Article uri icon

Overview

MeSH

  • Cell Line
  • Cell Line, Tumor
  • Genetic Vectors
  • Humans
  • Phosphorylation
  • Protein Kinases
  • Viral Proteins

MeSH Major

  • Herpes Zoster
  • Herpesvirus 3, Human
  • Histone Deacetylase 1
  • Histone Deacetylase 2

abstract

  • ORF66p, a virion-associated varicella-zoster virus (VZV) protein, is a member of a conserved Alphaherpesvirinae kinase family with homology to herpes simplex virus US3 kinase. Expression of ORF66p in cells infected with VZV or an adenovirus expressing only ORF66p results in hyperphosphorylation of histone deacetylase 1 (HDAC1) and HDAC2. Mapping studies reveal that phosphorylation is at a unique conserved Ser residue in the C terminus of both HDACs. This modification requires an active kinase domain in ORF66p, as neither protein is phosphorylated in cells infected with VZV lacking kinase activity. However, hyperphosphorylation appears to occur indirectly, as within the context of in vitro kinase reactions, purified ORF66p phosphorylates a peptide derived from ORF62p, a known substrate, but does not phosphorylate HDAC. These results support a model where ORF66p is necessary but not sufficient to effect hyperphosphorylation of HDAC1 and HDAC2.

publication date

  • November 2009

has subject area

  • Cell Line
  • Cell Line, Tumor
  • Genetic Vectors
  • Herpes Zoster
  • Herpesvirus 3, Human
  • Histone Deacetylase 1
  • Histone Deacetylase 2
  • Humans
  • Phosphorylation
  • Protein Kinases
  • Viral Proteins

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2772673

Digital Object Identifier (DOI)

  • 10.1128/JVI.01318-09

PubMed ID

  • 19740981

Additional Document Info

start page

  • 11502

end page

  • 11513

volume

  • 83

number

  • 22