Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an S-phase-like cellular environment

J Biol Chem. 2005 Mar 4;280(9):8156-63. doi: 10.1074/jbc.M411405200. Epub 2004 Dec 15.

Abstract

When exposed to genotoxic stress, eukaryotic cells demonstrate a DNA damage response with delay or arrest of cell-cycle progression, providing time for DNA repair. Induction of the Epstein-Barr virus (EBV) lytic program elicited a cellular DNA damage response, with activation of the ataxia telangiectasia-mutated (ATM) signal transduction pathway. Activation of the ATM-Rad3-related (ATR) replication checkpoint pathway, in contrast, was minimal. The DNA damage sensor Mre11-Rad50-Nbs1 (MRN) complex and phosphorylated ATM were recruited and retained in viral replication compartments, recognizing newly synthesized viral DNAs as abnormal DNA structures. Phosphorylated p53 also became concentrated in replication compartments and physically interacted with viral BZLF1 protein. Despite the activation of ATM checkpoint signaling, p53-downstream signaling was blocked, with rather high S-phase CDK activity associated with progression of lytic infection. Therefore, although host cells activate ATM checkpoint signaling with response to the lytic viral DNA synthesis, the virus can skillfully evade this host checkpoint security system and actively promote an S-phase-like environment advantageous for viral lytic replication.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ataxia Telangiectasia Mutated Proteins
  • Bromodeoxyuridine / pharmacology
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Cell Line, Tumor
  • DNA Damage
  • DNA-Binding Proteins / metabolism*
  • Herpesvirus 4, Human / metabolism*
  • Humans
  • Immunoblotting
  • Immunoprecipitation
  • In Situ Hybridization, Fluorescence
  • MRE11 Homologue Protein
  • Microscopy, Fluorescence
  • Nuclear Proteins / metabolism
  • Phosphorylation
  • Protein Binding
  • Protein Kinases / metabolism
  • Protein Serine-Threonine Kinases / metabolism*
  • S Phase
  • Serine / chemistry
  • Signal Transduction
  • Time Factors
  • Tumor Suppressor Protein p53 / metabolism
  • Tumor Suppressor Proteins / metabolism*

Substances

  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • MRE11 protein, human
  • NBN protein, human
  • Nuclear Proteins
  • Tumor Suppressor Protein p53
  • Tumor Suppressor Proteins
  • Serine
  • Protein Kinases
  • ATM protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • Protein Serine-Threonine Kinases
  • MRE11 Homologue Protein
  • Bromodeoxyuridine