Epstein-Barr virus-encoded protein kinase BGLF4 mediates hyperphosphorylation of cellular elongation factor 1delta (EF-1delta): EF-1delta is universally modified by conserved protein kinases of herpesviruses in mammalian cells

J Gen Virol. 2001 Jun;82(Pt 6):1457-1463. doi: 10.1099/0022-1317-82-6-1457.

Abstract

Translation elongation factor 1delta (EF-1delta) is hyperphosphorylated in various mammalian cells infected with alpha-, beta- and gammaherpesviruses and EF-1delta modification is mediated by viral protein kinases, including UL13 of herpes simplex virus type 1 and UL97 of human cytomegalovirus. In this study, the following is reported. (i) BGLF4 encoded by the prototype gammaherpesvirus Epstein-Barr virus was purified as a fusion protein that was labelled with [gamma-(32)P]ATP and labelling was eliminated by phosphatase. (ii) The ratio of the hyperphosphorylated form of human EF-1delta was increased both in Sf9 cells after infection with baculoviruses expressing GST-BGLF4 fusion proteins and in COS-7 cells after transfection with a BGLF4 expression plasmid. These results indicate that purified BGLF4 possesses protein kinase activity and mediates EF-1delta hyperphosphorylation. These data also support the hypothesis that the protein kinases that are conserved by herpesviruses universally mediate EF-1delta modification in mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Baculoviridae
  • Blotting, Western
  • COS Cells
  • Cell Line
  • Herpesvirus 4, Human / enzymology*
  • Herpesvirus 4, Human / genetics
  • Humans
  • Peptide Elongation Factor 1 / metabolism*
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / isolation & purification
  • Protein Serine-Threonine Kinases / metabolism*
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Spodoptera
  • Transfection
  • Viral Proteins*

Substances

  • Peptide Elongation Factor 1
  • Recombinant Fusion Proteins
  • Viral Proteins
  • Adenosine Triphosphate
  • BGLF4 protein, Epstein-Barr virus
  • Protein Serine-Threonine Kinases
  • Phosphoric Monoester Hydrolases