Epstein-Barr virus-specific DNA polymerase in virus-nonproducer Raji cells

J Virol. 1986 May;58(2):671-5. doi: 10.1128/JVI.58.2.671-675.1986.


Virus-nonproducer Raji cells, when induced to early antigen synthesis by 12-O-tetradecanoyl-phorbol-13-acetate and sodium butyrate, showed an increase in DNA polymerase activity. This enzyme has the characteristics of a typical Epstein-Barr virus DNA polymerase with regard to chromatographical pattern and biological properties: it is eluted from DEAE-cellulose at 0.08 M NaCl, has a high salt resistance, is sensitive to phosphonoacetic acid and phosphonoformate, and shows a substrate preference for poly(dC)-oligo(dG12-18). The resistance of Epstein-Barr virus polymerase activity to aphidicolin is a property distinct from that of HSV DNA polymerase. Viral DNA polymerase activity increases in the absence of Epstein-Barr virus DNA replication, indicating that this enzyme is an early viral protein.

MeSH terms

  • Antigens, Viral
  • Aphidicolin
  • Butyrates / pharmacology
  • Butyric Acid
  • Cell Line
  • DNA Replication
  • DNA-Directed DNA Polymerase / biosynthesis*
  • DNA-Directed DNA Polymerase / metabolism
  • Diterpenes / pharmacology
  • Enzyme Induction
  • Foscarnet
  • Herpesvirus 4, Human / enzymology*
  • Herpesvirus 4, Human / immunology
  • Herpesvirus 4, Human / physiology
  • Humans
  • Phosphonoacetic Acid / analogs & derivatives
  • Phosphonoacetic Acid / pharmacology
  • Substrate Specificity
  • Tetradecanoylphorbol Acetate / pharmacology
  • Virus Replication


  • Antigens, Viral
  • Butyrates
  • Diterpenes
  • Epstein-Barr virus early antigen
  • Butyric Acid
  • Foscarnet
  • Aphidicolin
  • DNA-Directed DNA Polymerase
  • Phosphonoacetic Acid
  • Tetradecanoylphorbol Acetate