Resistance to antiviral inhibitors caused by the mutation S889A in the highly-conserved 885-GDTDS motif of the herpes simplex virus type 1 DNA polymerase

Virology. 1993 Aug;195(2):831-5. doi: 10.1006/viro.1993.1439.


Most point substitutions in the highly-conserved 885-GDTDS motif of the HSV-1 DNA polymerase inactivate polymerase elongation activity. However, in an assay system based on expression by in vitro transcription-translation, the mutant GDTDA (S889A) possessed wild-type elongation activity which was highly resistant to phosphonoacetic acid and acyclovir triphosphate, but retained sensitivity to aphidicolin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antiviral Agents / pharmacology*
  • Base Sequence
  • Cloning, Molecular
  • Conserved Sequence*
  • DNA, Viral
  • DNA-Directed DNA Polymerase / genetics*
  • DNA-Directed DNA Polymerase / metabolism
  • Drug Resistance, Microbial / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Exodeoxyribonucleases / genetics*
  • Exodeoxyribonucleases / metabolism
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Point Mutation
  • Viral Proteins*


  • Antiviral Agents
  • DNA, Viral
  • Viral Proteins
  • DNA-Directed DNA Polymerase
  • Exodeoxyribonucleases
  • DNA polymerase, Simplexvirus