Single amino acid substitutions in the HSV-1 helicase protein that confer resistance to the helicase-primase inhibitor BAY 57-1293 are associated with increased or decreased virus growth characteristics in tissue culture

Arch Virol. 2007;152(8):1489-500. doi: 10.1007/s00705-007-0964-7. Epub 2007 Apr 4.

Abstract

Two mutants (BAYr1 and BAYr2) that are 100-fold and >3000-fold resistant, respectively, to the helicase-primase inhibitor (HPI) BAY 57-1293 were derived from a plaque-pure parental strain, HSV-1 SC16 cl-2. BAYr1 has two substitutions in the HSV-1 helicase (UL5) protein (A4 to V; K356 to Q) and BAYr2 has one (G352 to R). It was shown reproducibly that BAYr1 grows to higher titres in tissue culture while BAYr2 grows more slowly than wild-type. Marker transfer experiments confirmed that K356Q and G352R are the drug-resistance mutations and that they are directly associated with differences in virus growth in tissue culture. When BAYr1 was tested in a murine infection model, this virus was shown to be fully pathogenic. We present evidence that single mutations close to a predicted functional domain of an essential HSV-1 replication enzyme (helicase) are associated with drug resistance and virus growth characteristics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution*
  • Animals
  • Antiviral Agents / pharmacology
  • Chlorocebus aethiops
  • DNA Helicases / antagonists & inhibitors
  • DNA Helicases / genetics*
  • DNA Primase / antagonists & inhibitors
  • DNA Primase / genetics*
  • Drug Resistance, Viral / genetics*
  • Enzyme Inhibitors / pharmacology
  • Female
  • Herpes Simplex / mortality
  • Herpes Simplex / physiopathology
  • Herpes Simplex / virology
  • Herpesvirus 1, Human / drug effects
  • Herpesvirus 1, Human / enzymology
  • Herpesvirus 1, Human / genetics
  • Herpesvirus 1, Human / growth & development*
  • Herpesvirus 1, Human / pathogenicity
  • Humans
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Pyridines / pharmacology
  • Sulfonamides
  • Thiazoles / pharmacology
  • Vero Cells
  • Viral Proteins / antagonists & inhibitors
  • Viral Proteins / genetics*
  • Virus Replication*

Substances

  • Antiviral Agents
  • Enzyme Inhibitors
  • Pyridines
  • Sulfonamides
  • Thiazoles
  • Viral Proteins
  • pritelivir
  • DNA Primase
  • helicase-primase, Human herpesvirus 1
  • DNA Helicases