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Herpes simplex virus DNA polymerase as the site of phosphonoacetate sensitivity: temperature-sensitive mutants

Journal of Virology
|November 1, 1977
PubMed

Insights

Herpes simplex virus type 1 (HSV-1) DNA polymerase mutations affect phosphonoacetate (PAA) sensitivity. This study links temperature-sensitive lesions to PAA resistance, suggesting both are in the viral DNA polymerase gene.

Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • Herpes simplex virus type 1 (HSV-1) temperature-sensitive (ts) mutants often show impaired DNA polymerase induction.
  • Phosphonoacetate (PAA) is a known inhibitor of HSV replication and DNA polymerase activity.

Purpose of the Study:

  • To investigate the relationship between temperature-sensitive mutations in HSV-1 and sensitivity to phosphonoacetate (PAA).
  • To determine if PAA sensitivity is linked to specific genetic loci, potentially including the viral DNA polymerase gene.

Main Methods:

  • Testing 22 HSV-1 ts mutants across 15 complementation groups for PAA sensitivity.
  • Isolating and characterizing additional PAA-resistant (Pr) mutants.
  • Utilizing three-factor recombination analysis with double mutants (ts Pr phenotype) to map the PAA locus.
  • Correlating in vivo PAA sensitivity with in vitro DNA polymerase activity.

Main Results:

  • One mutant, tsD9, exhibited PAA resistance (Pr), while others were sensitive.
  • Revertants of tsD9 to ts+ also lost PAA resistance.
  • Three-factor recombination mapped the PAA locus to the same position as the ts lesion in tsD9.
  • In vivo PAA sensitivity directly correlated with in vitro DNA polymerase sensitivity.

Conclusions:

  • The temperature-sensitive lesion in tsD9 and the determinant for PAA sensitivity are likely located within the structural gene for HSV-1 DNA polymerase.
  • PAA resistance can serve as a marker for mutations within the HSV-1 DNA polymerase gene.

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