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Characteristics of herpesvirus mutants resistant to phosphonoformate and phosphonoacetate

Insights

Herpes simplex virus type 1 mutants resistant to phosphonoformate (PFA) and phosphonoacetate (PAA) show cross-resistance, indicating a shared interaction site. Viral DNA polymerase from these mutants is also cross-resistant to PFA and PAA.

Area of Science:

  • Virology
  • Molecular Biology
  • Antiviral Drug Development

Background:

  • Herpes simplex virus type 1 (HSV-1) is a significant human pathogen.
  • Antiviral drugs like phosphonoformate (PFA) and phosphonoacetate (PAA) are used to treat HSV-1 infections.
  • Understanding drug resistance mechanisms is crucial for developing effective antiviral therapies.

Purpose of the Study:

  • To investigate the resistance mechanisms of HSV-1 to PFA and PAA.
  • To characterize the cross-resistance patterns between PFA and PAA in HSV-1 mutants.
  • To examine the properties of viral DNA polymerase in drug-resistant HSV-1 strains.

Main Methods:

  • Selection of PFA-resistant (HSV-PFA(r)) and PAA-resistant (HSV-PAA(r)) HSV-1 mutants in cell culture.
  • Phenotypic characterization of drug resistance in the selected mutants.
  • Isolation and characterization of deoxyribonucleic acid polymerases from infected cells.
  • Assessment of enzyme susceptibility to PFA, PAA, vidarabine triphosphate, and pyrophosphate.

Main Results:

  • HSV-PFA(r) and HSV-PAA(r) mutants exhibited reciprocal cross-resistance to PFA and PAA, suggesting a common binding site.
  • The PFA-resistant mutant showed decreased susceptibility to vidarabine but not idoxuridine.
  • Viral DNA polymerases from both mutants were cross-resistant to PFA and PAA inhibition.
  • Enzymes from resistant mutants had reduced susceptibility to pyrophosphate inhibition.

Conclusions:

  • PFA and PAA likely target the same site in HSV-1.
  • Drug resistance in HSV-1 can involve alterations in viral DNA polymerase.
  • These findings provide insights into antiviral drug resistance mechanisms for HSV-1.

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