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Related Experiment Videos

Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce

Changying Jiang1, Ying T Hwang, John C W Randell

  • 1Department of Microbiology and Immunology, State University of New York, Upstate Medical University, 750 E. Adams St., Syracuse, NY 13210, USA.

Journal of Virology
|January 19, 2007
PubMed
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Altering herpes simplex virus DNA polymerase subunit UL42 affects viral replication and fidelity. Reduced DNA binding in UL42 mutants impacts progeny production and DNA synthesis, increasing mutation rates.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • The herpes simplex virus (HSV) DNA polymerase processivity subunit, UL42, is crucial for viral replication.
  • UL42 exhibits both polymerase and DNA-binding activities, with specific arginine residues on its surface implicated in DNA binding.
  • Previous research indicated that mutations in these arginine residues reduce DNA binding affinity and the polymerase's ability to synthesize long DNA chains.

Purpose of the Study:

  • To investigate the impact of specific UL42 arginine residue substitutions on viral progeny production, viral DNA replication, and DNA replication fidelity.
  • To elucidate the functional consequences of reduced DNA binding by the UL42 protein in the context of HSV infection.

Main Methods:

  • Construction and characterization of mutant HSV-1 viruses with alanine substitutions for key arginine residues in UL42.

Related Experiment Videos

  • Transient complementation assays to assess replication complementation of UL42 null mutants.
  • Transient DNA replication assays using plasmids with HSV-1 origin sequences.
  • Single-cycle growth assays to measure progeny virus production.
  • Real-time PCR to quantify viral DNA synthesis during different infection phases.
  • Mutation frequency analysis of a lacZ reporter gene within the viral genome.

    • Main Results:

    • All UL42 substitution mutants could complement UL42 null mutants and support plasmid DNA replication.
    • Mutant viruses produced significantly fewer progeny viruses compared to wild-type controls in single-cycle growth assays.
    • UL42 mutants showed reduced viral DNA synthesis during the early phase of infection but increased synthesis during the late phase.
    • A significant increase in mutation frequencies within the lacZ gene was observed in the substitution mutants.

    Conclusions:

    • Reduced DNA binding affinity of the UL42 protein is directly associated with impaired viral yields and altered viral DNA replication kinetics.
    • The processivity subunit UL42 plays a critical role in maintaining DNA replication fidelity during HSV infection in mammalian cells.
    • These findings highlight the influence of DNA processivity factors on the fidelity of viral DNA replication.