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Updated: Oct 11, 2025

Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
Herpesvirus DNA polymerase: Structures, functions, and mechanisms.
Donald M Coen1, Jessica L Lawler1, Jonathan Abraham2
1Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, United States.
Herpes simplex virus DNA polymerase, a key enzyme for viral replication, has two subunits crucial for its function. Understanding this enzyme is vital for developing new antiviral drugs against herpesviruses.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Herpesviruses are DNA viruses causing various diseases.
- Their replication involves a conserved two-subunit DNA polymerase, a target for antiviral drugs.
- This review focuses on herpes simplex virus (HSV) DNA polymerase.
Purpose of the Study:
- To review the structure, function, and mechanisms of HSV DNA polymerase.
- To highlight its role in viral replication and as an antiviral target.
- To discuss the contributions of its catalytic and accessory subunits.
Main Methods:
- Review of existing literature on HSV DNA polymerase structure and function.
- Analysis of functional information on the catalytic (Pol) and accessory subunits.
- Discussion of genetic and pharmacologic tools used to study the enzyme.
Main Results:
- HSV DNA polymerase has a catalytic subunit (Pol) with polymerization and exonuclease activities.
- The accessory subunit resembles sliding clamps and interacts with Pol and DNA.
- Both subunits influence replication fidelity.
- Antiviral inhibitors are most effective against HSV and human cytomegalovirus (HCMV) polymerases.
Conclusions:
- HSV DNA polymerase structure and function are well-studied but still present research questions.
- The enzyme remains an attractive target for novel antiviral drug discovery.
- Further research is needed to fully elucidate all its functions and interactions.
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