Herpes Simplex Virus Mutants with Multiple Substitutions Affecting DNA Binding of UL42 Are Impaired for Viral Replication and DNA Synthesis
Author:
Affiliation:
1. Department of Microbiology and Immunology, State University of New York Upstate Medical University, Syracuse, New York 13210
2. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115
Abstract
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JVI.01133-07
Reference15 articles.
1. Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42
2. Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template
3. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity
4. Hingorani, M. M., and M. Donnell. 2000. Sliding clamps: a (tail)ored fit. Curr. Biol.10:R25-R29.
5. Mutations That Decrease DNA Binding of the Processivity Factor of the Herpes Simplex Virus DNA Polymerase Reduce Viral Yield, Alter the Kinetics of Viral DNA Replication, and Decrease the Fidelity of DNA Replication
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