Open AccessHerpes Simplex Virus Mutants with Multiple Substitutions Affecting DNA Binding of UL42 Are Impaired for Viral Replication and DNA Synthesis
Author(s) -
Changying Jiang,
Ying T. Hwang,
Guangliang Wang,
John C.W. Randell,
Donald M. Coen,
Charles B. C. Hwang
Publication year - 2007
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01133-07
Subject(s) - biology , processivity , dna polymerase , single stranded binding protein , dna polymerase ii , replication factor c , dna replication , virology , dna clamp , dna , dna polymerase delta , replication protein a , viral replication , polymerase , microbiology and biotechnology , herpes simplex virus , control of chromosome duplication , genetics , dna binding protein , virus , gene , rna , reverse transcriptase , transcription factor
Herpes simplex virus mutants with single substitutions that decrease DNA binding by the DNA polymerase processivity subunit UL42 are only modestly impaired for viral replication. In this study, recombinant viruses harboring two or four of these mutations were constructed. The more substitutions, the more severe the defects in viral replication and DNA synthesis, suggesting that DNA binding by UL42 is important for these processes.