In vitro mutagenesis of the herpes simplex virus type 1 DNA polymerase gene results in altered drug sensitivity of the enzyme
Autor: | M L Haffey, James Thomas Matthews, R D Carroll, J T Stevens |
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Rok vydání: | 1989 |
Předmět: |
Aphidicolin
Phosphonoacetic Acid Genes Viral DNA polymerase viruses Immunology Genetic Vectors Molecular Sequence Data DNA-Directed DNA Polymerase Saccharomyces cerevisiae medicine.disease_cause Microbiology Antiviral Agents Virus chemistry.chemical_compound Mutant protein Virology medicine Serine Humans Simplexvirus Amino Acid Sequence Nucleic Acid Synthesis Inhibitors chemistry.chemical_classification Viral Structural Proteins Mutation biology Base Sequence Mutagenesis Molecular biology Kinetics Herpes simplex virus Enzyme chemistry Insect Science biology.protein Asparagine Diterpenes Oligonucleotide Probes Foscarnet HeLa Cells Research Article |
Zdroj: | Journal of virology. 63(11) |
ISSN: | 0022-538X |
Popis: | A mutation (asparagine 815 to serine 815) was introduced into the herpes simplex virus type 1 (HSV-1) DNA polymerase (pol). The HSV-1 pol enzyme in lysates of Saccharomyces cerevisiae cells expressing the mutant protein showed increased resistance to acyclovir triphosphate and increased sensitivity to phosphonoacetate but was not substantially altered with respect to sensitivity to phosphonoformate or aphidicolin. These results directly demonstrate that both resistance to acyclovir triphosphate and sensitivity to phosphonoacetate can be conferred by this mutation in the absence of other viral factors and that the yeast expression system can be used for structure-function studies on HSV-1 pol. |
Databáze: | OpenAIRE |
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