title: Investigation of the specificity of the herpes simplex virus type 1 protease by point mutagenesis of the autoproteolysis sites.
abstract: The herpes simplex virus type 1 (HSV-1) protease is cleaved at two autoprocessing sites during viral maturation, one of which shares amino acid identity with its substrate, ICP35. Similar autoprocessing sites have been observed within other members of the Herpesviridae. Introduction of point mutations within the autoprocessing sites of the HSV-1 protease indicated that specificity resides within the P4-P1' region of the cleavage sites.
authors.affiliation: Virology Department, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey 08543-4000.
authors.forename: P J
authors.initials: PJ
authors.lastname: McCann
authors.forename: D R
authors.initials: DR
authors.lastname: O'Boyle
authors.forename: I C
authors.initials: IC
authors.lastname: Deckman
mesh_terms: D000595:Amino Acid Sequence; D004252:DNA Mutational Analysis; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D018259:Herpesvirus 1, Human / Q000201:enzymology*; D008969:Molecular Sequence Data; D017354:Point Mutation; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014764:Viral Proteins / Q000378:metabolism
chemical_list: C054582:ICP35 protein, Human herpesvirus 1; D014764:Viral Proteins; C079287:scaffold protein, Herpes simplex virus-1; D010450:Endopeptidases