Neutralization of herpes simplex virus ribonucleotide reductase activity by an oligopeptide-induced antiserum directed against subunit H2.
Herpes simplex virus type 1 ribonucleotide reductase is associated with two polypeptides of apparent molecular weights 136,000 and 38,000. The two polypeptides form a tight complex and, therefore, are often coprecipitated by monoclonal antibodies. We report here that immunoglobulins G purified from polyclonal rabbit antisera (P9) raised against a nonapeptide corresponding to the carboxy terminus of the 38,000-dalton polypeptide specifically neutralize the herpes simplex virus ribonucleotide reductase activity. We suggest that the P9 immunoglobulin G neutralizes the reductase activity by impairing the association of the two subunits (H1 and H2) of the enzyme.
D000937:Antigen-Antibody Reactions; D000939:Epitopes; D046911:Macromolecular Substances; D008970:Molecular Weight; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors / Q000276:immunology*; D018139:Simplexvirus / Q000201:enzymology*
D000939:Epitopes; D046911:Macromolecular Substances; D012264:Ribonucleotide Reductases