Identification of viral polypeptides involved in pseudorabies virus ribonucleotide reductase activity.
We studied pseudorabies virus-induced ribonucleotide reductase and found that it exhibited biochemical properties very similar to those of herpes simplex virus reductase. A polyclonal rabbit antiserum (P9) directed against the carboxy terminus of subunit H2 polypeptide (38,000 daltons) of herpes simplex virus reductase neutralized the pseudorabies virus reductase, as well as the herpes simplex virus isozyme. This serum recognized two pseudorabies virus-specified polypeptides of 34,000 and 110,000 daltons, which may represent the two subunits of the enzyme. Furthermore, as already shown for herpes simplex virus reductase (E. A. Cohen, P. Gaudreau, P. Brazeau, and Y. Langelier, Nature [London] 321:441-443, 1986), we show that the nonapeptide itself specifically inhibited pseudorabies reductase activity.
D011558:Herpesvirus 1, Suid / Q000201:enzymology*; D007527:Isoenzymes / Q000276:immunology / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D012264:Ribonucleotide Reductases / Q000276:immunology / Q000378:metabolism*; D018139:Simplexvirus / Q000201:enzymology / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology / Q000378:metabolism*
D007527:Isoenzymes; D010455:Peptides; D014764:Viral Proteins; D012264:Ribonucleotide Reductases