Identification of viral polypeptides involved in pseudorabies virus ribonucleotide reductase activity.
AUTOR(ES)
Cohen, E A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=254217Documentos Relacionados
- Immunological characterization of herpes simplex virus type 1 and 2 polypeptide(s) involved in viral ribonucleotide reductase activity.
- Vaccinia virus-induced ribonucleotide reductase can be distinguished from host cell activity.
- Requirement of ribonucleotide reductase for cobamide coenzyme, a product of ribosomal activity.
- Chromosome-mediated gene transfer of hydroxyurea resistance and amplification of ribonucleotide reductase activity.
- Induction of a new ribonucleotide reductase after infection of mouse L cells with pseudorabies virus.