Inhibition of equine herpesvirus type 1 subtype 1-induced ribonucleotide reductase by the nonapeptide YAGAVVNDL.
The synthetic nonapeptide YAGAVVNDL [identical to the nine carboxy-terminal amino acids of the small subunit of herpes simplex virus (HSV)-encoded ribonucleotide reductase (RR)] was found to inhibit the RR activity induced by equine herpesvirus type 1 subtype 1 (EHV-1). Parallel experiments with HSV type 1 (HSV-1)-encoded RR established that the concentration of peptide required to inhibit 50% of the RR activity was 28 microM for both enzymes. The optimum pH for the EHV-1 enzyme was found to be between 8.0 and 8.1 which is the same as that of HSV-1 RR. By use of antisera made against peptides corresponding to different regions of the large subunit (RR1) of the HSV-1 enzyme and monoclonal antibodies directed against HSV-1 RR1 we have obtained evidence which suggests that the EHV-1 large subunit has an Mr of approximately 90,000 and lacks the N-terminal domain which is so far unique to HSV.
Telford
E
E
MRC Virology Unit, Institute of Virology, Glasgow, U.K.
Lankinen
H
H
Marsden
H
H
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D006564:Herpesviridae / Q000201:enzymology*; D004861:Herpesvirus 1, Equid / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000494:pharmacology*; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors* / Q000276:immunology; D018139:Simplexvirus / Q000201:enzymology
D000911:Antibodies, Monoclonal; D009842:Oligopeptides; D012264:Ribonucleotide Reductases