Poliovirus RNA synthesis in vitro: structural elements and antibody inhibition.
The poliovirus RNA polymerase complex has been analyzed by immunoautoradiography using antibody probes derived from purified replicase (P3) region viral polypeptides. Antibody preparations made against the polio RNA polymerase, P3-4b, detected a previously unreported cellular protein that copurifies with the RNA polymerase. An IgG fraction purified from rabbit antiserum to polypeptide P3-2, a precursor of the RNA polymerase, specifically inhibits poliovirus RNA synthesis in vitro. We have also immunoprecipitated a 60,000-dalton protein (P3-4a) with antiserum to protein P3-4b and have determined the precise genomic map position of this protein by automated Edman degradation. Protein P3-4a originates by cleavage of the RNA polymerase precursor at a glutamine-glycine amino acid pair not previously reported to be a viral cleavage site.
D000936:Antigen-Antibody Complex; D002712:Chlorides; D012321:DNA-Directed RNA Polymerases / Q000302:isolation & purification / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007106:Immune Sera; D017955:Poliovirus / Q000235:genetics*; D012367:RNA, Viral / Q000235:genetics*; D014158:Transcription, Genetic / Q000187:drug effects; D015032:Zinc / Q000494:pharmacology; D017967:Zinc Compounds
D000936:Antigen-Antibody Complex; D002712:Chlorides; D007106:Immune Sera; D012367:RNA, Viral; D017967:Zinc Compounds; C016837:zinc chloride; D012321:DNA-Directed RNA Polymerases; D015032:Zinc