title: Poliovirus RNA synthesis in vitro: structural elements and antibody inhibition.
abstract: 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.
mesh_terms: 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
chemical_list: 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