Identification of the virus-specific proteins of respiratory syncytial virus temperature-sensitive mutants by immunoprecipitation.
The proteins of Long strain RSV and three temperature-sensitive (ts) mutants of the A2 strain were compared by pulse labeling virus-infected cells with [35S]methionine and [3H]glucosamine followed by analysis of the cell lysates by polyacrylamide gel electrophoresis. At the permissive temperature (30 degrees) proteins ranging in molecular weight from 24,000 to 50,000 (VP24, VP27, VP33, VP44) could be identified. Immunoprecipitation of viral lysates by immune rabbit serum demonstrated antigenic similarity with VP27, VP44, VP50, and VP67 in all ts mutants and Long strain RSV. [3H]Glucosamine labeling demonstrated glycoproteins of 90,000 (GP90) and 50,000 (GP50) in Long strain and GP90 in the ts mutants.
D000818:Animals; D000936:Antigen-Antibody Complex; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D007118:Immunoassay; D008114:Liver Neoplasms, Experimental; D008970:Molecular Weight; D009154:Mutation; D051381:Rats; D012136:Respiratory Syncytial Viruses / Q000235:genetics*; D013696:Temperature; D014764:Viral Proteins / Q000235:genetics / Q000302:isolation & purification*
D000936:Antigen-Antibody Complex; D014764:Viral Proteins