Large-molecular-weight precursors of sindbis virus proteins.
Infection of chicken embryo fibroblasts with a temperature-sensitive mutant of Sindbis virus at the nonpermissive temperature leads to the accumulation of a large-molecular-weight protein. We have shown that this protein contains (14)C-arginine tryptic peptides present in the three virion proteins. We have also found that a slightly smaller protein which is detected in Sindbis-infected BHK cells contains the (14)C-arginine tryptic peptides of the two envelope proteins but not those of the capsid protein. Pulse-chase experiments indicate that the Sindbis virus protein in BHK cells is cleaved to the envelope proteins.
D000818:Animals; D001120:Arginine / Q000378:metabolism; D001345:Autoradiography; D002247:Carbon Isotopes; D002460:Cell Line; D002642:Chick Embryo; D002854:Chromatography, Paper; D006224:Cricetinae; D046508:Culture Techniques; D004590:Electrophoresis, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts; D007668:Kidney; D008970:Molecular Weight; D009154:Mutation; D010455:Peptides / Q000032:analysis; D011498:Protein Precursors / Q000032:analysis* / Q000096:biosynthesis; D012845:Sindbis Virus / Q000032:analysis* / Q000254:growth & development / Q000378:metabolism; D013696:Temperature; D014357:Trypsin; D014764:Viral Proteins / Q000032:analysis* / Q000096:biosynthesis
D002247:Carbon Isotopes; D010455:Peptides; D011498:Protein Precursors; D014764:Viral Proteins; D001120:Arginine; D014357:Trypsin