Protein synthesis in Sendai virus-infected cells.
The rate of protein synthesis in chicken embryo cells infected with Sendai virus 18 to 20 h previously was about two times greater than in mock-infected controls. At this time of infection six stable virus-induced proteins, four major structural proteins (P, NH, NP and M) and two non-structural proteins (28K and 61K), were identified by electrophoresis in SDS-polyacrylamide gel of total cell extracts. The structural glycopeptide F was not detected in the infected cell extracts. Pulse-chase experiments showed that PN NP, M and 28K proteins either did not undergo any post-translational processing or the processing occurred very rapidly. By contrast, a glycopeptide NH was apparently derived from one of two unstable precursons, 69K or 63K, which were revealed only after a short pulse. The synthesis of virus-specific proteins appeared to be regulated since its rate varied for individual classes of proteins. In nucleocapsid-particles isolated from infected cells two major structural proteins (P and NP) were found. A minor component with a very large mol. wt. was revealed in these particles as well as in the virus particle.
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001345:Autoradiography; D002250:Carbon Radioisotopes; D002642:Chick Embryo; D046508:Culture Techniques; D004591:Electrophoresis, Polyacrylamide Gel; D006020:Glycopeptides / Q000096:biosynthesis; D008970:Molecular Weight; D010222:Parainfluenza Virus 1, Human / Q000254:growth & development* / Q000378:metabolism; D010452:Peptide Biosynthesis; D014176:Protein Biosynthesis; D014764:Viral Proteins / Q000096:biosynthesis*
D000596:Amino Acids; D002250:Carbon Radioisotopes; D006020:Glycopeptides; D014764:Viral Proteins