Protein synthesis in cells infected with bovine rotavirus.
Bovine rotavirus was found to multiply efficiently in LLC-MK2 cells, a continuous line of rhesus monkey kidney, with a growth cycle which was essentially completed within 9 h after infection. The presence of low concentrations of trypsin (10 microgram/ml) in the virus inoculum was essential for infectivity. Polyacrylamide gel electrophoresis of infected cell extracts demonstrated the synthesis of at least eight virus-specific polypeptides 6 h post-infection with mol. wt. ranging from 102 X 10(3) to 29 X 10(3). Six polypeptides (about p102K, p91K, p84K, p37K and p34K) were identified as structural components of the virion. Two other polypeptides (54K and p29K) were identified as non-structural components. The synthesis of non-structural polypeptides appeared to precede that of the structural proteins. Pulse-chase experiments showed only one minor post-translation modification of the virus-specified proteins, namely an increase in the mobility of the 29K polypeptide.
D000818:Animals; D002417:Cattle; D002460:Cell Line; D003609:Dactinomycin / Q000494:pharmacology; D008253:Macaca mulatta; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D014176:Protein Biosynthesis; D012087:Reoviridae / Q000378:metabolism*; D012401:Rotavirus / Q000254:growth & development / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis*
D014764:Viral Proteins; D003609:Dactinomycin