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.