Uncoating of parental bluetongue virus to core and subcore particles in infected L cells.

A study was made of the fate of parental bluetongue virus (BTV) in infected cells. Within the first hour after infection, the BTV particles are converted to core particles with the loss of major capsid polypeptides P2 and P5. The particles are able to synthesize mRNA in vitro in a transcription reaction characterized by a temperature-dependent inhibition at high core concentrations. From about 6 hr after infection a second uncoating event is observed in which the 470 S core particles are converted to 390 S subcore particles. These particles are morphologically strikingly different from core particles and have a skeletonlike structure with a hexagonal profile and a side to side diameter of 40 nm. These subcore particles contain only one major structural protein, P3, and three minor proteins, P1, P4, and P6. They do, however, contain all 10 double-stranded RNA segments. The results suggest that the characteristic capsomeres on the surface of core particles are composed mainly of P7, the soluble group-specific antigen of BTV. The subcore particles are stable only at very low salt concentrations. Under these conditions no transcriptase activity can be demonstrated.