The protease and gag gene products of the human immunodeficiency virus: authentic cleavage and post-translational modification in an insect cell expression system.

Three recombinant baculoviruses which are capable of expressing human immunodeficiency virus (HIV) protease, p55gag, and both products simultaneously in insect cell culture have been constructed. Upon co-infection of cells with the protease and p55gag-expressing viruses, authentic processing of the gag precursor is observed to take place. This processing could be reproduced in vitro using mixtures of cellular lysates containing the expressed proteins. When expressed alone, uncleaved p55gag precursor appears to form retroviral core-like particles within the cytoplasm of infected cells. Metabolic labeling studies of the baculovirus-expressed gag products have demonstrated that p17 is myristylated at its amino terminus, and that p24 is phosphorylated. In these respects, the insect cell system is evidently capable of carrying out post-translational processing resembling that which occurs in authentic HIV-1 replication.