Structural and Intracellular Proteins of the Nonoccluded Baculovirus HZ-1

Abstract

A plaque-purified isolate of the baculovirus HZ-1 was used to examine the kinetics of replication of this persistent, nonoccluded virus in TN-368 cells. Twenty-eight virus structural proteins ranging in molecular weight from 153,000 to 14,000 were identified. Fourteen of these proteins were found to be glycosylated. The sequence of appearance of the 37 virus-induced intracellular polypeptides was determined by pulse-labeling with [ 35 S]methionine. N -[ 3 H]acetylglucosamine, [ 3 H]mannose, and the glycosylation inhibitor tunicamycin were used to detect virus structural glycoproteins. Post-transcriptional modification of two virus-induced proteins was detected.