Structural and Intracellular Proteins of the Nonoccluded Baculovirus HZ-1

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Abstract
A plaque-purified isolate of the baculovirus HZ-1 was used to examine the kinetics of replication of this persistent, nonoccluded virus in [Trichoplusia ni] TN-368 cells. Twenty-eight virus structural proteins ranging in MW from 13,000 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 [35S]methionine. N-[3H]acetylglucosamine, [3H]mannose and the glycosylation inhibitor tunicamycin were used to detect virus structural glycoproteins. Post-transcriptional modification of 2 virus-induced proteins was detected.