Infected cell-specific polypeptides (ICSP) in nuclear polyhedrosis virus (MNPV)-infected cells could be radiolabelled with various sugar precursors including mannose, -acetyl glucosamine, -acetyl mannosamine and glucose. Glycosylation occurred mainly late in infection. Eleven polypeptides were glycosylated including the major envelope protein, the polyhedron protein (very late in infection) and a major low molecular weight non-structural polypeptide (also very late in infection). Tunicamycin inhibited MNPV replication and prevented the addition of -acetyl glucosamine and, to a lesser extent, mannose to the appropriate proteins. This had the effect of enhancing the migration in SDS-polyacrylamide gels of some glycopolypeptides but not that of the polyhedron protein. Tunicamycin prevented the envelopment of nucleocapsids both within the nucleus and at the plasma membrane. Polyhedron formation did, however, occur in the presence of tunicamycin.


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