Posttranslational modification and intracellular transport of mumps virus glycoproteins.

Analysis of the pronase-derived glycopeptides of isolated mumps virus glycoproteins revealed the presence of both complex and high-mannose-type oligosaccharides on the HN and F1 glycoproteins, whereas only high-mannose-type glycopeptides were detected on F2. Endoglycosidase F, a newly described glycosidase that cleaves N-linked high mannose as well as complex oligosaccharides, appeared to completely cleave the oligosaccharides linked to HN and F2, whereas F1 was resistant to the enzyme. Two distinct cleavage products of F2 were observed, suggesting the presence of two oligosaccharide side chains. Tunicamycin was found to reduce the infectious virus yield and inhibit mumps virus particle formation. The two glycoproteins, HN and F, were not found in the presence of the glycosylation inhibitor. However, two new polypeptides were detected, with molecular weights of 63,000 (HNT) and 53,000 (FT), respectively, which may represent nonglycosylated forms of the glycoproteins. Synthesis of the nonglycosylated virus-coded proteins (L, NP, P, M, pI, and pII) was not affected by tunicamycin. The formation of HN oligomers and the proteolytic cleavage of the F protein were found to occur with the same kinetics. Analysis of the time course of appearance of mumps virus glycoproteins on the cell surface suggested that dimerization of HN and cleavage of F occur immediately after their exposure on the plasma membrane.