Biosynthesis of measles virus hemagglutinin in persistently infected cells.
The synthesis of the hemagglutinin (HA) glycoprotein of measles virus was investigated in a persistently infected cell line using a monoclonal anti-HA. The synthesis of the HA protein was shown to be associated with the rough endoplasmic reticulum. The unglycosylated (HA0) apoprotein is synthesized as a 65,000 dalton peptide and is inserted into the rough endoplasmic reticulum as a transmembrane protein with approximately 2 to 3000 daltons of the peptide exposed to the cytoplasmic membrane surface. Primary glycosylation of the HA protein was found to occur through the lipid-linked carrier, dolichol-phosphate, as determined by inhibition of glycosylation by tunicamycin. Glycosylation, however, was not a prerequisite for membrane insertion. Endo-beta-N-acetylglucosaminidase H digestion of the fully glycosylated HA protein indicated that both simple and complex oligosaccharides are present on the surface glycoprotein.
D000911:Antibodies, Monoclonal / Q000276:immunology; D000914:Antibodies, Viral / Q000276:immunology; D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis; D010450:Endopeptidases; D004721:Endoplasmic Reticulum / Q000032:analysis; D006389:Hemagglutinins, Viral / Q000032:analysis / Q000096:biosynthesis*; D006801:Humans; D008297:Male; D008459:Measles virus / Q000032:analysis*; D009844:Oligosaccharides / Q000032:analysis; D011467:Prostate; D012697:Serine Endopeptidases; D014415:Tunicamycin; D014764:Viral Proteins / Q000032:analysis
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D006389:Hemagglutinins, Viral; D009844:Oligosaccharides; D014764:Viral Proteins; D014415:Tunicamycin; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase