Maturation of measles virus hemagglutinin glycoprotein.
The processing of measles virus hemagglutinin glycoprotein (H) in infected cells was studied by pulse-chase method and two-dimensional isoelectric focusing and SDS-polyacrylamide slab gel electrophoresis. H glycoprotein was synthesized initially as polypeptides smaller than H glycoprotein present in the virions. They were then processed into a cohort of polypeptides of larger molecular size and with reduced charge. The change was associated with the expression of H glycoprotein on the cell surface. The removal of sialic acid from carbohydrate chain of H glycoprotein resulted in the shift of isoelectric point to a more basic range. The entire process of maturation of H glycoprotein required approximately 5 hours. Carbohydrate content in H was determined to be approximately 12 per cent by weight. Mannose, galactose, fucose, N-acetylglucosamine, and N-acetylneuraminic acid were the constituent monosaccharides.
D050260:Carbohydrate Metabolism; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000096:biosynthesis*; D006389:Hemagglutinins, Viral / Q000096:biosynthesis*; D006801:Humans; D007525:Isoelectric Focusing; D008459:Measles virus / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D011499:Protein Processing, Post-Translational
D006023:Glycoproteins; D006389:Hemagglutinins, Viral; D008565:Membrane Proteins