Maturation of measles virus hemagglutinin glycoprotein

Abstract

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.