
Glycosylation of Influenza Virus Proteins in the Presence of Fluoroglucose Occurs via a Different Pathway
Author(s) -
DATEMA Roelf,
SCHWARZ Ralph T.,
WINKLER Juliana
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04875.x
Subject(s) - dolichol , glycoprotein , glycosylation , biochemistry , mannose , chemistry , in vitro , oligosaccharide , pyrophosphate , enzyme , biosynthesis
In the presence of fluoroglucose, an inhibitor of formation of mannosylphosphoryl and glucosyl‐phosphoryl‐dolichol, lipid‐dependent glycosylation of influenza virus glycoproteins is strongly, but not completely inhibited. The oligosaccharides that were transferred to protein in the presence of fluoroglucose came directly from dolichol‐linked intermediates. However, they were smaller than the normal high‐mannose oligosaccharides and, furthermore, resistant towards digestion with endo‐β‐ N ‐acetylglucosaminidase H. By excluding mannosylphosphoryl‐dolichol, similar dolichyl‐pyrophosphate‐linked intermediates were synthesized in vitro by membranes from fluoroglucose‐treated cells and they were shown to glycosylate protein.