Glycosylation of influenza virus proteins in the presence of fluoroglucose occurs via a different pathway.

In the presence of fluoroglucose, an inhibitor of formation of mannosylphosphoryl and glucosylphosphoryl-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 dolichol-linked intermediates. However, they were smaller than the normal high-mannose oligosaccharides and, furthermore, resistant towards digestion with endo-beta-N-acetylglucosaminidase H. By excluding mannosylphosphoryl-dolichol, similar dolichyl-pyrophosphate-liked intermediates were synthesized in vitro by membranes from fluoroglucose-treated cells and they were shown to glycosylate protein.