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.
D004286:Dolichols / Q000378:metabolism; D005947:Glucose / Q000031:analogs & derivatives* / Q000494:pharmacology; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000096:biosynthesis*; D006155:Guanosine Diphosphate Mannose / Q000378:metabolism; D007700:Kinetics; D009975:Orthomyxoviridae / Q000187:drug effects / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis*
D004286:Dolichols; D006020:Glycopeptides; D006023:Glycoproteins; D014764:Viral Proteins; D006155:Guanosine Diphosphate Mannose; D005947:Glucose