PMID: 639813Apr 1, 1978Paper

Glycosylation in vitro of Semliki-Forest-virus and influenza-virus glycoproteins and its suppression by nucleotide-2-deoxy-hexose

European Journal of Biochemistry
R T SchwarzL Lehle

Abstract

Cell-free enzyme preparations from cultured fibroblasts infected with Semliki forest virus or fowl plague virus (an influenza A virus) incorporate [14C]-mannose into dolichol-phosphate-mannose, lipid-linked oligosaccharides and into endogenous virus-specific glycoproteins. When GDP-2-deoxy-D-[14C]glucose serves as substrate 2-deoxy-D-[14C]glucose is transferred to dolichol phosphate yielding dolichol-monophosphate-2-deoxy-D-[14C]glucose. UDP-2-deoxy-D-[14C]glucose gives rise also to a lipid which, however, is not a polyprenol derivative. The transfer of [14C]mannose to lipid-extractable fractions and glycoproteins in vitro is blocked by GDP-2-deoxy-D-glucose. It can be restored by exogenous dolichol monophosphate only with regard to the formation of dolichol-monophosphate-[14C]mannose-labelled oligosaccharides into glycoproteins. UDP-2-deoxy-D-glucose has no inhibitory effect on transfer reactions of [14C]mannose from GDP-[14C]mannose into various lipid fractions or into glycoprotein. It is concluded therefore, that the inhibition of glycosylation brought about by 2-deoxyglucose in vivo is caused by an interference of its GDP derivative with the formation of a correct lipid-oligosaccharide.

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Citations

Jan 1, 1987·Pharmacology & Therapeutics·R DatemaP A Romero
Sep 1, 1982·Antiviral Research·H D Klenk, R T Schwarz
Aug 15, 1984·European Journal of Biochemistry·Z N CanellakisA C Sartorelli
Jan 1, 1980·Pharmacology & Therapeutics·W M Shannon, F M Schabel
Apr 5, 2005·Methods : a Companion to Methods in Enzymology·Sung Hoon BackRandal J Kaufman
Feb 1, 1980·Wilhelm Roux's Archives of Developmental Biology·Alexej Romanovský, Jindřich Nosek
Nov 1, 1988·Biochimie·W McDowell, R T Schwarz
Jul 1, 1992·Archives of Biochemistry and Biophysics·C C GeilenW Reutter

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