Glycosylation in vitro of Semliki-Forest-Virus and Influenza-Virus Glycoproteins and Its Suppression by Nucleotide-2-deoxy-hexose
Autor: | Ralph T. Schwarz, Ludwig Lehle, Michael F. G. Schmidt |
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Rok vydání: | 1978 |
Předmět: |
Guanosine Diphosphate Mannose
Glycosylation Mannose Semliki Forest virus medicine.disease_cause Biochemistry Virus Dolichol monophosphate Viral Proteins chemistry.chemical_compound Dolichol Influenza A virus medicine Glycoproteins Dolichol Phosphates chemistry.chemical_classification biology Uridine Diphosphate Sugars biology.organism_classification Semliki forest virus Kinetics chemistry Guanosine Diphosphate Sugars lipids (amino acids peptides and proteins) Glycoprotein |
Zdroj: | European Journal of Biochemistry. 85:163-172 |
ISSN: | 1432-1033 0014-2956 |
Popis: | 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. |
Databáze: | OpenAIRE |
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