Sulphation of N-linked oligosaccharides of vesicular stomatitis and influenza virus envelope glycoproteins: host cell specificity, subcellular localization and identification of substituted saccharides
| Autor: | K. Velislava Karaivanova, G. Robert Spiro |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Swine
Oligosaccharides Hemagglutinin Glycoproteins Influenza Virus CHO Cells Cyclopentanes Antiviral Agents Biochemistry Vesicular stomatitis Indiana virus Cell Line Mice Vesicular Stomatitis chemistry.chemical_compound Dogs Viral Envelope Proteins Viral envelope Cricetinae Carbohydrate Conformation Tumor Cells Cultured Animals Molecular Biology chemistry.chemical_classification Brefeldin A Membrane Glycoproteins biology Sulfates urogenital system Chinese hamster ovary cell Cell Biology biology.organism_classification Rats Membrane glycoproteins Carbohydrate Sequence chemistry Kifunensine Vesicular stomatitis virus Galactose biology.protein Cattle Sulfotransferases Glycoprotein Subcellular Fractions Research Article |
| Zdroj: | Biochemical Journal. 329:511-518 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | The presence of sulphate groups on various saccharide residues of N-linked carbohydrate units has now been observed in a number of glycoproteins. To explore the cell specificity of this post-translational modification, we evaluated sulphate incorporation into virus envelope glycoproteins by a variety of cells, since it is believed that assembly of their N-linked oligosaccharides is to a large extent dependent on the enzymic machinery of the host. Employing the vesicular stomatitis virus (VSV) envelope glycoprotein (G protein) as a model, we noted that the addition of [35S]sulphate substituents into its complex carbohydrate units occurred in Madin-Darby canine kidney (MDCK), Madin-Darby bovine kidney, LLC-PK1 and BHK-21 cell lines but was not detectable in BRL 3A, BW5147.3, Chinese hamster ovary, HepG2, NRK-49F, IEC-18, PtK1 or 3T3 cells. The sulphate groups were exclusively located on C-3 of galactose [Gal(3-SO4)] and/or C-6 of N-acetylglucosamine [GlcNAc(6-SO4)] residues in the N-acetyllactosamine sequence of the branch chains. Moreover, we observed that the pronounced host-cell-dependence of the terminal galactose sulphation was reflected by the 3ʹ-phosphoadenosine 5ʹ-phosphosulphate:Gal-3-O-sulphotransferase activity assayed in vitro. Comparative studies carried out on the haemagglutinin of the influenza virus envelope formed by MDCK and LLC-PK1 cells indicated that sulphate in this glycoprotein was confined to its complex N-linked oligosaccharides where it occurred as Gal(3-SO4) and GlcNAc(6-SO4) on peripheral chains as well as on the mannose-substituted N-acetylglucosamine of the core. Since sulphation in both internal and peripheral locations of the virus glycoproteins was found to be arrested by the α1 → 2 mannosidase inhibitor, kifunensine, as well as by the intracellular migration block imposed by brefeldin A, it was concluded that this modification is a late biosynthetic event which most likely takes place in the trans-Golgi network. |
| Databáze: | OpenAIRE |
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