PMID: 9445377Mar 7, 1998Paper

Sulphation of N-linked oligosaccharides of vesicular stomatitis and influenza virus envelope glycoproteins: host cell specificity, subcellular localization and identification of substituted saccharides

The Biochemical Journal
V K Karaivanova, R G Spiro

Abstract

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 3'-phosphoadenosine 5'-phosphosulphate:Gal-3-O-sulphotransferase activity assayed...Continue Reading

Citations

Jul 19, 2012·PloS One·Yuki Kobayashi, Yoshiyuki Suzuki
Feb 29, 2000·Antiviral Chemistry & Chemotherapy·B W DonovanJ R Baker
Apr 1, 2006·Glycoconjugate Journal·E M RapoportN V Bovin
Dec 10, 2016·Critical Reviews in Microbiology·Beatrice Ellen TyrrellNicole Zitzmann
Jul 2, 2021·The Journal of Clinical Investigation·Jiwon JungGeorge Georgiou
Mar 26, 2019·Analytical Chemistry·Yi-Min SheTerry D Cyr

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