Document Detail

Sulphation of N-linked oligosaccharides of vesicular stomatitis and influenza virus envelope glycoproteins: host cell specificity, subcellular localization and identification of substituted saccharides.
MedLine Citation:
PMID:  9445377     Owner:  NLM     Status:  MEDLINE    
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 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 alpha1-->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.
V K Karaivanova; R G Spiro
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Biochemical journal     Volume:  329 ( Pt 3)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1998 Feb 
Date Detail:
Created Date:  1998-03-03     Completed Date:  1998-03-03     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  511-8     Citation Subset:  IM    
Department of Biological Chemistry, Harvard Medical School, Joslin Diabetes Center, Boston, MA 02215, USA.
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MeSH Terms
Antiviral Agents / pharmacology
Brefeldin A
CHO Cells
Carbohydrate Conformation
Carbohydrate Sequence
Cell Line
Cyclopentanes / pharmacology
Hemagglutinin Glycoproteins, Influenza Virus / chemistry,  drug effects,  metabolism*
Membrane Glycoproteins*
Oligosaccharides / chemistry,  metabolism*
Subcellular Fractions / enzymology,  metabolism
Sulfates / metabolism*
Sulfotransferases / metabolism
Tumor Cells, Cultured
Vesicular stomatitis Indiana virus*
Viral Envelope Proteins / chemistry,  drug effects,  metabolism*
Grant Support
Reg. No./Substance:
0/Antiviral Agents; 0/Cyclopentanes; 0/G protein, vesicular stomatitis virus; 0/Hemagglutinin Glycoproteins, Influenza Virus; 0/Membrane Glycoproteins; 0/Oligosaccharides; 0/Sulfates; 0/Viral Envelope Proteins; 20350-15-6/Brefeldin A; EC sulfotransferase; EC 2.8.2.-/Sulfotransferases

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