Carbohydrate structure of Marburg virus glycoprotein

Marburg virus was propagated in E6 cells, a cloned cell line of Vero cells, in the presence of [6-3H]glucosamine Radiolabelled viral glycoprotein was digested with trypsin, and oligosaccharides were liberated by sequential treatment with endo-β-N-acetylglucosaminidase H, peptide-N4-(N-acetyl-β-gluco...

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Bibliographic Details
Published in:Glycobiology 1992-08, Vol.2 (4), p.299-312
Main Authors: Geyer, Hildegard, Will, Christiane, Feldmann, Heinz, Klenk, Hans-Dieter, Geyer, Rudolf
Format: Article
Language:English
Subjects:
Amidohydrolases
Animals
Carbohydrate Conformation
Carbohydrate Sequence
Chromatography, Gel
Chromatography, High Pressure Liquid
Filoviridae
Glucosamine - metabolism
glycoprotein
Glycoproteins - chemistry
Glycoproteins - isolation & purification
Glycoside Hydrolases
Hexosaminidases
Hydrogen-Ion Concentration
Lectins
Marburg virus
Marburgvirus - chemistry
Methylation
Molecular Sequence Data
Molecular Structure
N-Acetylneuraminic Acid
oligosaccharides
Oligosaccharides - chemistry
Oligosaccharides - metabolism
Original
Peptide Fragments - metabolism
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Polysaccharides - chemistry
Polysaccharides - isolation & purification
Polysaccharides - metabolism
Sialic Acids - analysis
structure analysis
Tritium
Trypsin
Vero Cells
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Summary:Marburg virus was propagated in E6 cells, a cloned cell line of Vero cells, in the presence of [6-3H]glucosamine Radiolabelled viral glycoprotein was digested with trypsin, and oligosaccharides were liberated by sequential treatment with endo-β-N-acetylglucosaminidase H, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F and O-glycosidase, by β-elimination, and by alkaline hydrolysis. After fractionation by HPLC and gel filtration, glycans were characterized chromatographically, by digestion with exoglycosidases and, in part, by methylation analysis and liquid secondary ion mass spectrometry. The oligosaccharide structures thus established include oligomannosidic and hybrid-type N-glycans, as well as neutral fucosylated bitri- and tetraantennary species, most of which carry an additional bisecting N-acetylglucosamine. In addition, high amounts of neutral mucin-type O-glycans with type-1 and type-2 core structures were detected. None of the glycans present in this viral glycoprotein carried sialic acid residues.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/2.4.299