N-Glycosylation Pattern of E2 Glycoprotein from Classical Swine Fever Virus
| Autor: | Jorge R. Toledo, José A. Cremata, Pauline M. Rudd, David J. Harvey, Louise Royle, Maritza Barrera, Raquel Montesino, Oliberto Sánchez, R A Dwek, Yasser Zamora |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Glycan
Glycosylation Glycoside Hydrolases Molecular Sequence Data Sus scrofa Biology Kidney Biochemistry Mass Spectrometry Virus Cell Line chemistry.chemical_compound Viral Envelope Proteins N-linked glycosylation Polysaccharides Exoglycosidase Carbohydrate Conformation Animals Epithelial Cells General Chemistry biology.organism_classification Sialic acid carbohydrates (lipids) Carbohydrate Sequence chemistry Classical swine fever biology.protein Carbohydrate conformation |
| Zdroj: | Journal of Proteome Research. 8:546-555 |
| ISSN: | 1535-3907 1535-3893 |
| Popis: | The extracellular domain of E2 glycoprotein outer surface of the classical swine fever virus was expressed in epithelial kidney pig cells. The N-glycosylation determined by combination of Normal Phase-HPLC, Weak Anion Exchange-HPLC, exoglycosidase digestions and Mass Spectrometry revealed a complex mixture of neutral and monosialylated multiantennary N-glycans with variable number of alpha1-3-Gal-Gal antennae terminals. The most abundant neutral N-glycan has a composition of Hex(7)HexNAc(4)dHex(1), Negative ion ESI-MS/MS confirmed the presence of the alpha1-3-Gal-Gal motif on each arm of the fucosylated biantennary N-glycan. The most abundant monosialylated glycan was Hex(6)HexNAc(4)dHex(1)Neu(5)Ac(1), with the sialic acid linked to the terminal beta1-4-Gal-GlcNAc. Sialic acid on the antenna capping position was predominantly of the N-acetyl form. |
| Databáze: | OpenAIRE |
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