N-glycosylation pattern of E2 glycoprotein from classical swine fever virus.
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.
Montesino
Raquel
R
Department of Carbohydrate Chemistry, Center for Genetic Engineering and Biotechnology, Havana 10600, Cuba.
Toledo
Jorge R
JR
Sanchez
Oliberto
O
Zamora
Yasser
Y
Barrera
Maritza
M
Royle
Louise
L
Rudd
Pauline M
PM
Dwek
Raymond A
RA
Harvey
David J
DJ
Cremata
Jose A
JA
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006031:Glycosylation; D007668:Kidney / Q000166:cytology; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000032:analysis*; D034421:Sus scrofa; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism
D011134:Polysaccharides; D014759:Viral Envelope Proteins; C087086:glycoprotein E2, classical swine fever virus; D006026:Glycoside Hydrolases