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N-glycosylation pattern of E2 glycoprotein from classical swine fever virus

Abstract:

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 a1-3-Gal-Gal antennae terminals. The most abundant neutral N-glycan has a composition of Hex7HexNAc4dHex1 Negative ion ESI-MS/MS confirmed the presence of the α1-3-Gal-Gal motif on each arm of the fucosylated biantennary N-glycan. The most abundant monosialylated glycan was Hex6HexNAc4dHex 1Neu5Ac1, with the sialic acid linked to the terminal β1-4-Gal-GlcNAc. Sialic acid on the antenna capping position was predominantly of the N-acetyl form. © 2009 American Chemical Society.