Comprehensive analysis of alpha 2-3-linked sialic acid specific Maackia amurensis leukagglutinin reveals differentially occupied N-glycans and C-terminal processing

Kumar, Gnanesh B S and Surolia, Avadhesha (2017) Comprehensive analysis of alpha 2-3-linked sialic acid specific Maackia amurensis leukagglutinin reveals differentially occupied N-glycans and C-terminal processing. In: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 94 (A). pp. 114-121.

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Abstract

Seeds of Maackia amurensis constitutes two sialic acid specific agglutinins known as leukagglutinin and hemagglutinin. Maackia amurensis leukagglutinin (MAL) recognizes alpha 12-3-linked sialic acid present mainly in N-glycans and composed of two disulfide linked monomers. It exhibits potential N-glycosylation sites (four PNGs) which have been assumed to undergo differential occupancy. In this study we have characterized the site specific macro- and microheterogeneity of monomers in detail by analysing N-glycopeptides and peptides through liquid chromatography coupled to ion trap mass spectrometer in MS3 mode (LC-MSn). We observed the presence of mainly paucimannose N-glycans at Asn(61), Asn(113) and Asn(191) whereas a high mannose type with varying Man(5-9) occurs at Asn(179). Interestingly Asn(179) and Asn(191) exhibited differential occupancy which was evident by the presence of non-glycosylated peptides. This has contributed to the difference in molecular mass of monomers upon SDS-PAGE. Further the presence of disulfide linked peptides confirmed the covalent linkage of monomers which also undergoes uniform C-terminal processing. (C) 2016 Elsevier B.V. All rights reserved.

Item Type:	Journal Article
Publication:	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Additional Information:	Copy right for this article belongs to the ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	31 Jan 2017 05:28
Last Modified:	31 Jan 2017 05:28
URI:	http://eprints.iisc.ac.in/id/eprint/56112

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