Structures of the N-linked oligosaccharides of gp63, the major surface glycoprotein, from Leishmania mexicana amazonensis

Robert W. Olafson, Jerry R. Thomas, Michael A. J. Ferguson, Raymond A. Dwek, M. Chaudhuri, Kwang-Poo Chang, Thomas W. Rademacher

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    52 Citations (Scopus)

    Abstract

    The extent of protein N-glycosylation in Leishmania mexicana amazonensis has been proposed to be a factor in the virulence of the parasite. The N-linked oligosaccharides of gp63, the major surface glycoprotein of L. mexicana amazonensis, were characterized after their release by hydrazinolysis, re-N-acetylation, and reduction with NaB3H4. High voltage paper electrophoresis of the reduced oligosaccharides revealed only neutral species. Gel-permeation chromatography on Bio-Gel P-4 yielded four fractions, and the oligosaccharides present were structurally characterized by sequential exoglycosidase digestion, fragmentation by acetolysis, and methylation analysis. Four major structures were found and were biantennary oligomannose type with compositions of Glc1Man6GlcNAc2 (La), Man6GlcNAc2 (Lb), Man5GlcNAc2 (Lc), and Man4 GlcNAc2 (Ld). The largest oligosaccharide (La) was shown to contain a terminal glucopyranosyl residue on the a(1?3) arm. The biantennary oligomannose structures (Lb and Lc) and the glucosylated structure Glc1Man6GlcNAc2 (La) have not previously been reported as a component of a mature glycoprotein from any source.

    Original languageEnglish
    Pages (from-to)12240-12247
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume265
    Issue number21
    Publication statusPublished - 25 Jul 1990

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