Glycotyping of Trypanosoma brucei variant surface glycoprotein MITat1.8

Angela Mehlert, Lauren Sullivan, Michael A. J. Ferguson

    Research output: Contribution to journalArticle

    10 Citations (Scopus)

    Abstract

    Following a switch from variant surface glycoprotein MITat1.4 to variant surface glycoprotein MITat1.8 expression by Lister strain 427 Trypanosoma brucei brucei parasites, the latter uncharacterized variant surface glycoprotein was analysed. Variant surface glycoprotein MITat1.8 was found to be a disulphide-linked homodimer, containing a complex N-linked glycan at Asn58 and a glycosylphosphatidylinositol membrane anchor attached to Asp419. Mass spectrometric analyses demonstrated that the N-glycan is exclusively Gal beta-4GlcNAc beta 1-2Man alpha 1-3(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6)Man beta 1-4GlcNAc beta 1-4GlcNAc and that the conserved Man(3)GlcN-myo-inositol glycosylphosphatidylinositol anchor glycan core is substituted with an average of 4 hexose, most likely galactose, residues. The presence of a complex N-glycan at Asn58 is consistent with the relatively acidic environment of the Asn58 N-glycosylation sequon, that predicts N-glycosylation by T. brucei oligosaccharyltransferase TbSTDA with a Man(5)GlcNAc(2) structure destined for processing to a paucimannose and/or complex N-glycan (Izquierdo L, Schulz B, Rodrigues JA et al. EMBO J 2009;28:2650-61 [121). (C) 2010 Elsevier B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)74-77
    Number of pages4
    JournalMolecular and Biochemical Parasitology
    Volume174
    Issue number1
    DOIs
    Publication statusPublished - Nov 2010

    Keywords

    • Trypanosoma brucei
    • N-linked oligosaccharides
    • N-glycosylation
    • Glycosylphosphatidylinositol
    • GPI
    • Mass spectrometry
    • GLYCOSYLPHOSPHATIDYLINOSITOL MEMBRANE ANCHOR
    • ASPARAGINE-LINKED OLIGOSACCHARIDES
    • ANTIGENS
    • GLYCOSYLATION
    • EXPRESSION
    • PREDICTION
    • GLYCAN
    • COAT

    Cite this