Characterisation of the asparagine-linked oligosaccharides from Trypanosoma brucei type-I variant surface glycoproteins

Susanne E. Zamze, E. Wrenn Wooten, David A. Ashford, Michael A. J. Ferguson, Raymond A. Dwek, Thomas W. Rademacher

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    Abstract

    The complete primary structures of the Asn-linked oligosaccharides from the conserved glycosylation site of the type-I variant surface glycoproteins of Trypanosoma brucei MITat 1.4 and MITat 1.6 were determined using a combination of exoglycosidase digestions, permethylation analysis, acetolysis and 1H NMR. Both variants contained almost exclusively oligomannose-type oligosaccharides, identical in structure to those of mammalian glycoproteins. The oligosaccharides ranged in size from (Man)9(GlcNAc)2 to (Man)5(GlcNAc)2. The relative abundance of each component was similar in both variants. The major components were (Man)8(GlcNAc)2 and (Man)7(GlcNAc)2 with slightly less (Man)9(GlcNAc)2 and (Man)6(GlcNAc)2 and much less (Man)5(GlcNAc)2. Both variants also contained the same structural isomers. The close similarity of the oligomannose series indicates identical processing at the conserved site in both variants.

    Original languageEnglish
    Pages (from-to)657-663
    Number of pages7
    JournalEuropean Journal of Biochemistry
    Volume187
    Issue number3
    DOIs
    Publication statusPublished - 14 Feb 1990

    Fingerprint

    Trypanosoma brucei brucei
    Asparagine
    Membrane Glycoproteins
    Oligosaccharides
    Trypanosoma Variant Surface Glycoproteins
    Glycosylation
    Glycoside Hydrolases
    Isomers
    Digestion
    Glycoproteins
    Nuclear magnetic resonance
    N,N-diacetylchitobiose
    Processing
    mannosyl(9)-N-acetylglucosamine(2)

    Cite this

    Zamze, Susanne E. ; Wooten, E. Wrenn ; Ashford, David A. ; Ferguson, Michael A. J. ; Dwek, Raymond A. ; Rademacher, Thomas W. / Characterisation of the asparagine-linked oligosaccharides from Trypanosoma brucei type-I variant surface glycoproteins. In: European Journal of Biochemistry. 1990 ; Vol. 187, No. 3. pp. 657-663.
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    abstract = "The complete primary structures of the Asn-linked oligosaccharides from the conserved glycosylation site of the type-I variant surface glycoproteins of Trypanosoma brucei MITat 1.4 and MITat 1.6 were determined using a combination of exoglycosidase digestions, permethylation analysis, acetolysis and 1H NMR. Both variants contained almost exclusively oligomannose-type oligosaccharides, identical in structure to those of mammalian glycoproteins. The oligosaccharides ranged in size from (Man)9(GlcNAc)2 to (Man)5(GlcNAc)2. The relative abundance of each component was similar in both variants. The major components were (Man)8(GlcNAc)2 and (Man)7(GlcNAc)2 with slightly less (Man)9(GlcNAc)2 and (Man)6(GlcNAc)2 and much less (Man)5(GlcNAc)2. Both variants also contained the same structural isomers. The close similarity of the oligomannose series indicates identical processing at the conserved site in both variants.",
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    Characterisation of the asparagine-linked oligosaccharides from Trypanosoma brucei type-I variant surface glycoproteins. / Zamze, Susanne E.; Wooten, E. Wrenn; Ashford, David A.; Ferguson, Michael A. J.; Dwek, Raymond A.; Rademacher, Thomas W.

    In: European Journal of Biochemistry, Vol. 187, No. 3, 14.02.1990, p. 657-663.

    Research output: Contribution to journalArticle

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    AU - Zamze, Susanne E.

    AU - Wooten, E. Wrenn

    AU - Ashford, David A.

    AU - Ferguson, Michael A. J.

    AU - Dwek, Raymond A.

    AU - Rademacher, Thomas W.

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    N2 - The complete primary structures of the Asn-linked oligosaccharides from the conserved glycosylation site of the type-I variant surface glycoproteins of Trypanosoma brucei MITat 1.4 and MITat 1.6 were determined using a combination of exoglycosidase digestions, permethylation analysis, acetolysis and 1H NMR. Both variants contained almost exclusively oligomannose-type oligosaccharides, identical in structure to those of mammalian glycoproteins. The oligosaccharides ranged in size from (Man)9(GlcNAc)2 to (Man)5(GlcNAc)2. The relative abundance of each component was similar in both variants. The major components were (Man)8(GlcNAc)2 and (Man)7(GlcNAc)2 with slightly less (Man)9(GlcNAc)2 and (Man)6(GlcNAc)2 and much less (Man)5(GlcNAc)2. Both variants also contained the same structural isomers. The close similarity of the oligomannose series indicates identical processing at the conserved site in both variants.

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