Glycosyl-phosphatidylinositol moiety that anchors trypanosoma-brucei variant surface glycoprotein to the membrane

Michael A. J. Ferguson, Steve W. Homans, Raymond A. Dwek, Thomas W. Rademacher

    Research output: Contribution to journalArticlepeer-review

    529 Citations (Scopus)


    Two forms of protein-membrane anchor have been described for the externally disposed glycoproteins of eukaryotic plasma membranes; namely, the hydrophobic transmembrane polypeptide and the complex glycosylphosphatidylinositol (G-PI) moiety. The chemical structures of the major species of G-PI anchors found on a single variant surface glycoprotein (VSG) of the parasitic protozoan Trypanosoma brucei were determined by a combination of nuclear magnetic resonance spectroscopy, mass spectrometry, chemical modification, and exoglycosidase digestions. The G-PI anchor was found to be heterogeneous with respect to monosaccharide sequence, and several novel glycosidic linkages were present. The results are pertinent to the mechanism of the biosynthesis of G-PI anchors.

    Original languageEnglish
    Pages (from-to)753-759
    Number of pages7
    Issue number4841
    Publication statusPublished - 12 Feb 1988

    Cite this