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Science 12 February 1988: Vol. 239. no. 4841, pp. 753 - 759 DOI: 10.1126/science.3340856
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Articles
Science, Vol 239, Issue 4841, 753-759
Copyright © 1988 by American Association for the Advancement of Science
Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
MA Ferguson,
SW Homans,
RA Dwek,
and
TW Rademacher
Oxford Oligosaccharide Group, Department of Biochemistry, University of Oxford, England.
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.
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