Glycosyl-Phosphatidylinositol Moiety That Anchors Trypanosoma brucei Variant Surface Glycoprotein to the Membrane
- 12 February 1988
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 239 (4841) , 753-759
- https://doi.org/10.1126/science.3340856
Abstract
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.This publication has 47 references indexed in Scilit:
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