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

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 glycosyl-phosphatidylinositol (G-PI) moiety. The chemical structures of the major species of G-PI ancho...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1988-02, Vol.239 (4841), p.753-759
Main Authors: Ferguson, M.A.J, Homans, S.W, Dwek, R.A, Rademacher, T.W
Format: Article
Language:English
Subjects:
Animals
Biochemistry
BIOLOGIA MOLECULAR
Biological and medical sciences
BIOLOGIE MOLECULAIRE
Carbohydrate Conformation
Carbohydrate Sequence
Carbohydrates - analysis
Cell Membrane - metabolism
Cell membranes
Cell membranes. Ionic channels. Membrane pores
CELL STRUCTURE
Cell structures and functions
cell surface
Connectivity
ESTRUCTURA CELULAR
Fractions
Functional groups
Fundamental and applied biological sciences. Psychology
GLICOPROTEINAS
GLYCOPROTEINE
GLYCOPROTEINS
glycosylphosphatidylinositol
Magnetic Resonance Spectroscopy
Mass Spectrometry
Membrane glycoproteins
Membrane proteins
Methylation
Molecular and cellular biology
MOLECULAR BIOLOGY
Molecular Sequence Data
Oxidation
Phosphates
Phosphatidylinositols - analysis
plasma membranes
Polysaccharides
Polysaccharides - analysis
Protons
STRUCTURE CELLULAIRE
TRYPANOSOMA
Trypanosoma brucei
Trypanosoma brucei brucei - metabolism
Variant Surface Glycoproteins, Trypanosoma - metabolism
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Summary: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 glycosyl-phosphatidylinositol (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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.3340856