THE GLYCOSYLPHOSPHATIDYLINOSITOL MEMBRANE ANCHOR OF TRYPANOSOMA-BRUCEI VARIANT SURFACE GLYCOPROTEIN
THE GLYCOSYLPHOSPHATIDYLINOSITOL MEMBRANE ANCHOR OF TRYPANOSOMA-BRUCEI VARIANT SURFACE GLYCOPROTEIN
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DOI:
10.1042/bst0160265
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发表时间:
1988-06-01
影响因子:
3.9
通讯作者:
RADEMACHER, TW
中科院分区:
文献类型:
--
作者:
FERGUSON, MAJ;HOMANS, SW;RADEMACHER, TW
The cell surface integral membrane glycoproteins of eukaryotes can be classified with respect to the mode of attachment to the plasma membrane. The major class employs one or more transmembrane hydrophobic peptide sequences; the minor class is anchored via a covalent linkage to a phosphatidylinositol phospholipid. The latter anchor appears to be particularly common in protozoa. The variant surface glycoproteins of Trypunosomu brucei present a model system for the study of the structural and biosynthetic features of phosphatidylinositol-containing membrane anchors. The occurrence and general biochemistry of phosphatidylinositol-anchored proteins has been reviewed (Low et ul., 1986; Cross, 1987; Low. 1987; Ferguson 61 Williams, 1988). The basic arrangement of the T. brucei variant surface glycoprotein (VSG) membrane anchor was established by a variety of chemical modifications and by compositional analysis (Holder, 1983, 198.5; Ferguson 61 Cross, 1984; Ferguson et ul., 198Su, h) which showed that the anchor was a mannose-. galactose-and glucosamine-containing glycosylphosphatidylinositol (GPI) moiety, linked to the protein a-COOH group via an ethanolamine bridge. The complete structure of the GPI anchor of VSG variant MlTat. l. 4 has recently been determined by a combination of two-dimensional ‘H nmr, gas chromatography-mass spectrometry, chemical modifications and exoglycosidase digestion (Ferguson et ul., 1988)(see Fig. 1) The anchor displays