A glycolipid from Trypanosoma brucei related to the variant surface glycoprotein membrane anchor

The variant surface glycoprotein (VSG) of Trypanosoma brucei is covalently linked to a phosphatidylinositol-containing glycolipid which serves as a membrane anchor. We previously identified a molecule, glycolipid A, which appears to be a biosynthetic precursor to the anchor [9]. In this paper we des...

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Veröffentlicht in:Molecular and biochemical parasitology 1989-10, Vol.36 (3), p.263-270
Hauptverfasser: Krakow, Jessica L., Doering, Tamara L., Masterson, Wayne J., Hart, Gerald W., Englund, Paul T.
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Sprache:eng
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Zusammenfassung:The variant surface glycoprotein (VSG) of Trypanosoma brucei is covalently linked to a phosphatidylinositol-containing glycolipid which serves as a membrane anchor. We previously identified a molecule, glycolipid A, which appears to be a biosynthetic precursor to the anchor [9]. In this paper we describe a related molecule, glycolipid C, which is similar to glycolipid A but which is more hydrophobic. Chromatographic analyses indicate that the polar head groups in glycolipids A and C are similar or identical. Both glycolipids contain phosphatidylinositol, but the inositol in glycolipid C is modified by a hydrophobic moiety. Since treatment of glycolipid C with mild alkali results in partial conversion to a molecule chromatographically identical to glycolipid A, it is likely that glycolipid C has an alkali-sensitive hydrophobic group, such as a fatty acid, linked to its inositol moiety.
ISSN:0166-6851
1872-9428
DOI:10.1016/0166-6851(89)90174-6