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 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.
Krakow
J L
JL
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD.
Doering
T L
TL
Masterson
W J
WJ
Hart
G W
GW
Englund
P T
PT
D000818:Animals; D002855:Chromatography, Thin Layer; D006017:Glycolipids / Q000032:analysis* / Q000302:isolation & purification; D008562:Membrane Glycoproteins / Q000032:analysis*; D010716:Phosphatidylinositols; D012995:Solubility; D014346:Trypanosoma brucei brucei / Q000032:analysis*
D006017:Glycolipids; D008562:Membrane Glycoproteins; D010716:Phosphatidylinositols