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J. Biol. Chem., Vol. 261, Issue 26, 12147-12153, 09, 1986
JL Krakow, D Hereld, JD Bangs, GW Hart and PT Englund
The variant surface glycoprotein (VSG) of Trypanosoma brucei has a
glycolipid covalently attached to its C terminus. This glycolipid, which
anchors the protein to the cell membrane, is attached to the VSG
polypeptide within 1 min after translation (Bangs, J. D. Hereld, D.,
Krakow, J.L., Hart, G. W., and Englund, P. T. (1985) Proc. Natl. Acad. Sci.
U. S. A. 82, 3207-3211). This rapid processing suggests that, prior to
incorporation, the glycolipid may exist in the cell as a preformed
precursor which is transferred to the VSG polypeptide en bloc. We have
isolated a molecule which has properties consistent with it being a VSG
glycolipid precursor. It is highly polar and can be labeled by [3H]
myristate but not by [3H]palmitate. It reaches steady state during
continuous labeling with [3H]myristate and shows rapid turnover in
pulse-chase experiments, suggesting that it is a metabolic intermediate
rather than an end product. When treated with HNO2 it liberates
phosphatidylinositol, as does VSG (Ferguson, M. A. J., Low, M. G., and
Cross, G. A. M. (1985) J. Biol. Chem. 260, 14547-14555). Also, like VSG, it
releases a compound which co-migrates on thin layer chromatography with
dimyristylglycerol when treated with the purified endogenous phospholipase
C from trypanosomes. After treatment with this lipase, the putative
precursor can be immunoprecipitated by antibodies directed against the
C-terminal cross-reactive antigenic determinant of the VSG. These data
provide strong evidence that this glycolipid is a VSG precursor.
Identification of a glycolipid precursor of the Trypanosoma brucei variant surface glycoprotein
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