Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Identification of a variant surface glycoprotein (VSG) glycolipid precursor in Trypanosoma brucei

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7246753

The VSG coat protein of T. brucei has a glycolipid covalently attached to its C terminus which anchors it to the cell membrane. Compositional analyses of VSG, reported by several laboratories, indicate that the glycolipid contains myristic acid, glycerol, phosphate, inositol, several sugars, and ethanolamine. This glycolipid is found on the VSG polypeptide within 1 minute after translation, suggesting that prior to incorporation, it may exist in the cell as a preformed precursor. The authors have isolated a molecule which has properties consistent with being a VSG lipid precursor: it is highly polar and can be labelled by (/sup 3/H)myristate but not by (/sup 3/H)palmitate. It reaches steady-state during continuous labelling and shows rapid turnover in pulse-chase experiments, suggesting that it is a metabolic intermediate rather than an end product. When treated with HNO/sub 2/ it liberates phophatidylinositol, as does VSG, and, like VSG, releases dimyristylglycerol when treated with purified endogenous phospholipase C from trypanosomes. These data provide strong evidence that the glycolipid is a preformed precursor which is transferred to the VSG polypeptide en bloc.

Research Organization:
Johns Hopkins Medical School, Baltimore, MD
OSTI ID:
7246753
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:6; ISSN FEPRA
Country of Publication:
United States
Language:
English