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J. Biol. Chem., Vol. 265, Issue 16, 9033-9042, 06, 1990
AK Menon, RT Schwarz, S Mayor and GA Cross
Trypanosome variant surface glycoproteins exemplify a class of eukaryotic
cell surface glycoproteins that rely on a carboxyl-terminal
covalently-attached inositol-containing glycophospholipid for membrane
attachment. The glycolipid anchor is acquired soon after translation of the
polypeptide, apparently by replacement of a short carboxyl-terminal peptide
sequence with a prefabricated glycolipid. A candidate glycolipid precursor
(referred to as P2), and a related glycolipid (P3) have been identified
recently in polar lipid extracts from trypanosomes. In this paper we
describe the synthesis of P2 and P3 by trypanosome membranes. Analyses of
organic solvent extracts from membranes incubated with radioactive sugar
nucleotides (GDP-[3H]mannose or UDP-[3H]GlcNAc) showed a spectrum of
labelled lipids, ranging from partially glycosylated species to the final
products, P2 and P3. Structural analyses of these putative biosynthetic
intermediates suggest that glycolipid assembly occurs via the sequential
glycosylation of phosphatidylinositol.
Cell-free synthesis of glycosyl-phosphatidylinositol precursors for the glycolipid membrane anchor of Trypanosoma brucei variant surface glycoproteins. Structural characterization of putative biosynthetic intermediates
Rockefeller University, New York, New York 10021-6399.
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