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Glycobiology vol 4 no 6 pp. 845-853, 1994
© 1994
research-article |
Biosynthesis of lipophosphoglycan from Leishmania major: characterization of (ß1-3)-galactosyltransferase(s)
1The Walter and Eliza Hall Institute of Medical Research Post Office, Royal Melbourne Hospital, Victoria 3050, Australia
2Plant Cell Biology Research Centre, School of Botany, University of Melbourne Victoria 3052, Australia
3To whom correspondence should be addressed
Received on May 31, 1994; revised on August 8, 1994; accepted on August 8, 1994
Lipophosphoglycan (LPG) is the major cell surface molecule of promastigotes of all Leishmania species. It is comprised of three domains: a conserved GPI anchor linked to a repeating phosphorylated disaccharide (P2; PO4-6-Gal(ß1-4)Man(
1-) backbone variously substituted with galactose, glucose and arabinose residues in L.major and capped with a neutral oligosaccharide. Using a microsomal membrane preparation from L.major, we have been able to demonstrate that galactose from UDP-[14C]galactose can be transferred to an endogenous acceptor, characterized as LPG. An in vitro assay was established, based on anionexchange HPLC, that concurrently identifies and quantitates the products of the galactosyltransferases. We show that the products formed are [14C]galactose-labelled P3 (PO4-6-[Gal(ß1-3)]Gal(ß1-4)Man(1-), P4b (PO4-6-[Gal(ß1-3)Gal(ß1-3)]Gal(ß1-4)Man(1-) and P5b(PO4-6-[Gal(ß1-3)Gal(ß1-3)Gal(ß1-3)]Gal(ß1-4)Man(1-). These are major galactosylated repeating units of the backbone of L.major LPG. The same products are also formed when LPG from L.donovani, which contains an unbranched backbone of P2 repeats, is used as an exogenous acceptor with L.major microsomal membranes and UDP-[14C]galactose. In addition, no formation of radioactive backbone repeats (P2) was detected in membrane incubations containing UDP-[14C]galactose with or without added unlabelled GDP-mannose, indicating that the addition of the (ß1-3)-linked galactose branches is independent of the synthesis of the repeating disaccharide (P2) backbone. Preliminary kinetic analyses suggest that the addition of multiple (ß1-3)-linked galactose residues may be catalysed by more than one (ß1-3) galactosyltransferase. The (ß1-3)galactosyltransferase(s) activity was not detected in microsomal membrane preparations from promastigotes of L.donovani.
biosynthesis galactosyltransferases glycosyltransferases Leishmania lipophosphoglycan
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