Abstract
The striking ability of Leishmania parasites to survive in hostile environments with impunity throughout their life cycle has implicated the importance of specialized glycoconjugates on their surface. These glycoconjugates are generally glycoproteins or complex carbohydrates anchored in the membrane by covalently-linked glycosylphosphatidylinositol (GPI). Lipophosphoglycan (LPG) is the major cell surface glycoconjugate on the promastigote form of the parasite and is believed to be important for its uptake by and survival within macrophages. LPG consists of four domains: (i) a phosphatidylinositol lipid anchor, (ii) a glycan core, (iii) a repeating saccharide-phosphate region, and (iv) a small oligosaccharide cap structure. Some of the functions that have been attributed to LPG and related glycoconjugates have been determined by use of LPG-defective mutants of Leishmania parasites. These LPG- mutants were selected based on resistance to agglutination by the cytotoxic lectin rich agglutinin. One ricin-resistant clone, named R2D2, was found to be completely defective in the synthesis and expression of LPG, due to a defect in galactofuranose addition in the core region of LPG. The responsible defective protein in R2D2 is not yet precisely known, but is either the galactofuranosyltransferase or an enzyme involved in galactofuranose metabolism.
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