Galactofuranose-containing glycoconjugates in trypanosomatids

Abstract

Galactofuranose has been characterized in glycoinositolphospholipid (GIPL) anchor-like structures having a glycerolipid or a ceramide, as in lipopeptidophosphoglycan (LPPG) of Trypanosoma cruzi, in the oligosaccharide core of lipopeptidophosphoglycan (LPG) of Leishmania species, and also modifying high-mannose chains of trypanosomatid glycoproteins. Galactofuranose is usually present linked beta 1-->3 to Man, either as a terminal non-reducing unit, like in LPPG, or in the middle of the oligosaccharide core, as in LPG. The presence in protozoan parasites of galactose in the furanose configuration is a feature which deserves further attention since the mammalian hosts do not appear to produce glycoconjugates containing this structural unit. For that reason, hosts produce antibodies against galactofuranose, which may turn out to be important in understanding the pathogenesis and in the development of diagnostic methods. The metabolic pathways involved in the attachment to or removal of galactofuranose from glycoconjugates have not yet been elucidated. This is an area of incipient research, but of growing importance, since it will foster the design of inhibitors which may prove to be useful for the treatment of disease.