Galactofuranose-containing glycoconjugates in trypanosomatids
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 lipophosphoglycan (LPG) of Leishmania species, and also modifying high-man...
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| Autores principales: | , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_09596658_v5_n6_p547_DeLederkremer |
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| Sumario: | 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 lipophosphoglycan (LPG) of Leishmania species, and also modifying high-mannose chains of trypanosomatid glycoproteins. Galactofuranose is usually present linked β1→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 donot appear to produce glycoconjugates containing this structural unit. For that reason, hosts produceantibodies 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 ofincipient research, but of growing importance, since it will foster the design of inhibitors which may prove to be useful for the treatment of disease. © 1995 Oxford University Press. |
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