Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes
The lipopeptidophosphoglycan is the major cell surface glycoconjugate of the epimastigote forms of the parasitic protozoan Trypanosoma cruzi. A detailed partial structure for this molecule has been reported (Previato, J. O., Gorin, P. A. J., Mazurek, M., Xavier, M. T., Fournet, B., Wieruszesk, J. M....
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todo:paper_00219258_v266_n35_p23670_DeLederkremer2023-10-03T14:22:56Z Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes De Lederkremer, R.M. Lima, C. Ramirez, M.I. Ferguson, M.A.J. Homans, S.W. Thomas-Oates, J. glycan glycan phosphate lipoprotein unclassified drug article chemical structure epimastigote nonhuman priority journal trypanosoma cruzi Acylation Animal Carbohydrate Sequence Chromatography, High Pressure Liquid Magnetic Resonance Spectroscopy Molecular Sequence Data Oligosaccharides Peptidoglycan Phospholipids Spectrometry, Mass, Fast Atom Bombardment Support, Non-U.S. Gov't Trypanosoma cruzi The lipopeptidophosphoglycan is the major cell surface glycoconjugate of the epimastigote forms of the parasitic protozoan Trypanosoma cruzi. A detailed partial structure for this molecule has been reported (Previato, J. O., Gorin, P. A. J., Mazurek, M., Xavier, M. T., Fournet, B., Wieruszesk, J. M., and Mendonca-Previato, L. (1990) J. Biol. Chem. 265, 2518-2526). In this study, we complete the primary structure assignments and describe the microheterogeneity found in the lipopeptidophosphoglycan glycan, using a combination of 1H and 31P NMR, fast atom bombardment mass spectrometry, methylation linkage analysis, and exoglycosidase sequencing. The lipopeptidophosphoglycan is a glycosylated inositol-phosphoceramide with striking homology to glycosylphosphatidylinositol membrane anchors found attached to a wide variety of plasma membrane proteins throughout the eukaryotes. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219258_v266_n35_p23670_DeLederkremer |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
glycan glycan phosphate lipoprotein unclassified drug article chemical structure epimastigote nonhuman priority journal trypanosoma cruzi Acylation Animal Carbohydrate Sequence Chromatography, High Pressure Liquid Magnetic Resonance Spectroscopy Molecular Sequence Data Oligosaccharides Peptidoglycan Phospholipids Spectrometry, Mass, Fast Atom Bombardment Support, Non-U.S. Gov't Trypanosoma cruzi |
spellingShingle |
glycan glycan phosphate lipoprotein unclassified drug article chemical structure epimastigote nonhuman priority journal trypanosoma cruzi Acylation Animal Carbohydrate Sequence Chromatography, High Pressure Liquid Magnetic Resonance Spectroscopy Molecular Sequence Data Oligosaccharides Peptidoglycan Phospholipids Spectrometry, Mass, Fast Atom Bombardment Support, Non-U.S. Gov't Trypanosoma cruzi De Lederkremer, R.M. Lima, C. Ramirez, M.I. Ferguson, M.A.J. Homans, S.W. Thomas-Oates, J. Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes |
topic_facet |
glycan glycan phosphate lipoprotein unclassified drug article chemical structure epimastigote nonhuman priority journal trypanosoma cruzi Acylation Animal Carbohydrate Sequence Chromatography, High Pressure Liquid Magnetic Resonance Spectroscopy Molecular Sequence Data Oligosaccharides Peptidoglycan Phospholipids Spectrometry, Mass, Fast Atom Bombardment Support, Non-U.S. Gov't Trypanosoma cruzi |
description |
The lipopeptidophosphoglycan is the major cell surface glycoconjugate of the epimastigote forms of the parasitic protozoan Trypanosoma cruzi. A detailed partial structure for this molecule has been reported (Previato, J. O., Gorin, P. A. J., Mazurek, M., Xavier, M. T., Fournet, B., Wieruszesk, J. M., and Mendonca-Previato, L. (1990) J. Biol. Chem. 265, 2518-2526). In this study, we complete the primary structure assignments and describe the microheterogeneity found in the lipopeptidophosphoglycan glycan, using a combination of 1H and 31P NMR, fast atom bombardment mass spectrometry, methylation linkage analysis, and exoglycosidase sequencing. The lipopeptidophosphoglycan is a glycosylated inositol-phosphoceramide with striking homology to glycosylphosphatidylinositol membrane anchors found attached to a wide variety of plasma membrane proteins throughout the eukaryotes. |
format |
JOUR |
author |
De Lederkremer, R.M. Lima, C. Ramirez, M.I. Ferguson, M.A.J. Homans, S.W. Thomas-Oates, J. |
author_facet |
De Lederkremer, R.M. Lima, C. Ramirez, M.I. Ferguson, M.A.J. Homans, S.W. Thomas-Oates, J. |
author_sort |
De Lederkremer, R.M. |
title |
Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes |
title_short |
Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes |
title_full |
Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes |
title_fullStr |
Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes |
title_full_unstemmed |
Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes |
title_sort |
complete structure of the glycan of lipopeptidophosphoglycan from trypanosoma cruzi epimastigotes |
url |
http://hdl.handle.net/20.500.12110/paper_00219258_v266_n35_p23670_DeLederkremer |
work_keys_str_mv |
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