Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors
The lipopeptidophosphoglycan (LPPG) from Trypanosoma cruzi, a major constituent of the plasma membrane of epimastigote forms, has been now extracted with butanol/water from delipidated cells and purified by hydrophobic chromatography. We have found that the LPPG undergoes two reactions, characterist...
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1990
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v192_n2_p337_deLEDERKREMER http://hdl.handle.net/20.500.12110/paper_00142956_v192_n2_p337_deLEDERKREMER |
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paper:paper_00142956_v192_n2_p337_deLEDERKREMER2023-06-08T14:36:41Z Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors Muchnik de Lederkremer, Rosa María Ramírez, María Isabel Casal de Russo, Olga Liliana glycan lipid peptide phospholipase article cell membrane enzyme linked immunosorbent assay invertebrate nonhuman priority journal protozoon trypanosoma cruzi Animal Ceramides Chromatography, High Pressure Liquid Enzyme-Linked Immunosorbent Assay Glycolipids Glycosylphosphatidylinositols Oxidation-Reduction Peptidoglycan Phosphatidylinositols Phospholipase C Phospholipids Support, Non-U.S. Gov't Trypanosoma cruzi Bacillus thuringiensis Invertebrata Protozoa Trypanosoma Trypanosoma cruzi The lipopeptidophosphoglycan (LPPG) from Trypanosoma cruzi, a major constituent of the plasma membrane of epimastigote forms, has been now extracted with butanol/water from delipidated cells and purified by hydrophobic chromatography. We have found that the LPPG undergoes two reactions, characteristic of the glycosylphosphatidylinositol anchors: (a) cleavage of the ceramide by phosphatidylinositol‐specific phospholipase C(PtdIns‐specific phospholipase C) from Bacillus thuringiensis, (b) nitrous acid deamination of the non‐N‐acylated glucosamine. Palmitoylsphinganine, palmitoylsphingosine, lignoceroylsphinganine and, as minor components, the stearoylceramides were identified by gas liquid chromatography/mass spectrometry. The presence of cross reacting determinant (CRD) epitopes in the glycophosphoinositol released by PtdIns‐specific phospholipase C was investigated by direct and inhibition ELISA. A sample of glycophosphoinositol containing 5 μg carbohydrate caused 60% inhibition of the binding of anti‐CRD antibodies raised against the soluble form of variant surface glycoprotein. Copyright © 1990, Wiley Blackwell. All rights reserved Fil:de LEDERKREMER, R.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:RAMIREZ, M.I. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:CASAL, O.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1990 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v192_n2_p337_deLEDERKREMER http://hdl.handle.net/20.500.12110/paper_00142956_v192_n2_p337_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 lipid peptide phospholipase article cell membrane enzyme linked immunosorbent assay invertebrate nonhuman priority journal protozoon trypanosoma cruzi Animal Ceramides Chromatography, High Pressure Liquid Enzyme-Linked Immunosorbent Assay Glycolipids Glycosylphosphatidylinositols Oxidation-Reduction Peptidoglycan Phosphatidylinositols Phospholipase C Phospholipids Support, Non-U.S. Gov't Trypanosoma cruzi Bacillus thuringiensis Invertebrata Protozoa Trypanosoma Trypanosoma cruzi |
spellingShingle |
glycan lipid peptide phospholipase article cell membrane enzyme linked immunosorbent assay invertebrate nonhuman priority journal protozoon trypanosoma cruzi Animal Ceramides Chromatography, High Pressure Liquid Enzyme-Linked Immunosorbent Assay Glycolipids Glycosylphosphatidylinositols Oxidation-Reduction Peptidoglycan Phosphatidylinositols Phospholipase C Phospholipids Support, Non-U.S. Gov't Trypanosoma cruzi Bacillus thuringiensis Invertebrata Protozoa Trypanosoma Trypanosoma cruzi Muchnik de Lederkremer, Rosa María Ramírez, María Isabel Casal de Russo, Olga Liliana Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors |
topic_facet |
glycan lipid peptide phospholipase article cell membrane enzyme linked immunosorbent assay invertebrate nonhuman priority journal protozoon trypanosoma cruzi Animal Ceramides Chromatography, High Pressure Liquid Enzyme-Linked Immunosorbent Assay Glycolipids Glycosylphosphatidylinositols Oxidation-Reduction Peptidoglycan Phosphatidylinositols Phospholipase C Phospholipids Support, Non-U.S. Gov't Trypanosoma cruzi Bacillus thuringiensis Invertebrata Protozoa Trypanosoma Trypanosoma cruzi |
description |
The lipopeptidophosphoglycan (LPPG) from Trypanosoma cruzi, a major constituent of the plasma membrane of epimastigote forms, has been now extracted with butanol/water from delipidated cells and purified by hydrophobic chromatography. We have found that the LPPG undergoes two reactions, characteristic of the glycosylphosphatidylinositol anchors: (a) cleavage of the ceramide by phosphatidylinositol‐specific phospholipase C(PtdIns‐specific phospholipase C) from Bacillus thuringiensis, (b) nitrous acid deamination of the non‐N‐acylated glucosamine. Palmitoylsphinganine, palmitoylsphingosine, lignoceroylsphinganine and, as minor components, the stearoylceramides were identified by gas liquid chromatography/mass spectrometry. The presence of cross reacting determinant (CRD) epitopes in the glycophosphoinositol released by PtdIns‐specific phospholipase C was investigated by direct and inhibition ELISA. A sample of glycophosphoinositol containing 5 μg carbohydrate caused 60% inhibition of the binding of anti‐CRD antibodies raised against the soluble form of variant surface glycoprotein. Copyright © 1990, Wiley Blackwell. All rights reserved |
author |
Muchnik de Lederkremer, Rosa María Ramírez, María Isabel Casal de Russo, Olga Liliana |
author_facet |
Muchnik de Lederkremer, Rosa María Ramírez, María Isabel Casal de Russo, Olga Liliana |
author_sort |
Muchnik de Lederkremer, Rosa María |
title |
Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors |
title_short |
Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors |
title_full |
Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors |
title_fullStr |
Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors |
title_full_unstemmed |
Structural features of the lipopeptidophosphoglycan from Trypanosoma cruzi common with the glycophosphatidylinositol anchors |
title_sort |
structural features of the lipopeptidophosphoglycan from trypanosoma cruzi common with the glycophosphatidylinositol anchors |
publishDate |
1990 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v192_n2_p337_deLEDERKREMER http://hdl.handle.net/20.500.12110/paper_00142956_v192_n2_p337_deLEDERKREMER |
work_keys_str_mv |
AT muchnikdelederkremerrosamaria structuralfeaturesofthelipopeptidophosphoglycanfromtrypanosomacruzicommonwiththeglycophosphatidylinositolanchors AT ramirezmariaisabel structuralfeaturesofthelipopeptidophosphoglycanfromtrypanosomacruzicommonwiththeglycophosphatidylinositolanchors AT casalderussoolgaliliana structuralfeaturesofthelipopeptidophosphoglycanfromtrypanosomacruzicommonwiththeglycophosphatidylinositolanchors |
_version_ |
1768544668619898880 |