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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| Autores principales: | , , |
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| Publicado: |
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 |
| Aporte de: |
| Sumario: | 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 |
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