Trypanosoma cruzi: The Tc-85 surface glycoprotein shed by trypomastigotes bears a modified glycosylphosphatidylinositol anchor
ABUIN, G., COUTO, A. S., DE LEDERKREMER, R. M., CASAL, O. L., GALLI, C., COLLI, W., AND ALVES, M. J. M. 1996. Trypanosoma cruzi: The Tc-85 surface glycoprotein shed by trypomastigotes bears a modified glycosylphosphatidylinositol anchor. Experimental Parasitology 82, 290-297. Tc-85, an 85-kDa surfac...
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1996
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00144894_v82_n3_p290_Abuin http://hdl.handle.net/20.500.12110/paper_00144894_v82_n3_p290_Abuin |
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| Sumario: | ABUIN, G., COUTO, A. S., DE LEDERKREMER, R. M., CASAL, O. L., GALLI, C., COLLI, W., AND ALVES, M. J. M. 1996. Trypanosoma cruzi: The Tc-85 surface glycoprotein shed by trypomastigotes bears a modified glycosylphosphatidylinositol anchor. Experimental Parasitology 82, 290-297. Tc-85, an 85-kDa surface glycoprotein specific for the trypomastigote stage of Trypanosoma cruzi, has been implicated in the invasion of host cells by the parasite. Radioactive palmitic acid was incorporated into Tc-85 immunoprecipitated from the culture medium with the H1A10 monoclonal antibody, suggesting that shedding occurs with Tc-85 bearing its GPI anchor. In contrast to the glycoprotein remaining in the parasites, the glycosylphosphatidylinositol moiety in shed Tc-85 is resistant to phosphatidylinositol phospholipase C and becomes susceptible to the enzyme following alkali treatment. An alkylglycerol was identified by thin layer chromatography of an ether extract after the enzymatic reaction. Resistance to cleavage by phospholipase C is due to fatty acid esterification of the inositol residue in shed Tc-85. This is the first example of inositol modification in anchors from a glycoprotein of Trypanosoma cruzi. © 1996 Academic Press, Inc. |
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