Trypanosoma cruzi: A 52-kDa Protein Sharing Sequence Homology with Glutathione S-Transferase Is Localized in Parasite Organelles Morphologically Resembling Reservosomes
| Autor: | M.A. Ouaissi, A. Tartar, C. Sergheraert, R. Schöneck, R. Fernandezgomez, Odile Billaut-Mulot, R. Gomezcorvera, J P Kusnierz, A. Taibi, Jean-François Dubremetz, Marc Loyens |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Trypanosoma rangeli
Trypanosoma cruzi Immunoblotting Molecular Sequence Data Immunology Protozoan Proteins Fluorescent Antibody Technique Antigens Protozoan Organelle Animals Parasite hosting Leishmania major Microscopy Immunoelectron Glutathione Transferase Organelles Base Sequence biology General Medicine Immunogold labelling Blotting Northern biology.organism_classification Molecular biology Infectious Diseases Biochemistry Cytoplasm Ultrastructure Parasitology Biomarkers |
| Zdroj: | Experimental Parasitology. 81:453-461 |
| ISSN: | 0014-4894 |
| Popis: | We have previously isolated and characterized a Trypanosoma cruzi cDNA encoding a polypeptide with a molecular mass of 52 kDa (Tc52) sharing significant homology to glutathione S-transferase. In the present study, by molecular and immunological approaches, we showed that Tc52 is preferentially expressed by dividing forms of the parasite: (e.g., epimatigotes and amastigotes). Moreover, we could identify the reactive antigen in different T. cruzi strains. A different pattern of reactivity on immunoblots was observed in the case of Trypanosoma rangeli. Furthermore, immunofluorescence assays using T. cruzi epimastigote culture forms revealed that the reactive antigen is localized within cytoplasmic organelles morphologically ressembling the structures previously designated as the reservosome found mostly at the posterior end of the parasite. Furthermore, the antibodies did not react against trypomastigotes which emerged from infected fibroblasts, whereas amastigotes showed polar fluorescence. Immunogold labeling and electron micrographs further revealed that the Tc52 protein is mainly associated with organelles composed of a large network of multivesicular structures, the latter being more abundant in epimastigotes. Taken together, these results demonstrated that Tc52 is associated with organelles composed of a multivesicular network and appears to be developmentally regulated, being fully expressed by parasite dividing forms. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect