First molecular characterisation of hydrogenosomes in the protozoan parasite Histomonas meleagridis
| Autor: | Christian P. Vivarès, Muriel Mazet, John F. Alderete, Frédéric Delbac, Marie Diogon |
|---|---|
| Přispěvatelé: | Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Université d'Auvergne - Clermont-Ferrand I (UdA), Department of Microbiology, Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Iron-Sulfur Proteins
MESH: Trichomonas vaginalis MESH: Malate Dehydrogenase MESH: Sequence Homology Amino Acid Hydrogenosome Genes Protozoan Fluorescent Antibody Technique MESH: Trichomonas MESH: Amino Acid Sequence MESH: Base Sequence medicine.disease_cause Histomonas meleagridis Malate Dehydrogenase Succinate-CoA Ligases MESH: Animals MESH: Fluorescent Antibody Technique MESH: Succinate-CoA Ligases 0303 health sciences Malic enzyme MESH: Hydrogen Immunohistochemistry 3. Good health Infectious Diseases [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Biochemistry MESH: Genes Protozoan MESH: Hydrogenase Trichomonas Iron-hydrogenase Immunoelectron microscopy Molecular Sequence Data α-Succinyl coenzyme A synthetase MESH: Sequence Alignment Biology MESH: Cell Adhesion 03 medical and health sciences Hydrogenase medicine Trichomonas vaginalis Animals Amino Acid Sequence 030304 developmental biology Antiserum Organelles MESH: Molecular Sequence Data Base Sequence Sequence Homology Amino Acid 030306 microbiology Cell adhesion Blackhead disease MESH: Immunohistochemistry MESH: Iron-Sulfur Proteins medicine.disease biology.organism_classification Cytoplasm Polyclonal antibodies biology.protein Parasitology Sequence Alignment Hydrogen MESH: Organelles |
| Zdroj: | International Journal for Parasitology International Journal for Parasitology, Elsevier, 2008, 38 (2), pp.177-90. ⟨10.1016/j.ijpara.2007.06.006⟩ International Journal for Parasitology, 2008, 38 (2), pp.177-90. ⟨10.1016/j.ijpara.2007.06.006⟩ |
| ISSN: | 0020-7519 |
| DOI: | 10.1016/j.ijpara.2007.06.006⟩ |
| Popis: | International audience; Histomonas meleagridis is a trichomonad species that undergoes a flagellate-to-amoeba transformation during tissue invasion and causes a serious disease in gallinaceous birds (blackhead disease or histomoniasis). Living in the avian cecum, the flagellated form can be grown in vitro in the presence of an ill-defined bacterial flora. Its cytoplasm harbours numerous spherical bodies which structurally resemble hydrogenosomes. To test whether these organelles may be involved in anaerobic metabolism, we undertook the identification of H. meleagridis genes encoding some potentially conserved hydrogenosomal enzymes. The strategy was based on several PCR amplification steps using primers designed from available sequences of the phylogenetically-related human parasite Trichomonas vaginalis. We first obtained a C-terminal sequence of an iron-hydrogenase homologue (Hm_HYD) with typical active site signatures (H-cluster domain). Immunoelectron microscopy with anti-Hm_HYD polyclonal antibodies showed specific gold labelling of electron-dense organelles, thus confirming their hydrogenosomal nature. The whole genes encoding a malic enzyme (Hm_ME) and the alpha-subunit of a succinyl coenzyme A synthetase (Hm_alpha-SCS) were then identified. Short N-terminal presequences for hydrogenosomal targeting were predicted in both proteins. Anti-Hm_ME and anti-Hm_alpha-SCS antisera provided immunofluorescence staining patterns of H. meleagridis cytoplasmic granules similar to those observed with anti-Hm_HYD antiserum or mAb F5.2 known to react with T. vaginalis hydrogenosomes. Hm_ME, Hm_alpha-SCS and Hm_HYD were also detected as reactive bands on immunoblots of proteins from purified hydrogenosomes. Interestingly, anti-Hm_alpha-SCS staining of the cell surface in non-permeabilised parasites suggests a supplementary role for SCS in cytoadherence, as previously demonstrated in T. vaginalis. |
| Databáze: | OpenAIRE |
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