Immunolocalization of two hydrogenosomal enzymes of Trichomonas vaginalis.
Three monoclonal antibodies specific for malic enzyme and for the alpha- and beta-subunits, respectively, of the succinyl-coenzyme A (CoA) synthetase of Trichomonas vaginalis were used to immunolocalize these proteins in the cell. All antibodies labeled the hydrogenosome matrix as determined both by immunofluorescence and by immunogold staining. There was no labeling on the cell surface or in any other cell compartment. These results support the idea that these proteins are restricted to a hydrogenosomal function and do not play a role as adhesins at the plasma membrane surface.
Brugerolle
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Biologie des Protistes, UPRESA 6023, Université Blaise Pascal de Clermont-Ferrand, Aubiere, France. brugerolle@cicsun.univ-bpclermont.fr
Bricheux
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Coffe
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D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D005455:Fluorescent Antibody Technique; D007150:Immunohistochemistry; D008291:Malate Dehydrogenase / Q000276:immunology / Q000378:metabolism*; D015388:Organelles / Q000201:enzymology*; D013389:Succinate-CoA Ligases / Q000276:immunology / Q000378:metabolism*; D014246:Trichomonas vaginalis / Q000201:enzymology*
D000911:Antibodies, Monoclonal; D008291:Malate Dehydrogenase; D013389:Succinate-CoA Ligases