Golgi apparatus components in Entamoeba histolytica and Entamoeba dispar after monensin treatment

Highly dynamic ribosomes, glycogen granules, thinly fibrillar material, and multiple membrane‐bound vesicles are embedded in the matrix‐rich cytoplasm of Entamoeba spp. trophozoites. The absence of a Golgi apparatus in these amoebae has been commonly accepted. Here we challenge this observation by incubating Entamoeba histolytica and Entamoeba dispar with monensin, an ionophore that produces swelling of the Golgi apparatus. We observe changes in the trophozoites through standard transmission electron microscopy, cryofixation and cryosubstitution, and analyze the label and expression of known resident proteins of the cis‐GM130 and trans‐TGN38 Golgi network through confocal microscopy and Western blot assays. Cryosubstitution and standard methods using the treatment, preserved membranous lamellae resembling Golgi components. GM130 and TGN38 Golgi antigens were found by immunoelectron, immunoblot, and co‐localization by confocal microscopy using the reagent NBD C6‐ceramide. Our results indicate that previously undetected Golgi apparatus components are present in the cytoplasm of E. histolytica and E. dispar. Monensin enhances the cytoplasmic cisternae formation in E. histolytica and E. dispar. Golgi apparatus‐like components were shown in amoebae processed by cryosubstitution. NBD‐6 ceramide showed colocalization with Golgi resident proteins in amoebae.