Protein Sumoylation Is Crucial for Phagocytosis in Entamoeba histolytica Trophozoites

Posttranslational modifications provide Entamoeba histolytica proteins the timing and signaling to intervene during different processes, such as phagocytosis. However, SUMOylation has not been studied in E. yet. Here, we characterized SUMO gene, its product (EhSUMO), relevance of Our results indicated that EhSUMO an extended N-terminus differentiates from ubiquitin. It also presents GG residues at C-terminus ?KXE/D binding motif, both involved target protein contact. Additionally, genome possesses enzymes belonging SUMOylation-deSUMOylation machinery. Confocal microscopy assays disclosed a remarkable membrane activity with convoluted changing structures trophozoites erythrophagocytosis. SUMOylated appeared pseudopodia, phagocytic channels, around adhered ingested erythrocytes. Docking analysis predicted interaction EhADH (an ALIX family protein), immunoprecipitation immunofluorescence revealed association increased phagocytosis; whereas EhVps32 (a ESCRT-III complex)-EhSUMO stronger since basal conditions. In knocked-down trophozoites, bizarre membranous disappeared, diminished. evidenced presence gene This is supported by bioinformatics screening many other phagocytosis, which present putative sites motif.