New insights into molecular mechanisms of phagocytosis in Entamoeba histolytica by proteomic analysis.

The protozoan parasite Entamoeba histolytica ingests microorganisms and mammalian cells. Phagocytosis is essential for cell growth and is implicated in pathogenesis of E. histolytica. Phagocytosis consists of a number of steps including recognition of and binding to ligands on the target cells via a galactose/N-acetylgalactosamine-specific lectin, activation of a signaling pathway leading to cytoskeletal reorganization, and vesicle trafficking, all of which play distinct but coordinated roles in phagocytosis. Recent studies of proteomic analysis of purified phagosomes or affinity-purified Gal/GalNAc-binding proteins using reversed phase capillary liquid chromatography and ion trap tandem mass spectrometry enabled high throughput identification of proteins involved in phagosome biogenesis. These studies provided a list of proteins involved in the pathway and also shed light on the dynamic process of phagosome maturation. These approaches should provide significant insights into molecular mechanisms of phagosome biogenesis and help to elucidate the pathogenesis of this important parasite.