RESUMO
Though both Entamoeba histolytica and E. dispar colonize the human gut, only the former is capable of invading tissues and causing disease. Although the biology of the parasite and the mechanism of pathogenesis have been intensively studied, there is a lack of consensus about the molecules of E. histolytica that actively participate in pathogenesis. This article reviews some key molecules involved. Ga1NAc-inhibitable adhesin is a membrane-associated glycoprotein nature, consisting of heavy and light subunits; each of these is encoded by multiple genes. The heavy subunit is useful in differentiating E. histolytica from E. dispar. Three structurally similar isoforms of amebapore, A, B and C, have been identified in E. histolytica but C is absent in E. dispar. Proteolytic enzymes such as collagenase and cysteine proteinases and cytolytic enzymes like phospholipase A are important. Collagenase activity is mainly accumulated in electron-dense granules. Cysteine proteinase is encoded by six genes, of which EhCP5 is exclusively present in E. histolytica.