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The protozoan intestinal parasite  Entamoeba histolytica  infects millions of people worldwide and is capable of causing amebic dysentery and amebic liver abscess. The closely related species  Entamoeba dispar  colonizes many more individuals, but this organism does not induce disease. To identify molecular differences between these two organisms that may account for their differential ability to cause disease in humans, we used two-dimensional gel-based (DIGE) proteomic analysis to compare whole cell lysates of  E. histolytica  and  E. dispar . We observed 141 spots expressed at a substantially (>5-fold) higher level in  E. histolytica  HM-1∶IMSS than  E. dispar  and 189 spots showing the opposite pattern. Strikingly, 3 of 4 proteins consistently identified as different at a greater than 5-fold level between  E. histolytica  HM-1∶IMSS and  E. dispar  were identical to proteins recently identified as differentially expressed between  E. histolytica  HM-1∶IMSS and the reduced virulence strain  E. histolytica  Rahman. One of these was  E. histolytica  alcohol dehydrogenase 3 (EhADH3). We found that  E. histolytica  possesses a higher level of NADP-dependent alcohol dehydrogenase activity than  E. dispar  and that some EhADH3 can be localized to the surface of  E. histolytica . Episomal overexpression of EhADH3 in  E. histolytica  trophozoites resulted in only subtle phenotypic differences in  E. histolytica  virulence in animal models of amebic colitis and amebic liver abscess, making it difficult to directly link EhADH3 levels to virulence differences between  E. histolytica  and less-pathogenic  Entamoeba .

Proteomic Comparison of Entamoeba histolytica and Entamoeba dispar and the Role of E. histolytica Alcohol Dehydrogenase 3 in Virulence