Role of epigenetic processes in controlling the adaptation of Entamoeba histolytica to environmental stresses.
Entamoeba histolytica is an intestinal parasite responsible for amebiasis. Approximately 50 million people have invasive disease annually resulting in 100,000 deaths per year making it the second most common cause of parasitic death in humans. The vegetative stages (trophozoites) of E. histolytica live in the large intestine and form encysted stages (cysts) that are excreted with feces. The trophozoites can penetrate into the intestinal wall and invade the liver and other organs to produce clinical forms of amebosis, most frequently intestinal amebosis and hepatic amebosis (amoebic liver abscess). The infection is transmitted by cysts from one human to another due to transmission of mature cysts with contaminated foods (fruit vegetables), drinking water or fecally contaminated hands. Inside its human host, the parasite is challenged by various stressful conditions that originate in part from the immune system of its human host (like the production of nitric oxide by phagocytes). My laboratory is studying the role of epigenetic processes in controlling the adaptation of the parasite to environmental stresses with an emphasis on Dnmt2 catalyzed DNA/tRNA methylation.
Baumel-Alterzon S, Weber C, Guillén N, Ankri S. Identification of dihydropyrimidine dehydrogenase as a virulence factor essential for the survival of Entamoeba histolytica in glucose-poor environments. Cell Microbiol. 15(1), 130–144. 2013
Katz, S., Kushnir, O., Tovy, A., Siman Tov, R., Ankri, S. The Entamoeba histolytica methylated LINE-binding protein EhMLBP provides protection against heat shock. Cell Microbiol. 2012 14(1), 58-70.
Tovy A, Hertz R, Siman-Tov R, Syan S, Faust D, Guillen N, Ankri S. Glucose starvation boosts Entamoeba histolytica virulence. PLoS Negl Trop Dis., 5(8):e1247. 2011.
Tovy, A., Siman Tov, R., Gaentzsch, R., Helm, M., Ankri, S. A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: The metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity. PLoS PATHOGENS, 6(2):e1000775. 2010.