Singh Meetali, Sharma Shalini, Bhattacharya Alok, Tatu Utpal
Department of Biochemistry, Indian Institute of Science Bangalore, India.
School of Life Sciences, Jawaharlal Nehru University New Delhi, India.
Front Microbiol. 2015 Oct 13;6:1125. doi: 10.3389/fmicb.2015.01125. eCollection 2015.
Enteric protozoan Entamoeba histolytica is a major cause of debilitating diarrheal infection worldwide with high morbidity and mortality. Even though the clinical burden of this parasite is very high, this infection is categorized as a neglected disease. Parasite is transmitted through feco-oral route and exhibit two distinct stages namely - trophozoites and cysts. Mechanism and regulation of encystation is not clearly understood. Previous studies have established the role of Heat shock protein 90 (Hsp90) in regulating stage transition in various protozoan parasites like Giardia, Plasmodium, Leishmania, and Toxoplasma. Our study for the first time reports that Hsp90 plays a crucial role in life cycle of Entamoeba as well. We identify Hsp90 to be a negative regulator of encystation in Entamoeba. We also show that Hsp90 inhibition interferes with the process of phagocytosis in Entamoeba. Overall, we show that Hsp90 plays an important role in virulence and transmission of Entamoeba.
肠道原生动物溶组织内阿米巴是全球范围内导致使人虚弱的腹泻感染的主要原因，发病率和死亡率都很高。尽管这种寄生虫造成的临床负担非常大，但这种感染仍被归类为被忽视的疾病。该寄生虫通过粪口途径传播，呈现出两种不同的阶段，即滋养体和包囊。包囊形成的机制和调控尚未完全清楚。先前的研究已经证实热休克蛋白90（Hsp90）在调节贾第虫、疟原虫、利什曼原虫和弓形虫等各种原生动物寄生虫的阶段转变中发挥作用。我们的研究首次报道Hsp90在溶组织内阿米巴的生命周期中也起着关键作用。我们确定Hsp90是溶组织内阿米巴包囊形成的负调节因子。我们还表明，抑制Hsp90会干扰溶组织内阿米巴的吞噬过程。总体而言，我们证明Hsp90在溶组织内阿米巴的毒力和传播中发挥重要作用。
