Coşkun Kübra Açıkalın, Tutar Yusuf
Department of Bioengineering, Faculty of Natural Sciences and Engineering, Gaziosmanpaşa University, Tokat, Turkey.
Division of Biochemistry, Department of Basic Sciences, Faculty of Pharmacy, Cumhuriyet University, Sivas, Turkey.
Exp Parasitol. 2015 Jun;153:91-7. doi: 10.1016/j.exppara.2015.02.007. Epub 2015 Feb 26.
Toxoplasma gondii is an intracellular parasitic protozoon which infects human and most warm-blooded animals. Almost one-third of the world's population is affected by life-threatening infection of T. gondii tachyzoites form. Slow growing, transmissible and encysted bradyzoites forms are composed after tachyzoites stage. Cellular and environmental stresses induce conversion of tachyzoites from bradyzoites and this condition is associated with Heat Shock Protein (Hsps) family. Hsp100 is a member of this protein family, and coordinates to disassemble protein aggregates with Hsp70 and Hsp40 in an ATP dependent manner. Several proteins are involved during this stage differentiation and Hsp100 may help them to be in their native soluble form to perform their function as observed in other organisms. For this purpose, Hsp100-Batu1 was isolated from T. gondii RH strain to characterize its biochemical properties in this current study. Hsp100 proteins play a role in survival and virulence of pathogens as shown in the literature. Therefore, manipulation of protein-protein interaction may perturb T. gondii infection and impair conversion to tachyzoites by inhibiting Hsp100 function. Therefore, results of this work present a potential route for vaccination or immunotherapy.
刚地弓形虫是一种细胞内寄生原生动物，可感染人类和大多数温血动物。世界上近三分之一的人口受到刚地弓形虫速殖子形式的致命感染影响。速殖子阶段之后会形成生长缓慢、具有传染性且包囊化的缓殖子形式。细胞和环境应激会促使速殖子向缓殖子转化，这种情况与热休克蛋白（Hsps）家族有关。Hsp100是该蛋白家族的一员，它以ATP依赖的方式与Hsp70和Hsp40协同作用，拆解蛋白质聚集体。在这一阶段的分化过程中有多种蛋白质参与，正如在其他生物体中观察到的那样，Hsp100可能帮助它们保持天然的可溶形式以发挥其功能。为此，在本研究中从刚地弓形虫RH株中分离出Hsp100 - Batu1以表征其生化特性。如文献所示，Hsp100蛋白在病原体的存活和毒力方面发挥作用。因此，操纵蛋白质 - 蛋白质相互作用可能会干扰刚地弓形虫感染，并通过抑制Hsp100功能来损害其向速殖子的转化。因此，这项工作的结果为疫苗接种或免疫治疗提供了一条潜在途径。
