Blatch Gregory L
The Vice Chancellery, The University of Notre Dame Australia, Fremantle, WA, Australia.
Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa.
Front Cell Dev Biol. 2022 May 16;10:921739. doi: 10.3389/fcell.2022.921739. eCollection 2022.
is a unicellular protozoan parasite and causative agent of the most severe form of malaria in humans. The malaria parasite has had to develop sophisticated mechanisms to preserve its proteome under the changing stressful conditions it confronts, particularly when it invades host erythrocytes. Heat shock proteins, especially those that function as molecular chaperones, play a key role in protein homeostasis (proteostasis) of . Soon after invading erythrocytes, the malaria parasite exports a large number of proteins including chaperones, which are responsible for remodeling the infected erythrocyte to enable its survival and pathogenesis. The infected host cell has parasite-resident and erythrocyte-resident chaperones, which appear to play a vital role in the folding and functioning of proteins and potentially host proteins. This review critiques the current understanding of how the major chaperones, particularly the Hsp70 and Hsp40 (or J domain proteins, JDPs) families, contribute to proteostasis of the malaria parasite-infected erythrocytes.
是一种单细胞原生动物寄生虫，也是人类最严重疟疾形式的病原体。疟原虫必须发展出复杂的机制，以便在其面临的不断变化的应激条件下维持其蛋白质组，特别是当它侵入宿主红细胞时。热休克蛋白，尤其是那些作为分子伴侣发挥作用的热休克蛋白，在疟原虫的蛋白质稳态（蛋白质平衡）中起关键作用。疟原虫侵入红细胞后不久，就会输出大量包括伴侣蛋白在内的蛋白质，这些蛋白质负责重塑被感染的红细胞，以使其存活和致病。被感染的宿主细胞有寄生虫驻留和红细胞驻留的伴侣蛋白，它们似乎在疟原虫蛋白质以及潜在的宿主蛋白质的折叠和功能发挥中起着至关重要的作用。本综述对目前关于主要伴侣蛋白，特别是Hsp70和Hsp40（或J结构域蛋白，JDPs）家族如何促进疟原虫感染红细胞的蛋白质平衡的理解进行了批判。
