Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Departments of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, Canada.
Adv Exp Med Biol. 2021;1340:125-139. doi: 10.1007/978-3-030-78397-6_5.
Studies in mammalian and yeast chaperone systems have significantly advanced our understanding of the biochemistry of heat shock protein 90 (Hsp90), particularly as it pertains to structural details, interaction regulation, and function. Harnessing this body of knowledge, parasitologists have made tremendous steps in understanding the role of the Hsp90 chaperone machine in protozoal parasites, especially in malaria. Heat shock proteins are a crucial part of the signaling events involved in malaria parasite acclimatization in the host. Even though studies of the role of Hsp90 in malaria have been thorough and discovered some of the most intricate details of the utility of the Hsp90 interactome for pathogen-host interactions, the full and elaborate extent of the role of Hsp90 homologs in malaria remains to be uncovered. This chapter discusses the current knowledge about the biochemistry and cellular role of Hsp90 in Plasmodium falciparum malaria. In addition, the involvement of both parasitic and host Hsp90s by the parasite in the infected cell is discussed.
哺乳动物和酵母伴侣系统的研究极大地促进了我们对热休克蛋白 90（Hsp90）的生物化学的理解，特别是在结构细节、相互作用调节和功能方面。寄生虫学家利用这方面的知识，在理解 Hsp90 伴侣机器在原生动物寄生虫中的作用方面取得了巨大的进展，特别是在疟疾方面。热休克蛋白是疟疾寄生虫在宿主中适应过程中所涉及的信号事件的关键部分。尽管 Hsp90 在疟疾中的作用的研究已经很彻底，并发现了 Hsp90 相互作用组在病原体-宿主相互作用中的一些最复杂的细节，但 Hsp90 同源物在疟疾中的作用的完整和详细程度仍有待揭示。本章讨论了 Hsp90 在恶性疟原虫疟疾中的生物化学和细胞作用的现有知识。此外，还讨论了寄生虫和宿主 Hsp90 参与感染细胞中的寄生虫。
