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.
Keywords: Antimalarials; Heat shock proteins; Malaria; Plasmodium falciparum.
© 2021. The Author(s), under exclusive license to Springer Nature Switzerland AG.