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While Hsp90 has been extensively studied in many prokaryotic and higher eukaryotic model organisms, its structural, functional, and biological properties in parasitic protozoans are less well defined. Hsp90 collaborates with a wide range of co-chaperones that fine-tune its protein folding pathway. Co-chaperones play many roles in the regulation of Hsp90, including selective targeting of client proteins, and the modulation of its ATPase activity, conformational changes, and post-translational modifications. Plasmodium falciparum is responsible for the most lethal form of human malaria. The survival of the malaria parasite inside the host and the vector depends on the action of molecular chaperones. The major cytosolic P. falciparum Hsp90 (PfHsp90) is known to play an essential role in the development of the parasite, particularly during the intra-erythrocytic stage in the human host. Although PfHsp90 shares significant sequence and structural similarity with human Hsp90, it has several major structural and functional differences. Furthermore, its co-chaperone network appears to be substantially different to that of the human host, with the potential absence of a key homolog. Indeed, PfHsp90 and its interface with co-chaperones represent potential drug targets for antimalarial drug discovery. In this review, we critically summarize the current understanding of the properties of Hsp90, and the associated co-chaperones of the malaria parasite.<\/jats:p>","DOI":"10.3390\/biom12081018","type":"journal-article","created":{"date-parts":[[2022,7,22]],"date-time":"2022-07-22T12:53:45Z","timestamp":1658494425000},"page":"1018","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Hsp90 and Associated Co-Chaperones of the Malaria Parasite"],"prefix":"10.3390","volume":"12","author":[{"given":"Tanima","family":"Dutta","sequence":"first","affiliation":[{"name":"The Vice Chancellery, The University of Notre Dame Australia, Fremantle, WA 6160, Australia"},{"name":"The Institute of Immunology and Infectious Diseases, Murdoch University, Perth, WA 6150, Australia"},{"name":"PathWest Nedlands, QEII Medical Centre, Perth, WA 6009, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harpreet","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Bioinformatics, Hans Raj Mahila Maha Vidyalaya, Jalandhar 144008, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3615-6651","authenticated-orcid":false,"given":"Adrienne L","family":"Edkins","sequence":"additional","affiliation":[{"name":"Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0778-8577","authenticated-orcid":false,"given":"Gregory L","family":"Blatch","sequence":"additional","affiliation":[{"name":"The Vice Chancellery, The University of Notre Dame Australia, Fremantle, WA 6160, Australia"},{"name":"The Institute of Immunology and Infectious Diseases, Murdoch University, Perth, WA 6150, Australia"},{"name":"Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa"},{"name":"Biomedical Research and Drug Discovery Research Group, Faculty of Health Sciences, Higher Colleges of Technology, Sharjah P.O. 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