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Chaperones and Proteases of Plasmodium falciparum

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Heat Shock Proteins of Malaria

Abstract

In 2010, there were about 216 million malaria cases and an estimated 655,000 deaths (WHO). With half of the world’s population living in endemic regions, the struggle against this parasite is more salient than ever. Plasmodium falciparum is the causative agent of the most severe form of human malaria. It is known that this parasite experiences large heat shock upon entry to the human host and in the febrile episodes that accompany pathology. Thus, the protein homeostasis machinery composed of chaperones and proteases is expected to play an essential role in parasite survival. However, research on the proteostasis machinery of P. falciparum is still in its infancy. Bioinformatic analyses reveal that the parasite contains a total of about 184 chaperones and proteases. This review will summarize the available biochemical data on the chaperone and proteases and their proposed functions in parasite biology. The following chaperones and proteases are discussed: Hsp90, Hsp70, Hsp40, Hsp60, Hsp10, proteasome, and Clp proteases.

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Acknowledgements

Kaiyin Liu is the recipient of the Ontario Graduate Scholarship. This work was supported by a grant from the Natural Sciences and Engineering Research Council of Canada (RGPIN 238282-2013) to WAH.

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  1. Department of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada

    Kaiyin Liu & Walid A. Houry

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  1. Dept. of Biochemistry and Microbiology, University of Zululand, KwaDlangezwa, South Africa

    Addmore Shonhai

  2. College of Health and Biomedicine, Victoria University, Melbourne, Victoria, Australia

    Gregory L. Blatch

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Liu, K., Houry, W. (2014). Chaperones and Proteases of Plasmodium falciparum . In: Shonhai, A., Blatch, G. (eds) Heat Shock Proteins of Malaria. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-7438-4_9

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