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Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives

Published online by Cambridge University Press:  25 March 2014

E.-R. PESCE*
Affiliation:
College of Health and Biomedicine, Victoria University, Melbourne, Victoria 8001, Australia
G. L. BLATCH*
Affiliation:
College of Health and Biomedicine, Victoria University, Melbourne, Victoria 8001, Australia
*
*Corresponding authors: College of Health and Biomedicine, Victoria University, Melbourne 8001, Victoria, Australia. E-mail: Gregory.Blatch@vu.edu.au and Eva-Rachele.Pesce@vu.edu.au
*Corresponding authors: College of Health and Biomedicine, Victoria University, Melbourne 8001, Victoria, Australia. E-mail: Gregory.Blatch@vu.edu.au and Eva-Rachele.Pesce@vu.edu.au

Summary

Plasmodium falciparum displays a large and remarkable variety of heat shock protein 40 family members (PfHsp40s). The majority of the PfHsp40s are poorly characterized, and although the functions of some of them have been suggested, their exact mechanism of action is still elusive and their interacting partners and client proteins are unknown. The P. falciparum heat shock protein 70 family members (PfHsp70s) have been more extensively characterized than the PfHsp40s, with certain members shown to function as molecular chaperones. However, little is known about the PfHsp70-PfHsp40 chaperone partnerships. There is mounting evidence that these chaperones are important not only in protein homoeostasis and cytoprotection, but also in protein trafficking across the parasitophorous vacuole (PV) and into the infected erythrocyte. We propose that certain members of these chaperone families work together to maintain exported proteins in an unfolded state until they reach their final destination. In this review, we critically evaluate what is known and not known about PfHsp40s and PfHsp70s.

Type
Special Issue Article
Copyright
Copyright © Cambridge University Press 2014 

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