Journal article

Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte

Simone Kuelzer, Sarah Charnaud, Tal Dagan, Jan Riedel, Pradipta Mandal, Eva R Pesce, Gregory L Blatch, Brendan S Crabb, Paul R Gilson, Jude M Przyborski

Cellular Microbiology | WILEY | Published : 2012

Abstract

Malaria parasites modify their host cell, the mature human erythrocyte. We are interested in the molecules mediating these processes, and have recently described a family of parasite-encoded heat shock proteins (PfHsp40s) that are targeted to the host cell, and implicated in host cell modification. Hsp40s generally function as co-chaperones of members of the Hsp70 family, and until now it was thought that human Hsp70 acts as the PfHsp40 interaction partner within the host cell. Here we revise this hypothesis, and identify and characterize an exported parasite-encoded Hsp70, referred to as PfHsp70-x. PfHsp70-x is exported to the host erythrocyte where it forms a complex with PfHsp40s in struc..

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Grants

Awarded by DFG


Funding Acknowledgements

We particularly wish to thank Ulrike Boehme and the Pathogen Sequencing Unit at the Sanger Centre for their help with sequence analysis. Kerstin Maas-Enriquez provided excellent technical assistance and Addmore Shonhai assisted in choice of PfHsp70x sequences for immunization. We furthermore thank Rowan Hatherley for assistance with preparation of r70x and Alan Cowman for the gift of anti-ATS monoclonal antibodies. This work was supported by DFG project PR1099/3-1 (SPP1580, J. M. P.), and by the Australian NHMRC (B. S. C.). The authors gratefully acknowledge the contribution to this work of the Victorian Operational Infrastructure Support Program. We thank the Australian Red Cross Blood Bank for the provision of human blood and serum. S. C. is supported by a Monash Graduate Scholarship, and gratefully acknowledges funding from OzEMalaR Researcher Exchange and the Australian Society of Parasitology.