Journal article

Trafficking of the exported P. falciparum chaperone PfHsp70x

Manuel Rhiel, Verena Bittl, Anke Tribensky, Sarah C Charnaud, Maja Strecker, Sebastian Mueller, Michael Lanzer, Cecilia Sanchez, Christine Schaeffer-Reiss, Benoit Westermann, Brendan S Crabb, Paul R Gilson, Simone Kuelzer, Jude M Przyborski

SCIENTIFIC REPORTS | NATURE PUBLISHING GROUP | Published : 2016

Abstract

Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transp..

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Grants

Awarded by German Research Council


Funding Acknowledgements

We wish to thank Lars-Oliver Essen for enlightening discussions and Jorg Kahnt for help with proteomic analyses. Work in the Przyborski lab is supported by the SPP1580, German Research Council (PR1099/3-2). SK was supported by a post-doctoral fellowship from the German Research Council. This manuscript is dedicated to the memory of Klaus Lingelbach (1955-2015) who was one of the first to study protein traffic in this system.