Journal article

The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites

Sarah C Charnaud, Matthew WA Dixon, Catherine Q Nie, Lia Chappell, Paul R Sanders, Thomas Nebl, Eric Hanssen, Matthew Berriman, Jo-Anne Chan, Adam J Blanch, James G Beeson, Julian C Rayner, Jude M Przyborski, Leann Tilley, Brendan S Crabb, Paul R Gilson

PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2017

Abstract

Malaria is caused by five different Plasmodium spp. in humans each of which modifies the host erythrocyte to survive and replicate. The two main causes of malaria, P. falciparum and P. vivax, differ in their ability to cause severe disease, mainly due to differences in the cytoadhesion of infected erythrocytes (IE) in the microvasculature. Cytoadhesion of P. falciparum in the brain leads to a large number of deaths each year and is a consequence of exported parasite proteins, some of which modify the erythrocyte cytoskeleton while others such as PfEMP1 project onto the erythrocyte surface where they bind to endothelial cells. Here we investigate the effects of knocking out an exported Hsp70-..

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