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An exported kinase family mediates species-specific erythrocyte remodelling and virulence in human malaria

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Davies, Heledd | Belda, Hugo | Broncel, Malgorzata | Ye, Xingda | Bisson, Claudine | Introini, Viola | Dorin-Semblat, Dominique | Semblat, Jean-Philippe | Tibúrcio, Marta | Gamain, Benoit | Kaforou, Myrsini | Treeck, Moritz

Edité par CCSD ; Nature Publishing Group -

International audience. The most severe form of human malaria is caused by Plasmodium falciparum. Its virulence is closely linked to the increase in rigidity of infected erythrocytes and their adhesion to endothelial receptors, obstructing blood flow to vital organs. Unlike other human-infecting Plasmodium species, P. falciparum exports a family of 18 'FIKK' serine/threonine kinases into the host cell, suggesting that phosphorylation may modulate erythrocyte modifications. We reveal substantial species-specific phosphorylation of erythrocyte proteins by P. falciparum, but not by Plasmodium knowlesi, which does not export FIKK kinases. By conditionally deleting all FIKK kinases Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:

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