Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton
Melanie Rug, Marek Cyrklaff, Antti Mikkonen, Leandro Lemgruber, Simone Kuelzer, Cecilia P Sanchez, Jennifer Thompson, Eric Hanssen, Matthew O'Neill, Christine Langer, Michael Lanzer, Friedrich Frischknecht, Alexander G Maier, Alan F Cowman
Blood | AMER SOC HEMATOLOGY | Published : 2014
Following invasion of human red blood cells (RBCs) by the malaria parasite, Plasmodium falciparum, a remarkable process of remodeling occurs in the host cell mediated by trafficking of several hundred effector proteins to the RBC compartment. The exported virulence protein, P falciparum erythrocyte membrane protein 1 (PfEMP1), is responsible for cytoadherence of infected cells to host endothelial receptors. Maurer clefts are organelles essential for protein trafficking, sorting, and assembly of protein complexes. Here we demonstrate that disruption of PfEMP1 trafficking protein 1 (PfPTP1) function leads to severe alterations in the architecture of Maurer's clefts. Furthermore, 2 major surfac..View full abstract
Awarded by National Health and Medical Research Council (NHMRC)
Awarded by Bill and Melinda Gates grant
This work was supported by the National Health and Medical Research Council (NHMRC; grant numbers: 1011453 and 637406), Victorian State Government Operational Infrastructure Support, and Australian Government NHMRC IRIISS. M.C. was supported by a Bill and Melinda Gates grant (Grand Challenges Explorations: OPP1069409); L.L. by a postdoctoral fellowship from the University of Heidelberg Cluster of Excellence CellNetworks; F.F. by the Chica and Heinz Schaller Foundation; and S.K. by a postdoctoral fellowship from the Deutsche Forschungsgemeinschaft.A.G.M. is an Australian Research Fellow supported by the Australian Research Council and A.F.C. is a Howard Hughes International Scholar.