Research Publications


Export of virulence proteins by malaria-infected erythrocytes involves remodelling of host actin cytoskeleton

Rug, M; Cyrklaff, M; Mikkonen, A; Lemgruber, L; Kuelzer, S; Sanchez, CP; Thompson, J; Hanssen, E; O'Neill, M; Langer, C; Lanzer, M; Frischknecht, F; Maier, AG; Cowman, AF
Journal Article
Following invasion of human red blood cells (RBC) by the malaria parasite, Plasmodium falciparum, a remarkable process of remodelling 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's clefts are organelles essential for protein trafficking, sorting and assembly of protein complexes. Here we demonstrate that disruption of PfPTP1 (PfEMP1 trafficking protein 1) function leads to severe alterations in the architecture of Maurer's clefts. Furthermore, two major surface antigen families, PfEMP1 and STEVOR, are no longer displayed on the host cell surface leading to ablation of cytoadherence to host receptors. PfPTP1 functions in a large complex of proteins and is required for linking of Maurer's clefts to the host actin cytoskeleton.
American Society of Hematology
Infection and Immunity
Refer to article for additional funding acknowledgements
Copyright © 2014 by American Society of Hematology

Creation Date 2014-09-12 02:01:45 Last Modified 2014-12-10 03:44:57