Export of virulence proteins by malaria-infected erythrocytes involves remodelling of host actin cytoskeleton
Publication Year 2014-08-19, Volume 124, Issue #23, Page 3459-68
Journal Title
Publication Type
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
WEHI Research Division(s)
Infection And Immunity
NHMRC Grants
NHMRC/1011453 NHMRC/637406
Rights Notice
Copyright © 2014 by American Society of Hematology

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