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

Rug, M. et al. (2014) Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton. Blood, 124(3), pp. 3459-3468. (doi: 10.1182/blood-2014-06-583054) (PMID:25139348) (PMCID:PMC4246041)

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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 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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Lemgruber Soares, Dr Leandro
Authors: Rug, M., Cyrklaff, M., Mikkonen, A., Lemgruber Soares, L., Kuelzer, S., Sanchez, C. P., Thompson, J., Hanssen, E., O'Neill, M., Langer, C., Lanzer, M., Frischknecht, F., Maier, A. G., and Cowman, A. F.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Blood
Publisher:American Society of Hematology
ISSN (Online):1528-0020
Copyright Holders:Copyright © 2014 The American Society of Hematology

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