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Blood, 15 May 2005, Vol. 105, No. 10, pp. 4078-4087.
Prepublished online as a Blood First Edition Paper on February 3, 2005; DOI 10.1182/blood-2004-12-4666.
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RED CELLS
Trafficking of the major virulence factor to the surface of transfected P falciparum–infected erythrocytes
Ellen Knuepfer,
Melanie Rug,
Nectarios Klonis,
Leann Tilley, and
Alan F. Cowman
From The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia; and Department of Biochemistry, La Trobe University, Bundoora, Australia.
After invading human red blood cells (RBCs) the malaria parasite Plasmodium falciparum remodels the host cell by trafficking proteins to the RBC compartment. The virulence protein P falciparum erythrocyte membrane protein 1 (PfEMP1) is responsible for cytoadherence of infected cells to host endothelial receptors. This protein is exported across the parasite plasma membrane and parasitophorous vacuole membrane and inserted into the RBC membrane. We have used green fluorescent protein chimeras and fluorescence photobleaching experiments to follow PfEMP1 export through the infected RBC. Our data show that a knob-associated histidine-rich protein (KAHRP) N-terminal protein export element appended to the PfEMP1 transmembrane and C-terminal domains was sufficient for efficient trafficking of protein domains to the outside of the P falciparum–infected RBC. The physical state of the exported proteins suggests trafficking as a complex rather than in vesicles and supports the hypothesis that endogenous PfEMP1 is trafficked in a similar manner. This study identifies the sequences required for expression of proteins to the outside of the P falciparum–infected RBC membrane.
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