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Blood, 15 November 2001, Vol. 98, No. 10, pp. 3132-3135
RED CELLS
Plasmodium falciparum erythrocyte membrane protein 1 functions as a ligand for P-selectin
Anna M. Senczuk,
John C. Reeder,
Magda M. Kosmala, and
May Ho
From the Department of Microbiology and Infectious
Diseases and Immunology Research Group, University of Calgary, Calgary,
Alberta, Canada; the Division of Infection and Immunity, The Walter and
Eliza Hall of Medical Research, Melbourne, Victoria, Australia.
The malarial protein Plasmodium falciparum erythrocyte
membrane protein 1 (PfEMP1) is a parasite protein that is exported to
the surface of the infected erythrocyte, where it is inserted into the
red cell cytoskeleton in the second half of the parasite life cycle.
The surface expression of PfEMP1 coincides with the occurrence of the
adhesion of infected erythrocytes to vascular endothelium. This protein
has been shown to interact with CD36, intercellular adhesion molecule-1
(ICAM-1) and chondroitin sulfate A (CSA). In this study, it is
demonstrated by affinity purification and western blot analysis that
PfEMP1 also functions as a cell surface ligand for P-selectin, an
adhesion molecule that has been shown to mediate the rolling of
infected erythrocytes under physiologic flow conditions, leading to a
significant increase in adhesion to CD36 on activated platelets and
microvascular endothelium.
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