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J. Biol. Chem., Vol. 282, Issue 37, 26754-26758, September 14, 2007

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Plasmodium falciparum Erythrocyte Membrane Protein 3 (PfEMP3) Destabilizes Erythrocyte Membrane Skeleton^*

Xinhong Pei, Xinhua Guo, Ross Coppel, Narla Mohandas, and Xiuli An¹

From the Red Cell Physiology Laboratory, New York Blood Center, New York, New York 10065 and Department of Microbiology, Monash University, Monash, Victoria 3800, Australia

Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) is a parasite-derived protein that appears on the cytoplasmic surface of the host cell membrane in the later stages of the parasite's development where it associates with membrane skeleton. We have recently demonstrated that a 60-residue fragment (FIa1, residues 38–97) of PfEMP3 bound to spectrin. Here we show that this polypeptide binds specifically to a site near the C terminus of -spectrin at the point that spectrin attaches to actin and protein 4.1R in forming the junctions of the membrane skeletal network. We further show that this polypeptide disrupts formation of the ternary spectrin-actin-4.1R complex in solution. Importantly, when incorporated into the cell, the PfEMP3 fragment causes extensive reduction in shear resistance of the cell. We conjecture that the loss of mechanical cohesion of the membrane may facilitate the exit of the mature merozoites from the cell.

Received for publication, February 23, 2007 , and in revised form, May 16, 2007.

^* This work was supported in part by National Institutes of Health Grants DK 26263 and DK 32094 and the National Health and Medical Research Council of Australia. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Red Cell Physiology Laboratory, 310 E. 67th St., New York, NY 10021. Tel.: 212-570-3247; Fax: 212-570-3195; E-mail: xan{at}nybloodcenter.org.

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