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Band 3 Is a Host Receptor Binding Merozoite Surface Protein 1 during the Plasmodium falciparum Invasion of Erythrocytes
Vikas K. Goel, Xuerong Li, Huiqing Chen, Shih-Chun Liu, Athar H. Chishti and Steven S. Oh
Proceedings of the National Academy of Sciences of the United States of America
Vol. 100, No. 9 (Apr. 29, 2003), pp. 5164-5169
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3139683
Page Count: 6
You can always find the topics here!Topics: Merozoites, Parasites, Receptors, Erythrocyte invasion, Proteins, Antibodies, Yeasts, Western blotting, Erythrocytes, Amino acids
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We report the molecular identification of a sialic acid-independent host-parasite interaction in the Plasmodium falciparum malaria parasite invasion of RBCs. Two nonglycosylated exofacial regions of human band 3 in the RBC membrane were identified as a crucial host receptor binding the C-terminal processing products of merozoite surface protein 1 (MSP1). Peptides derived from the receptor region of band 3 inhibited the invasion of RBCs by P. falciparum. A major segment of the band 3 receptor (5ABC) bound to native MSP142 and blocked the interaction of native MSP142 with intact RBCs in vitro. Recombinant MSP119 (the C-terminal domain of MSP142) bound to 5ABC as well as RBCs. The binding of both native MSP142 and recombinant MSP119 was not affected by the neuraminidase treatment of RBCs, but sensitive to chymotrypsin treatment. In addition, recombinant MSP138 showed similar interactions with the band 3 receptor and RBCs, although the interaction was relatively weak. These findings suggest that the chymotrypsin-sensitive MSP1-band 3 interaction plays a role in a sialic acid-independent invasion pathway and reveal the function of MSP1 in the Plasmodium invasion of RBCs.
Proceedings of the National Academy of Sciences of the United States of America © 2003 National Academy of Sciences