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Science 24 June 1994:
Vol. 264. no. 5167, pp. 1941 - 1944
DOI: 10.1126/science.8009226
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Articles

Science, Vol 264, Issue 5167, 1941-1944
Copyright © 1994 by American Association for the Advancement of Science

articles

Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum

BK Sim, CE Chitnis, K Wasniowska, TJ Hadley, and LH Miller

Laboratory of Malaria Research, National Institutes of Health, Bethesda, MD 20892.

A 175-kilodalton erythrocyte binding protein, EBA-175, of the parasite Plasmodium falciparum mediates the invasion of erythrocytes. The erythrocyte receptor for EBA-175 is dependent on sialic acid. The domain of EBA-175 that binds erythrocytes was identified as region II with the use of truncated portions of EBA-175 expressed on COS cells. Region II, which contains a cysteine-rich motif, and native EBA-175 bind specifically to glycophorin A, but not to glycophorin B, on the erythrocyte membrane. Erythrocyte recognition of EBA-175 requires both sialic acid and the peptide backbone of glycophorin A. The identification of both the receptor and ligand domains may suggest rational designs for receptor blockade and vaccines.


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