Receptor and Ligand Domains for Invasion of Erythrocytes by Plasmodium falciparum
BKL Sim, CE Chitnis, K Wasniowska, TJ Hadley… - Science, 1994 - science.org
BKL Sim, CE Chitnis, K Wasniowska, TJ Hadley, LH Miller
Science, 1994•science.orgA 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 …
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 …
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.
