Publication | Closed Access
Receptor and Ligand Domains for Invasion of Erythrocytes by <i>Plasmodium falciparum</i>
552
Citations
22
References
1994
Year
Signal TransductionBiochemistryRegion IiNatural SciencesG Protein-coupled ReceptorMalariaImmunologyGlycobiologyMolecular BiologyLigand DomainsParasite Plasmodium FalciparumSialic AcidVector-parasite RelationshipMedicineCell SignalingParasite GenomicsPhagocyte
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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