Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl).

Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl) Short title: GPC is the receptor for PfEBP-2

The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL.

Plasmodium vivax uses a single member of the Duffy binding-like (DBL) receptor family to invade erythrocytes and is not found in West Africa where its erythrocyte ligand, the Duffy blood group antigen, is missing. In contrast, Plasmodium falciparum expresses four members of the DBL family, and remarkably, single-point mutations of two of these receptors (BAEBL and JESEBL) bind to entirely diffe...

Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175.

A member of a Plasmodium receptor family for erythrocyte invasion was identified on chromosome 13 from the Plasmodium falciparum genome sequence of the Sanger Centre (Cambridge, U.K.). The protein (named BAEBL) has homology to EBA-175, a P. falciparum receptor that binds specifically to sialic acid and the peptide backbone of glycophorin A on erythrocytes. Both EBA-175 and BAEBL localize to the...

Polymorphisms in erythrocyte binding antigens 140 and 181 affect function and binding but not receptor specificity in Plasmodium falciparum.

Invasion of human erythrocytes by the malaria parasite Plasmodium falciparum utilizes multiple ligand-receptor interactions involving erythrocyte receptors and parasite erythrocyte binding proteins of the Duffy binding-like family. Erythrocyte binding antigen 175 (EBA-175) binds to glycophorin A, the most abundant protein on the human erythrocyte surface and EBA-140 (also known as BAEBL) binds ...

Host Erythrocyte Engagement by PfEBA-140 1 Molecular Basis for Sialic Acid-dependent Receptor Recognition by Plasmodium falciparum Erythrocyte Binding Antigen 140/BAEBL

Background: PfEBA-140 recognizes sialic acid on its receptor Glycophorin C during erythrocyte invasion. Results: PfEBA-140 contains two sialic acid binding pockets distinct from other sialic acid binding proteins and with divergent roles in receptor recognition. Conclusion: The glycan binding pockets define receptor recognition, specificity, and putative switching. Significance: The first detai...