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. 2003 Jun 1;101(11):4628-31.
doi: 10.1182/blood-2002-10-3076. Epub 2003 Feb 6.

Glycophorin C Is the Receptor for the Plasmodium Falciparum Erythrocyte Binding Ligand PfEBP-2 (Baebl)

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Glycophorin C Is the Receptor for the Plasmodium Falciparum Erythrocyte Binding Ligand PfEBP-2 (Baebl)

Cheryl-Ann Lobo et al. Blood. .

Abstract

We report in this paper that glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. PfEBP-2 is a member of the Duffy binding-like erythrocyte binding protein (DBL-EBP) family. Although several reports have been published characterizing PfEBP-2, the identity of its erythrocytic receptor was still unknown. Using a combination of enzymatically treated red blood cells (RBCs) and rare, variant RBCs lacking different surface proteins, we have shown that PfEBP-2 does not bind to cells lacking GPC. Additionally, we found that PfEBP-2 binds differentially to variants of GPC lacking exon 2 or exon 3, and determined that the binding domain on GPC is potentially restricted to amino acid residues 14 through 22 within exon 2. Thus PfEBP-2 is involved in a sialic acid-dependent pathway of invasion, which does not involve glycophorin A or glycophorin B and represents a novel route of entry into the RBCs.

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