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

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 publ...

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Bibliographic Details
Published in:Blood 2003-06, Vol.101 (11), p.4628-4631
Main Authors: Lobo, Cheryl-Ann, Rodriguez, Marilis, Reid, Marion, Lustigman, Sara
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Biological and medical sciences
Carrier Proteins - metabolism
Carrier Proteins - physiology
Erythrocyte Membrane - chemistry
Exons
Genetic Variation
Glycophorins - genetics
Glycophorins - metabolism
Glycophorins - physiology
Human protozoal diseases
Humans
Infectious diseases
Malaria
Medical sciences
Membrane Proteins
N-Acetylneuraminic Acid
Parasitic diseases
Plasmodium falciparum - pathogenicity
Protozoal diseases
Protozoan Proteins - metabolism
Protozoan Proteins - physiology
Receptors, Cell Surface - genetics
Receptors, Cell Surface - metabolism
Sequence Deletion
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Summary: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.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood-2002-10-3076