Host Erythrocyte Engagement by PfEBA-140 1 Molecular Basis for Sialic Acid-dependent Receptor Recognition by Plasmodium falciparum Erythrocyte Binding Antigen 140/BAEBL
نویسندگان
چکیده
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 detailed molecular view of receptor recognition by a critical P. falciparum invasion ligand.
منابع مشابه
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 published characterizing PfEBP-2, the identity of its erythrocytic receptor was still unknown. Using ...
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