Glycophorin B is the Erythrocyte Receptor of Plasmodium Falciparum Erythrocyte-Binding Ligand, EBL-1

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Glycophorin B is the Erythrocyte Receptor of Plasmodium Falciparum Erythrocyte-Binding Ligand, EBL-1

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Title: Glycophorin B is the Erythrocyte Receptor of Plasmodium Falciparum Erythrocyte-Binding Ligand, EBL-1
Author: Mayer, D. C. Ghislaine; Cofie, Joann; Jiang, Lubin; Hartl, Daniel L.; Tracy, Erin; Kabat, Juraj; Mendoza, Laurence H.; Miller, Louis H.

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Citation: Mayer, D.C. Ghislaine, Joann Cofie, Lubin Jiang, Daniel L. Hartl, Erin Tracy, Juraj Kabat, Laurence H. Mendoza, and Louis H. Miller. 2009. Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1. Proceedings of the National Academy of Sciences 106(13): 5348-5352.
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Abstract: In the war against Plasmodium, humans have evolved to eliminate or modify proteins on the erythrocyte surface that serve as receptors for parasite invasion, such as the Duffy blood group, a receptor for Plasmodium vivax, and the Gerbich-negative modification of glycophorin C for Plasmodium falciparum. In turn, the parasite counters with expansion and diversification of ligand families. The high degree of polymorphism in glycophorin B found in malaria-endemic regions suggests that it also may be a receptor for Plasmodium, but, to date, none has been identified. We provide evidence from erythrocyte-binding that glycophorin B is a receptor for the P. falciparum protein EBL-1, a member of the Duffy-binding-like erythrocyte-binding protein (DBL-EBP) receptor family. The erythrocyte-binding domain, region 2 of EBL-1, expressed on CHO-K1 cells, bound glycophorin B􏰑 but not glycophorin B-null erythrocytes. In addition, glycophorin B􏰑 but not glycophorin B-null erythrocytes adsorbed native EBL-1 from the P. falciparum culture supernatants. Interestingly, the Efe pygmies of the Ituri forest in the Democratic Republic of the Congo have the highest gene frequency of glycophorin B-null in the world, raising the possibility that the DBL-EBP family may have expanded in response to the high frequency of glycophorin B-null in the population.
Published Version: http://dx.doi.org/10.1073/pnas.0900878106
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:3630585

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  • FAS Scholarly Articles [7374]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University
 
 

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