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Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1

Citation:

Mayer, DC, J Cofie, L Jiang, DL Hartl, E Tracy, J Kabat, LH Mendoza, and LH Miller. 2009. “Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1.” Proc Natl Acad Sci U S A 106: 5348-52.

Date Published:

Mar 31

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.

Notes:

Mayer, D C GhislaineCofie, JoannJiang, LubinHartl, Daniel LTracy, ErinKabat, JurajMendoza, Laurence HMiller, Louis Heng2009/03/13 09:00Proc Natl Acad Sci U S A. 2009 Mar 31;106(13):5348-52. doi: 10.1073/pnas.0900878106. Epub 2009 Mar 11.

Last updated on 05/12/2015