Mayer, D. C. GhislaineCofie, JoannJiang, LubinHartl, DanielTracy, ErinKabat, JurajMendoza, Laurence H.Miller, Louis H.2010-02-112009Mayer, 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): 5348-5352.0027-8424http://nrs.harvard.edu/urn-3:HUL.InstRepos:3630585In 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.en-USDuffy-binding-like erythrocyte-binding proteininvasionmalariared blood cellsJournal Article2014-10-2210.1073/pnas.0900878106