Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1
In: Proceedings of the National Academy of Sciences of the United States of America, Jg. 106 (2009-03-13), Heft 13
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Zugriff:
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.
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Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1
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Autor/in / Beteiligte Person: | Miller, Louis H. ; Tracy, Erin ; D. C. Ghislaine Mayer ; Kabat, Juraj ; Cofie, Joann ; Mendoza, Laurence H. ; Jiang, Lubin ; Hartl, Daniel L. |
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Zeitschrift: | Proceedings of the National Academy of Sciences of the United States of America, Jg. 106 (2009-03-13), Heft 13 |
Veröffentlichung: | 2009 |
Medientyp: | unknown |
ISSN: | 1091-6490 (print) |
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