Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl)
Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl)
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DOI：
10.1182/blood-2002-10-3076
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发表时间：
2003-06-01
期刊：
影响因子：
20.3
通讯作者：
Lustigman, S
中科院分区：
文献类型：
--
作者：
Lobo, CA;Rodriguez, M;Lustigman, S
本文报道血型糖蛋白C（GPC）是新发现的恶性疟原虫红细胞结合配体PfEBP-2（baebl，EBA-140）的受体。PfEBP-2是Duffy结合样红细胞结合蛋白（DBL-EBP）家族的成员。虽然已经发表了几篇描述PfEBP-2的报道，但其红细胞受体的身份仍然未知。使用酶处理的红细胞（RBC）和缺乏不同表面蛋白的罕见变体RBC的组合，我们已经表明PfEBP-2不结合缺乏GPC的细胞。此外，我们发现PfEBP-2与缺失外显子2或外显子3的GPC变体的结合差异，并确定GPC上的结合结构域可能限于外显子2内的氨基酸残基14至22。因此，PfEBP-2参与唾液酸依赖性侵袭途径，其不涉及血型糖蛋白A或血型糖蛋白B，并且代表进入RBC的新途径。(C)2003年，美国血液学会。
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 a combination of enzymatically treated red blood cells (RBCs) and rare, variant RBCs lacking different surface proteins, we have shown that PfEBP-2 does not bind to cells lacking GPC. Additionally, we found that PfEBP-2 binds differentially to variants of GPC lacking exon 2 or exon 3, and determined that the binding domain on GPC is potentially restricted to amino acid residues 14 through 22 within exon 2. Thus PfEBP-2 is involved in a sialic acid-dependent pathway of invasion, which does not involve glycophorin A or glycophorin B and represents a novel route of entry into the RBCs. (C) 2003 by The American Society of Hematology.