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首页> 外文期刊>Infection and immunity >Identification of Glycosaminoglycan Binding Domains in Plasmodium falciparum Erythrocyte Membrane Protein 1 of a Chondroitin Sulfate A-Adherent Parasite
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Identification of Glycosaminoglycan Binding Domains in Plasmodium falciparum Erythrocyte Membrane Protein 1 of a Chondroitin Sulfate A-Adherent Parasite

机译：硫酸软骨素A粘附寄生虫的恶性疟原虫红细胞膜蛋白1中的糖胺聚糖结合域的鉴定。

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摘要

Accumulation of Plasmodium falciparum-infected erythrocytes in the placenta is a key feature of maternal malaria. This process is mediated in part by the parasite ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1) at the surface of the infected erythrocyte interacting with the host receptor chondroitin sulfate A (CSA) on the placental lining. We have localized CSA binding activity to two adjacent domains in PfEMP1 of an adherent parasite line and shown the presence of at least three active glycosaminoglycan binding sites. A putative CSA binding sequence was identified in one domain, but nonlinear binding motifs are also likely to be present, since binding activity in the region was shown to be dependent on conformation. Characterization of this binding region provides an opportunity to investigate further its potential as a target for antiadhesion therapy.
机译：恶性疟原虫感染的红细胞在胎盘中积累是母源性疟疾的关键特征。该过程部分由寄生虫配体 P介导。感染的红细胞表面的falciparum 红细胞膜蛋白1（PfEMP1）与胎盘衬里的宿主受体硫酸软骨素A（CSA）相互作用。我们已将CSA结合活性定位于附着的寄生虫株系PfEMP1中的两个相邻域，并显示了至少三个活性糖胺聚糖结合位点的存在。在一个结构域中鉴定了假定的CSA结合序列，但由于该区域的结合活性已显示出依赖于构象，因此也可能存在非线性结合基序。该结合区的表征提供了进一步研究其作为抗粘附疗法靶标的潜力的机会。

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