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首页> 外文期刊>Infection and immunity >Polymorphisms in Erythrocyte Binding Antigens 140 and 181 Affect Function and Binding but Not Receptor Specificity in Plasmodium falciparum
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Polymorphisms in Erythrocyte Binding Antigens 140 and 181 Affect Function and Binding but Not Receptor Specificity in Plasmodium falciparum

机译：红细胞结合抗原140和181中的多态性影响恶性疟原虫的功能和结合而不是受体特异性

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Invasion of human erythrocytes by the malaria parasite Plasmodium falciparum utilizes multiple ligand-receptor interactions involving erythrocyte receptors and parasite erythrocyte binding proteins of the Duffy binding-like family. Erythrocyte binding antigen 175 (EBA-175) binds to glycophorin A, the most abundant protein on the human erythrocyte surface and EBA-140 (also known as BAEBL) binds to glycophorin C, while the receptor for EBA-181 (also known as JESEBL) remains unknown. EBA binding is mediated via region II, a highly structured extracellular domain that shows a degree of sequence variability between different laboratory strains/isolates. Here, we determined the influence of region II polymorphisms on host cell receptor binding and overall function during invasion of EBA-140, EBA-175, and EBA-181. Polymorphisms in the binding domains of EBA-140 and EBA-181 have been suggested previously to alter their respective receptor specificities. In our hands, these polymorphisms affected the levels of EBA-140 and EBA-181 binding to receptors but, critically, not the receptor specificities of these proteins. The degree of EBA-140 binding to glycophorin C correlates with the level of function for this ligand-receptor interaction in merozoite invasion. In contrast, EBA-175, which is highly polymorphic in region II, shows no variability in its ability to bind to its receptor, glycophorin A. Combined, these data highlight the importance of sequence variability in EBAs as driven by immune selection but not by receptor specificity.
机译：疟原虫恶性疟原虫对人红细胞的入侵利用了多个配体-受体相互作用，其中涉及达菲结合样家族的红细胞受体和寄生虫红细胞结合蛋白。红细胞结合抗原175（EBA-175）与人血红蛋白表面上最丰富的蛋白质-糖蛋白A结合，而EBA-140（也称为BAEBL）与糖蛋白C结合，而EBA-181的受体（也称为JESEBL） ）仍然未知。 EBA结合是通过区域II介导的，该区域是高度结构化的细胞外结构域，显示出不同实验室菌株/分离株之间一定程度的序列变异性。在这里，我们确定了区域II多态性对EBA-140，EBA-175和EBA-181入侵期间宿主细胞受体结合和整体功能的影响。先前已经提出EBA-140和EBA-181的结合结构域中的多态性会改变它们各自的受体特异性。在我们手中，这些多态性影响了EBA-140和EBA-181与受体的结合水平，但至关重要的是，并未影响这些蛋白质的受体特异性。 EBA-140结合糖蛋白C的程度与裂殖子入侵中该配体-受体相互作用的功能水平相关。相反，在区域II中高度多态的EBA-175与其受体糖蛋白A的结合能力没有变化。这些数据综合起来，强调了EBA序列变异性的重要性，这是由免疫选择驱动的，而不是由免疫选择驱动的。受体特异性。

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