恶性疟原虫EBA175配体结构域的结构及宿主特异性的分子基础。
The structure of the Plasmodium falciparum EBA175 ligand domain and the molecular basis of host specificity.
作者信息
Chattopadhyay Debasish, Rayner Julian, McHenry Amy M, Adams John H
机构信息
Division of Geographic Medicine, University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA.
出版信息
Trends Parasitol. 2006 Apr;22(4):143-5. doi: 10.1016/j.pt.2006.02.007. Epub 2006 Feb 23.
Abstract
Erythrocyte-binding antigen 175 (EBA175) is one of the best-characterized Plasmodium falciparum merozoite ligands; the recently solved crystal structure of EBA175 reveals that terminal sialic acids on the erythrocyte glycoprotein glycophorin A are a crucial factor for erythrocyte recognition by EBA175 because they lock into pockets on its surface. Comparison with Plasmodium reichenowi EBA175 indicates that these interactions have a pivotal role in the host-specific adaptations of parasite ligands.
摘要
红细胞结合抗原175（EBA175）是恶性疟原虫裂殖子配体中特征最为明确的一种；最近解析出的EBA175晶体结构表明，红细胞糖蛋白血型糖蛋白A上的末端唾液酸是EBA175识别红细胞的关键因素，因为它们嵌入其表面的口袋中。与赖氏疟原虫EBA175的比较表明，这些相互作用在寄生虫配体的宿主特异性适应中起关键作用。
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