School of Biological Sciences, Nanyang Technological University, Singapore 637551,
Infect Immun. 2011 Jul;79(7):2880-8. doi: 10.1128/IAI.01326-10. Epub 2011 Apr 11.
Invasion of the host cell by the malaria parasite is a key step for parasite survival and the only stage of its life cycle where the parasite is extracellular, and it is therefore a target for an antimalaria intervention strategy. Multiple members of the reticulocyte binding protein homologues (RH) family are found in all plasmodia and have been shown to bind to host red blood cells directly. In the study described here, we delineated the erythrocyte binding domain (EBD) of one member of the RH family, termed Py235, from Plasmodium yoelii. Moreover, we have obtained the low-resolution structure of the EBD using small-angle X-ray scattering. Comparison of the EDB structure to other characterized Plasmodium receptor binding domains suggests that there may be an overall structural conservation. These findings may help in developing new approaches to target receptor ligand interactions mediated by parasite proteins.
疟原虫侵入宿主细胞是寄生虫存活的关键步骤，也是其生命周期中唯一处于细胞外的阶段，因此是抗疟干预策略的一个目标。所有疟原虫中都发现有多个网织红细胞结合蛋白同源物（RH）家族成员，并且已经证明它们可以直接与宿主的红细胞结合。在本文所描述的研究中，我们描绘了来自约氏疟原虫的 RH 家族的一个成员，称为 Py235 的红细胞结合域（EBD）。此外，我们还使用小角度 X 射线散射获得了 EBD 的低分辨率结构。将 EDB 结构与其他已鉴定的疟原虫受体结合结构域进行比较表明，可能存在整体结构的保守性。这些发现可能有助于开发针对寄生虫蛋白介导的受体配体相互作用的新方法。
