...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell Reports >Architecture of Human IgM in Complex with P. falciparum Erythrocyte Membrane Protein 1
【24h】

Architecture of Human IgM in Complex with P. falciparum Erythrocyte Membrane Protein 1

机译：人恶性疟原虫红细胞膜蛋白1复合物中的人IgM的体系结构。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Plasmodium falciparum virulence is associated with sequestration of infected erythrocytes. Microvascular binding mediated by PfEMP1 in complex with non-immune immunoglobulin M (IgM) is common among parasites that cause both severe childhood malaria and pregnancy-associated malaria. Here, we present cryo-molecular electron tomography structures of human IgM, PfEMP1 and their complex. Three-dimensional reconstructions of IgM reveal that it has a dome-like core, randomly oriented Fab"2s units, and the overall shape of a turtle. PfEMP1 is a C- shaped molecule with a flexible N terminus followed by an arc-shaped backbone and a bulky C terminus that interacts with IgM. Our data demonstrate that the PfEMP1 binding pockets on IgM overlap with those of C1q, and the bulkiness of PfEMP1 limits the capacity of IgM to interact with PfEMP1. We suggest that P. falciparum exploits IgM to cluster PfEMP1 into an organized matrix to augment its affinity to host cell receptors.
机译：恶性疟原虫的毒力与被感染的红细胞隔离有关。由PfEMP1介导的与非免疫免疫球蛋白M（IgM）结合的微血管结合在引起严重的儿童疟疾和与妊娠相关的疟疾的寄生虫中很常见。在这里，我们介绍了人类IgM，PfEMP1及其复合物的低温分子电子断层扫描结构。 IgM的三维重建显示它具有圆顶状核心，随机定向的Fab“ 2s单元和乌龟的整体形状。PfEMP1是具有柔性N端和后接弧形主链的C形分子我们的数据表明，IgM上的PfEMP1结合口袋与C1q重叠，并且PfEMP1的庞大限制了IgM与PfEMP1相互作用的能力。我们建议恶性疟原虫利用IgM来将PfEMP1聚集成一个有组织的基质，以增强其对宿主细胞受体的亲和力。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号