...
首页> 外文期刊>Structure >Visualization of single receptor molecules bound to human rhinovirus under physiological conditions
【24h】

Visualization of single receptor molecules bound to human rhinovirus under physiological conditions

机译:在生理条件下与人鼻病毒结合的单个受体分子的可视化

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

Dynamic force microscopy (DFM) was used to image human rhinovirus HRV2 alone and complexed with single receptor molecules under near physiological conditions. Specific and site-directed immobilization of HRV2 on a model cell membrane resulted in a crystalline arrangement of virus particles with hexagonal symmetry and 35 nm spacing. High-resolution imaging of the virus capsid revealed about 20 resolvable structural features with 3 nm diameters; this finding is in agreement with protrusions seen by cryo-electron microscopy. Binding of receptor molecules to individual virus particles was observed after injection of soluble receptors into the liquid cell. Virus-receptor complexes with zero, one, two, or three attached receptor molecules were resolved. The number of receptor molecules associated to virions increased over time. Occasionally, dissociation of single receptor molecules from viral particles was also observed.
机译:动态力显微镜(DFM)用于单独成像人鼻病毒HRV2,并在接近生理条件下与单个受体分子复合。 HRV2在模型细胞膜上的特异性和定点固定导致六边形对称和35 nm间距的病毒颗粒的晶体排列。病毒衣壳的高分辨率成像显示了直径约3 nm的约20个可分辨结构特征;这一发现与通过冷冻电子显微镜观察到的突起一致。将可溶性受体注入液体细胞后,观察到受体分子与单个病毒颗粒的结合。解析了具有零个,一个,两个或三个附着的受体分子的病毒-受体复合物。与病毒体相关的受体分子的数量随时间增加。有时,还观察到单个受体分子从病毒颗粒上解离。

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