• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nature >NEUTRALIZING ANTIBODY TO HUMAN RHINOVIRUS 14 PENETRATES THE RECEPTOR-BINDING CANYON
【24h】

NEUTRALIZING ANTIBODY TO HUMAN RHINOVIRUS 14 PENETRATES THE RECEPTOR-BINDING CANYON

机译：中和人类鼻病毒14的抗体穿透结合受体的峡谷

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

THE three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion(1,2) has been determined to 4.0 Angstrom resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody-antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds(3,4). Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition, Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system. [References: 29]
机译：已通过组合测定将完整的人鼻病毒14（HRV-14）与Fab片段（Fab17-IA）的三维结构结合，该抗体来自与二价结合到病毒体（1,2）的强中和抗体，分辨率为4.0埃X射线晶体学和低温电子显微镜检查。与最普遍持有的抗体介导的中和模型相反，Fab17-IA不会在HRV-14衣壳中诱导构象变化。相反，抗体的互补位经历大的构象变化以适应表位。与任何先前描述的抗体-抗原结构不同，抗体的保守框架区与病毒表面广泛接触。 Fab17-IA穿透峡谷深处，HRV-14的细胞受体与之结合（3,4）。因此，病毒的四级结构不可能仅仅为了逃避免疫识别而进化，相反，病毒上受体结合区的形状和位置很可能决定了受体的结合和随后的脱壳事件，并且几乎没有或根本没有影响隐藏病毒。免疫系统。 [参考：29]

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