...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Full-Length Influenza Hemagglutinin HA2 Refolds into the Trimeric Low-pH-Induced Conformation
【24h】

Full-Length Influenza Hemagglutinin HA2 Refolds into the Trimeric Low-pH-Induced Conformation

机译：全长流感血凝素HA2重新折叠成三聚体低pH诱导的构象

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 influenza virus uses hemagglutinin (HA) to fuse the viral and cellular membranes.As part of an effort to study the membrane-interacting elements of HA,the fusion peptide,and the C-terminal transmembrane anchor,we have expressed in Escherichia coll the full-length HA_2 chain with maltose-binding protein fused at its N-terminus.The chimeric protein can be refolded in vitro in the presence of specific detergents to yield stable,homogeneous trimers,as determined by analytical ultracentrifugation.The trimers have the so-called "low pH" conformation-the rearranged HA_2 conformation obtained when intact HA_1/HA_2 is induced to refold by exposure to low pH-as detected by electron microscopy and monoclonalantibody reactivity.These results provide further evidence for the notion that the neutral-pH structure of intact HA is metastable and that binding of protons lowers the kinetic barriers that prevent rearrangement to the minimum-free-energy conformation.The refolded chimeric protein described here is a suitable species for undertaking studies of how the fusion peptide inserts into membranes and assessing the nature of possible intermediates in the fusion process.
机译：流感病毒使用血凝素（HA）融合病毒和细胞膜。作为研究HA的膜相互作用元件，融合肽和C端跨膜锚的努力的一部分，我们在大肠杆菌中进行了表达。全长HA_2链在其N端融合了麦芽糖结合蛋白。嵌合蛋白可以在特异去污剂存在下进行体外折叠，以产生稳定，均质的三聚体，这是通过分析超速离心法测定的。电子显微镜和单克隆抗体反应性检测到，被称为“低pH”构象-当通过暴露于低pH诱导完整的HA_1 / HA_2重折叠时获得的重排HA_2构象。这些结果为中性pH结构的概念提供了进一步的证据完整的HA的亚稳态是稳定的，并且质子的结合降低了阻止重排至最小自由能构象的​​动力学障碍。这里的床是用于研究融合肽如何插入膜并评估融合过程中可能的中间体性质的合适物种。

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