...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of bacteriology >Mapping of the Neisseria meningitidis NadA Cell-Binding Site: Relevance of Predicted α-Helices in the NH2-Terminal and Dimeric Coiled-Coil Regions
【24h】

Mapping of the Neisseria meningitidis NadA Cell-Binding Site: Relevance of Predicted α-Helices in the NH2-Terminal and Dimeric Coiled-Coil Regions

机译：脑膜炎奈瑟氏球菌NadA细胞结合位点的映射：在NH 2终端和二聚螺旋线圈区域中预测的α螺旋的相关性。

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

摘要

NadA is a trimeric autotransporter protein of Neisseria meningitidis belonging to the group of oligomeric coiled-coil adhesins. It is implicated in the colonization of the human upper respiratory tract by hypervirulent serogroup B N. meningitidis strains and is part of a multiantigen anti-serogroup B vaccine. Structure prediction indicates that NadA is made by a COOH-terminal membrane anchor (also necessary for autotranslocation to the bacterial surface), an intermediate elongated coiled-coil-rich stalk, and an NH2-terminal region involved in cell interaction. Electron microscopy analysis and structure prediction suggest that the apical region of NadA forms a compact and globular domain. Deletion studies proved that the NH2-terminal sequence (residues 24 to 87) is necessary for cell adhesion. In this study, to better define the NadA cell binding site, we exploited (i) a panel of NadA mutants lacking sequences along the coiled-coil stalk and (ii) several oligoclonal rabbit antibodies, and their relative Fab fragments, directed to linear epitopes distributed along the NadA ectodomain. We identified two critical regions for the NadA-cell receptor interaction with Chang cells: the NH2 globular head domain and the NH2 dimeric intrachain coiled-coil α-helices stemming from the stalk. This raises the importance of different modules within the predicted NadA structure. The identification of linear epitopes involved in receptor binding that are able to induce interfering antibodies reinforces the importance of NadA as a vaccine antigen.
机译：NadA是脑膜炎奈瑟氏球菌的三聚体自转运蛋白，属于低聚卷曲螺旋粘附素。它与高毒力血清型B N在人类上呼吸道的定殖有关。脑膜炎菌株，是多抗原抗血清B群疫苗的一部分。结构预测表明，NadA是由一个COOH末端的膜锚（对于自动转移到细菌表面也是必需的），一个中间的细长的卷曲螺旋富集的茎和一个NH 2 末端区域组成。在细胞相互作用中。电子显微镜分析和结构预测表明，NadA的顶端区域形成一个紧凑的球状结构域。缺失研究证明，NH 2 -末端序列（24-87位残基）对于细胞粘附是必需的。在这项研究中，为了更好地定义NadA细胞结合位点，我们利用了（i）沿卷曲螺旋茎缺乏序列的一组NadA突变体，以及（ii）针对线性表位的几种寡克隆兔抗体及其相对Fab片段沿NadA胞外域分布。我们确定了NadA细胞受体与Chang细胞相互作用的两个关键区域：NH 2 球形头部结构域和NH 2 二聚体链内卷曲螺旋α-螺旋茎。这提高了预测的NadA结构中不同模块的重要性。能够诱导干扰抗体的参与受体结合的线性表位的鉴定加强了NadA作为疫苗抗原的重要性。

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