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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
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Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk

机译：新城疫病毒血凝素-神经氨酸酶（HN）胞外域的结构揭示了四螺旋束茎。

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摘要

The paramyxovirus hemagglutinin-neuraminidase (HN) protein plays multiple roles in viral entry and egress, including binding to sialic acid receptors, activating the fusion (F) protein to activate membrane fusion and viral entry, and cleaving sialic acid from carbohydrate chains. HN is an oligomeric integral membrane protein consisting of an N-terminal transmembrane domain, a stalk region, and an enzymatically active neuraminidase (NA) domain. Structures of the HN NA domains have been solved previously; however, the structure of the stalk region has remained elusive. The stalk region contains specificity determinants for F interactions and activation, underlying the requirement for homotypic F and HN interactions in viral entry. Mutations of the Newcastle disease virus HN stalk region have been shown to affect both F activation and NA activities, but a structural basis for understanding these dual affects on HN functions has been lacking. Here, we report the structure of the Newcastle disease virus HN ectodomain, revealing dimers of NA domain dimers flanking the N-terminal stalk domain. The stalk forms a parallel tetrameric coiled-coil bundle (4HB) that allows classification of extensive mutational data, providing insight into the functional roles of the stalk region. Mutations that affect both F activation and NA activities map predominantly to the 4HB hydro phobic core, whereas mutations that affect only F-protein activation map primarily to the 4HB surface. Two of four NA domains interact with the 4HB stalk, and residues at this interface in both the stalk and NA domain have been implicated in HN function.
机译：副粘病毒血凝素神经氨酸酶（HN）蛋白在病毒的进入和流出中起多种作用，包括与唾液酸受体结合，激活融合（F）蛋白以激活膜融合和病毒进入以及从碳水化合物链上裂解唾液酸。 HN是由N端跨膜结构域，茎区域和具有酶活性的神经氨酸酶（NA）结构域组成的寡聚完整膜蛋白。 HN NA域的结构先前已经解决；然而，茎区域的结构仍然难以捉摸。茎区域包含F相互作用和激活的特异性决定因素，这是病毒进入时对同型F和HN相互作用的要求。已表明新城疫病毒HN茎区域的突变既影响F活化又影响NA活性，但是缺乏了解这些对HN功能的双重影响的结构基础。在这里，我们报告了新城疫病毒HN胞外域的结构，揭示了NA域二聚体位于N末端茎域两侧的二聚体。茎形成平行的四聚体卷曲螺旋束（4HB），允许对大量突变数据进行分类，从而深入了解茎区域的功能角色。影响F激活和NA活性的突变主要映射到4HB疏水核心，而仅影响F蛋白激活的突变主要映射到4HB表面。四个NA结构域中的两个与4HB茎相互作用，并且茎和NA结构域中此接口处的残基都与HN功能有关。

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    Ping Yuan; Kurt A. Swanson; George P. Leser; Reay G. Paterson; Robert A. Lamb; Theodore S. Jardetzky;

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    Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305;

    Howard Hughes Medical Institute,Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;

    Howard Hughes Medical Institute,Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;

    Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;

    Howard Hughes Medical Institute,Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;

    Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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