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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 a core fragment of glycoprotein H from pseudorabies virus in complex with antibody
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Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody

机译：伪狂犬病病毒糖蛋白H核心片段与抗体复合物的结构

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摘要

Compared with many well-studied enveloped viruses, herpesvi-ruses use a more sophisticated molecular machinery to induce fusion of viral and cellular membranes during cell invasion. This essential function is carried out by glycoprotein B (gB), a class III viral fusion protein, together with the heterodimer of glycoproteins H and L (gH/gL). In pseudorabies virus (PrV), a porcine herpesvirus, it was shown that gH/gL can be substituted by a chimeric fusion protein gDgH, containing the receptor binding domain (RBD) of glycoprotein D fused to a truncated version of gH lacking its N-terminal domain. We report here the 2.1-A resolution structure of the core fragment of gH present in this chimera, bound to the Fab fragment of a PrV gH-specific monoclonal antibody. The structure strongly complements the information derived from the recently reported structure of gH/gL from herpes simplex virus type 2 (HSV-2). Together with the structure of Epstein-Barr virus (EBV) gH/gL reported in parallel, it provides insight into potentially functional conserved structural features. One feature is the presence of a syntaxin motif, and the other is an extended "flap" masking a conserved hydrophobic patch in the C-terminal domain, which is closest to the viral membrane. The negative electrostatic surface potential of this domain suggests repulsive interactions with the lipid heads. The structure indicates the possible unmasking of an extended hydrophobic patch by movement of the flap during a receptor-triggered conformational change of gH, exposing a hydro-phobic surface to interact with the viral membrane during the fusion process.
机译：与许多经过充分研究的包膜病毒相比，疱疹病毒使用更复杂的分子机制在细胞入侵过程中诱导病毒膜和细胞膜融合。该基本功能由糖蛋白B（gB），III类病毒融合蛋白以及糖蛋白H和L的异二聚体（gH / gL）共同完成。在猪疱疹病毒伪狂犬病病毒（PrV）中，显示gH / gL可以被嵌合融合蛋白gDgH取代，该融合蛋白包含糖蛋白D的受体结合结构域（RBD），与糖蛋白D的截短形式融合，而缺少N-终端域。我们在这里报告了存在于该嵌合体中的gH核心片段的2.1-A解析结构，该结构与PrV gH特异性单克隆抗体的Fab片段结合。该结构强烈补充了最近报道的来自2型单纯疱疹病毒（HSV-2）的gH / gL结构的信息。与并行报道的爱泼斯坦-巴尔病毒（EBV）gH / gL的结构一起，它可以洞悉潜在的功能保守结构特征。一个特征是语法素基序的存在，另一个特征是扩展的“襟翼”，掩盖了最靠近病毒膜的C端结构域中的保守疏水性补丁。该区域的负静电表面电势表明与脂质头的排斥相互作用。该结构表明，在受体触发的gH构象变化过程中，襟翼可能会移动，从而扩展了疏水性补丁的覆盖范围，从而使疏水性表面在融合过程中与病毒膜相互作用。

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    Marija Backovic; Rebecca M. DuBois; Joseph J. Cockburn; Andrew J. Sharff; Marie-Christine Vaney; Harald Granzow; Barbara G. Klupp; Gerard Bricogne; Thomas C. Mettenleiter; Felix A. Rey;

  • 作者单位

    lnstitut Pasteur, Departement de Virologie, Unite de Virologie Structural, 75724 Paris Cedex 15, France,Centre National de la Recherche Scientifique, Unitede Recherche Associee 3015, 75724 Paris Cedex 15, France;

    lnstitut Pasteur, Departement de Virologie, Unite de Virologie Structural, 75724 Paris Cedex 15, France,Centre National de la Recherche Scientifique, Unitede Recherche Associee 3015, 75724 Paris Cedex 15, France;

    lnstitut Pasteur, Departement de Virologie, Unite de Virologie Structural, 75724 Paris Cedex 15, France,Centre National de la Recherche Scientifique, Unitede Recherche Associee 3015, 75724 Paris Cedex 15, France;

    Global Phasing Ltd., Cambridge CB3 OAX, United Kingdom;

    lnstitut Pasteur, Departement de Virologie, Unite de Virologie Structural, 75724 Paris Cedex 15, France,Centre National de la Recherche Scientifique, Unitede Recherche Associee 3015, 75724 Paris Cedex 15, France;

    lnstitute of Molecular Biology,Friedrich-Loeffler-lnstitut, 17493 Greifswald-lnsel Riems, Germany;

    lnstitute of Molecular Biology,Friedrich-Loeffler-lnstitut, 17493 Greifswald-lnsel Riems, Germany;

    Global Phasing Ltd., Cambridge CB3 OAX, United Kingdom;

    lnstitute of Molecular Biology,Friedrich-Loeffler-lnstitut, 17493 Greifswald-lnsel Riems, Germany;

    lnstitut Pasteur, Departement de Virologie, Unite de Virologie Structural, 75724 Paris Cedex 15, France,Centre National de la Recherche Scientifique, Unitede Recherche Associee 3015, 75724 Paris Cedex 15, France;

  • 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);
  • 原文格式 PDF
  • 正文语种 eng
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  • 关键词

    herpesvirus entry; herpesvirus envelope proteins; membrane fusion; syntaxins and intracellular vesicle fusion; protein disulfide isomerase motif;

    机译：疱疹病毒进入;疱疹病毒包膜蛋白;膜融合;Syntaxins与细胞内囊泡融合;蛋白质二硫键异构酶基序;

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