The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy.
The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy.
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DOI：
10.1371/journal.pone.0029608
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Booth TF
中科院分区：
文献类型：
--
作者：
Beniac DR;Melito PL;Devarennes SL;Hiebert SL;Rabb MJ;Lamboo LL;Jones SM;Booth TF
丝状病毒，包括埃博拉病毒，是丝状动物病毒中的罕见病毒。迄今为止，关于丝状病毒组分分子的排列、化学计量和组织的结构数据一直缺乏，部分原因是需要在4级生物防护下工作。目前的研究为这种致命病原体的结构提供了独特的见解。我们已经研究了埃博拉病毒的结构，使用冷冻电子显微镜，冷冻电子断层扫描，子断层平均，和单粒子图像处理的组合。在这里，我们报告了埃博拉病毒的三维结构和架构，并建立了多个拷贝的RNA基因组可以包装产生多倍体病毒颗粒，通过极端程度的长度多态性。我们表明，螺旋状埃博拉病毒的内核衣壳含有RNA和核蛋白是稳定的外层VP 24-VP 35桥。在其天然状态下的膜相关糖蛋白的结构的阐明表明，推定的受体结合位点被封闭在分子内，而主要的中和表位暴露在其表面上接近病毒包膜。基质蛋白VP 40在包膜内形成规则的晶格，尽管它与核衣壳的接触是不规则的。这项研究的结果表明，埃博拉病毒的模块化组织，容纳一个有序的，对称的核衣壳内的灵活，管状膜包膜。
Filoviruses, including Ebola virus, are unusual in being filamentous animal viruses. Structural data on the arrangement, stoichiometry and organisation of the component molecules of filoviruses has until now been lacking, partially due to the need to work under level 4 biological containment. The present study provides unique insights into the structure of this deadly pathogen. We have investigated the structure of Ebola virus using a combination of cryo-electron microscopy, cryo-electron tomography, sub-tomogram averaging, and single particle image processing. Here we report the three-dimensional structure and architecture of Ebola virus and establish that multiple copies of the RNA genome can be packaged to produce polyploid virus particles, through an extreme degree of length polymorphism. We show that the helical Ebola virus inner nucleocapsid containing RNA and nucleoprotein is stabilized by an outer layer of VP24-VP35 bridges. Elucidation of the structure of the membrane-associated glycoprotein in its native state indicates that the putative receptor-binding site is occluded within the molecule, while a major neutralizing epitope is exposed on its surface proximal to the viral envelope. The matrix protein VP40 forms a regular lattice within the envelope, although its contacts with the nucleocapsid are irregular. The results of this study demonstrate a modular organization in Ebola virus that accommodates a well-ordered, symmetrical nucleocapsid within a flexible, tubular membrane envelope.
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