Visualizing molecular interactions that determine assembly of a bullet-shaped vesicular stomatitis virus particle.
Visualizing molecular interactions that determine assembly of a bullet-shaped vesicular stomatitis virus particle.
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DOI：
10.1038/s41467-022-32223-1
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发表时间：
2022-08-15
影响因子：
16.6
通讯作者：
中科院分区：
文献类型：
--
作者：
水疱性口炎病毒（VSV）是一种基因组不分节段的负链RNA病毒，与狂犬病病毒密切相关。两者都具有典型的子弹状形状。我们报告了通过低温电子显微镜测定的完整、感染性 VSV 颗粒的结构。通过计算分类补偿病毒颗粒之间的多态性，我们以 3.5 Å 的分辨率重建了轴（“树干”），而圆形尖端的分辨率较低。核糖核蛋白 (RNP) 是与核蛋白 (N) 复合的基因组 RNA，卷曲成圆顶状结构，在转变为规则的螺旋主干之前，有大约八个逐渐扩展的转角。两层基质 (M) 蛋白将 RNP 与膜连接起来。径向层间亚基接触固定在单个RNA-N-M1-M2模块内，但灵活的横向和轴向相互作用允许多态性病毒体的组装。结合已发表的不同状态下的重组 N 结构，我们的结果表明了 VSV 及其相关物的膜耦合自组装机制。水泡性口炎病毒 (VSV) 是研究最广泛的负义 RNA 病毒原型。 VSV 颗粒的结构测定特别具有挑战性，因为它们具有不同螺旋对称性的多态性。在这里，珍妮等人。应用计算分类方法对不同的形态进行排序，并获得 3.5-4.1 A 分辨率的 CryoEM 重建。他们表明，基质蛋白（M）存在于病毒体中的两层中，其中内层与vRNP的N蛋白结合。
Vesicular stomatitis virus (VSV) is a negative-strand RNA virus with a non-segmented genome, closely related to rabies virus. Both have characteristic bullet-like shapes. We report the structure of intact, infectious VSV particles determined by cryogenic electron microscopy. By compensating for polymorphism among viral particles with computational classification, we obtained a reconstruction of the shaft (“trunk”) at 3.5 Å resolution, with lower resolution for the rounded tip. The ribonucleoprotein (RNP), genomic RNA complexed with nucleoprotein (N), curls into a dome-like structure with about eight gradually expanding turns before transitioning into the regular helical trunk. Two layers of matrix (M) protein link the RNP with the membrane. Radial inter-layer subunit contacts are fixed within single RNA-N-M1-M2 modules, but flexible lateral and axial interactions allow assembly of polymorphic virions. Together with published structures of recombinant N in various states, our results suggest a mechanism for membrane-coupled self-assembly of VSV and its relatives. Vesicular stomatitis virus (VSV) is the most widely studied prototype for negative-sense RNA viruses. Structure determination of VSV particles is particularly challenging because they are polymorphic with different helical symmetries. Here, Jenni et al. apply computational classification approaches to sort different morphologies, and obtain CryoEM reconstructions at 3.5–4.1 A resolution. They show that the matrix protein (M) is present in the virion in two layers, of which the inner layer associates with N protein of vRNPs.
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影响因子：
5.4
作者：
Green, Todd J.;Rowse, Michael;Luo, Ming
通讯作者：
Luo, Ming
DOI：
10.1107/s2059798318006551
发表时间：
2018-06-01
期刊：
Acta crystallographica. Section D, Structural biology
影响因子：
--
作者：
Afonine PV;Poon BK;Read RJ;Sobolev OV;Terwilliger TC;Urzhumtsev A;Adams PD
通讯作者：
Adams PD
影响因子：
5.4
作者：
BARGE, A;GAUDIN, Y;RUIGROK, RWH
通讯作者：
RUIGROK, RWH
DOI：
10.1107/s0907444909042073
发表时间：
2010-01
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Chen VB;Arendall WB 3rd;Headd JJ;Keedy DA;Immormino RM;Kapral GJ;Murray LW;Richardson JS;Richardson DC
通讯作者：
Richardson DC
影响因子：
8.8
作者：
Jenni, Simon;Bloyet, Louis-Marie;Harrison, Stephen C.
通讯作者：
Harrison, Stephen C.