Structure of the Macrobrachium rosenbergii nodavirus: A new genus within the Nodaviridae?
Structure of the Macrobrachium rosenbergii nodavirus: A new genus within the Nodaviridae?
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DOI：
10.1371/journal.pbio.3000038
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发表时间：
2018-10
期刊：
影响因子：
9.8
通讯作者：
Bhella D
中科院分区：
文献类型：
--
作者：
Ho KL;Gabrielsen M;Beh PL;Kueh CL;Thong QX;Streetley J;Tan WS;Bhella D
罗氏沼虾诺达病毒(Macrobrachium rosenbergii nodaVirus，MRNV)是一种淡水对虾的病原体，对粮食安全构成威胁，给许多发展中国家的水产养殖业造成巨大的经济损失。对新城疫病毒粒子结构的详细了解将有助于制定控制暴发的战略。MRNV衣壳也被设计成展示异种抗原，因此了解其原子分辨结构将有助于开发基于该平台的工具。在这里，我们提出了一个MR NV衣壳蛋白(CP)的原子分辨率模型，该模型是通过在昆虫细胞中产生的MR NV病毒样颗粒(VLP)的低温电子显微镜(CryoEM)计算的，并在3.3？分辨率下进行三维(3D)图像重建。从受感染的淡水对虾仔虾中提纯的MRNV病毒粒子的冷冻EM产生了6.6？分辨率结构，证实了VLP结构的生物学相关性。我们的数据显示，不同于其他已知的诺达病毒结构，已被证明组装具有三聚体尖峰的衣壳，而先生NV组装具有二聚体尖峰的T=3衣壳。我们还发现了Mr NV衣壳结构与Tombusviridae衣壳结构之间的一些令人惊讶的相似之处：1)衣壳内部有广泛的N-末端臂(NTA)网络，形成长距离相互作用，将不对称单位连接在一起；2)衣壳由每个不对称单位中的3对钙离子稳定；3)突出的尖峰结构域显示出与Tombus病毒尖峰中看到的非常相似的折叠。这些结构上的相似之处引发了关于先生NV的分类的问题。罗氏沼虾诺达病毒(Macrobrachium rosenbergii nodaVirus，Mr NV)是一种重要的淡水对虾病原。通过低温电子显微镜测定mrNV病毒粒子的结构，发现了一种衣壳蛋白，它与其他已知的诺达病毒高度不同，但与植物感染的番茄病毒有惊人的相似之处。罗氏沼虾是一种被广泛种植的食用虾。生产受到白尾病病原罗氏沼虾诺达病毒(Mr NV)的威胁。孵化场的暴发往往导致幼虫和后期幼虫高达100%的死亡率，导致毁灭性的经济损失和威胁粮食安全。我们描述了MR NV衣壳的原子结构，并通过低温电子显微镜和三维图像重建解决了这一问题。我们的分析揭示了新城疫病毒与其他已知诺达病毒的结构之间惊人的差异。此外，我们观察到了新城疫病毒衣壳的几个特征，这些特征在植物侵染番茄病毒家族的病毒粒子结构中已经被描述过。最值得注意的是，Mr NV衣壳在其表面显示出明显的二聚体尖峰，该区域的拓扑结构非常类似于Tombus病毒衣壳尖峰。已知的诺达病毒结构具有三聚体尖峰，并且不显示相同的蛋白质折叠。Mr NV衣壳由二价阳离子稳定，并由排列在病毒粒子内部的N端臂网络连接在一起。我们的分析对新城疫病毒的分类提出了质疑，同时也揭示了这一重要病原体的衣壳结构。这些数据有可能为未来预防白尾病的干预措施的发展提供信息。
Macrobrachium rosenbergii nodavirus (MrNV) is a pathogen of freshwater prawns that poses a threat to food security and causes significant economic losses in the aquaculture industries of many developing nations. A detailed understanding of the MrNV virion structure will inform the development of strategies to control outbreaks. The MrNV capsid has also been engineered to display heterologous antigens, and thus knowledge of its atomic resolution structure will benefit efforts to develop tools based on this platform. Here, we present an atomic-resolution model of the MrNV capsid protein (CP), calculated by cryogenic electron microscopy (cryoEM) of MrNV virus-like particles (VLPs) produced in insect cells, and three-dimensional (3D) image reconstruction at 3.3 Å resolution. CryoEM of MrNV virions purified from infected freshwater prawn post-larvae yielded a 6.6 Å resolution structure, confirming the biological relevance of the VLP structure. Our data revealed that unlike other known nodavirus structures, which have been shown to assemble capsids having trimeric spikes, MrNV assembles a T = 3 capsid with dimeric spikes. We also found a number of surprising similarities between the MrNV capsid structure and that of the Tombusviridae: 1) an extensive network of N-terminal arms (NTAs) lines the capsid interior, forming long-range interactions to lace together asymmetric units; 2) the capsid shell is stabilised by 3 pairs of Ca2+ ions in each asymmetric unit; 3) the protruding spike domain exhibits a very similar fold to that seen in the spikes of the tombusviruses. These structural similarities raise questions concerning the taxonomic classification of MrNV. Macrobrachium rosenbergii nodavirus (MrNV) is an economically important pathogen of freshwater prawns. Determination of the structure of the MrNV virion by cryo-electron microscopy reveals a capsid protein that is highly divergent from other known nodaviruses but has a surprising resemblance to plant-infecting tombusviruses. The freshwater prawn Macrobrachium rosenbergii is widely cultivated for food. Production is threatened by Macrobrachium rosenbergii nodavirus (MrNV), the causative agent of white-tail disease. Outbreaks in hatcheries often result in mortality rates of up to 100% in larvae and post-larvae, leading to devastating economic losses and threatening food security. We describe the atomic structure of the MrNV capsid, solved by cryogenic electron microscopy and three-dimensional image reconstruction. Our analysis revealed surprising differences between the structure of MrNV and that of other known nodaviruses. Moreover, we observed several features in the MrNV capsid that have been previously described in virion structures of the plant-infecting tombusvirus family. Most notably, the MrNV capsid exhibits pronounced dimeric spikes on its surface, the topology of this region closely resembling tombusvirus capsid spikes. Known nodavirus structures have trimeric spikes and do not display the same protein fold. The MrNV capsid is stabilised by divalent cations and laced together by a network of N-terminal arms that line the interior of the virion. Our analysis raises questions about the taxonomic classification of MrNV as well as revealing the structure of the capsid of this important pathogen. These data have the potential to inform the development of future interventions to prevent white-tail disease.
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影响因子：
2.7
作者：
Hanapi UF;Yong CY;Goh ZH;Alitheen NB;Yeap SK;Tan WS
通讯作者：
Tan WS
影响因子：
6.7
作者：
Chen NC;Yoshimura M;Guan HH;Wang TY;Misumi Y;Lin CC;Chuankhayan P;Nakagawa A;Chan SI;Tsukihara T;Chen TY;Chen CJ
通讯作者：
Chen CJ
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
DOI：
10.1002/prot.340230412
发表时间：
1995-12-01
期刊：
PROTEINS-STRUCTURE FUNCTION AND GENETICS
影响因子：
--
作者：
Frishman, D;Argos, P
通讯作者：
Argos, P
影响因子：
2.5
作者：
Qian, D;Shi, Z;Bonami, JR
通讯作者：
Bonami, JR