Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy.
Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy.
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DOI：
10.1016/j.str.2015.06.028
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发表时间：
2015-10-06
期刊：
影响因子：
--
通讯作者：
Orlova EV
中科院分区：
文献类型：
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作者：
Clare DK;Pechnikova EV;Skurat EV;Makarov VV;Sokolova OS;Solovyev AG;Orlova EV
大麦条纹花叶病毒(BSMV，HordeiVirus)是一种杆状单链RNA病毒，结构上与烟草病毒属相似。在这里，我们报道了用低温电子显微镜获得的第一个BSMV的高分辨结构，其分辨率为4.1°。我们发现，BSMV形成两种类型的病毒粒子，每轮的外壳蛋白(CP)亚基数量和CP亚基之间的相互作用不同。虽然BSMV和烟草花叶病毒CP亚基具有相似的折叠，并使用保守残基与RNA相互作用，但这两个病毒组的CP之间的轴向接触有很大不同。BSMV CP亚基缺乏大量的轴向接触，通过相互作用环在病毒粒子表面形成以前未观察到的横向接触，该相互作用环从CP疏水核心突出到相邻的CP亚基。这些数据提供了对螺旋病毒结构组织多样性的洞察。测定了大麦条纹花叶病毒(BSMV)的近原子结构，发现了BSMV的两种形态，这两种形态对BSMV的生活史都很重要。确定了对BSMV结构稳定至关重要的新的侧向接触，BSMV结构可能为生物模板材料中TMV的替代提供了一种选择。在4.1°测定了大麦条纹花叶病毒的结构，发现有两个截然不同的病毒粒子。作者发现了衣壳蛋白之间的一种新的侧向接触，这对病毒粒子的稳定性至关重要。
Barley stripe mosaic virus (BSMV, genus Hordeivirus) is a rod-shaped single-stranded RNA virus similar to viruses of the structurally characterized and well-studied genus Tobamovirus. Here we report the first high-resolution structure of BSMV at 4.1 Å obtained by cryo-electron microscopy. We discovered that BSMV forms two types of virion that differ in the number of coat protein (CP) subunits per turn and interactions between the CP subunits. While BSMV and tobacco mosaic virus CP subunits have a similar fold and interact with RNA using conserved residues, the axial contacts between the CP of these two viral groups are considerably different. BSMV CP subunits lack substantial axial contacts and are held together by a previously unobserved lateral contact formed at the virion surface via an interacting loop, which protrudes from the CP hydrophobic core to the adjacent CP subunit. These data provide an insight into diversity in structural organization of helical viruses. Determined the near-atomic structure of barley stripe mosaic virus (BSMV) Two forms of BSMV were found, both of which are important for its life cycle Identified a new lateral contact that is essential for the stability of BSMV BSMV structure may offer an alternative to TMV in biotemplated materials Clare et al. have determined the structure of barley stripe mosaic virus at 4.1 Å and found that there were two distinct virions. The authors have found a new lateral contact between the capsid proteins that is essential for virion stability.