Cryo-EM structure of a novel calicivirus, Tulane virus.
Cryo-EM structure of a novel calicivirus, Tulane virus.
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DOI：
10.1371/journal.pone.0059817
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Jiang W
中科院分区：
文献类型：
--
作者：
Yu G;Zhang D;Guo F;Tan M;Jiang X;Jiang W
杜兰病毒（Tulane virus，TV）是一种新分离的可培养杯状病毒，主要感染幼年恒河猴。在这里，我们报告了一个6.3 μ m分辨率的冷冻电子显微镜结构的电视病毒体。TV病毒粒子直径约400 μ m，由包围RNA基因组的T=3二十面体蛋白衣壳组成。 180个拷贝的主要衣壳蛋白VP 1（约57 KDa）被组织成两种类型的二聚体A/B和C/C，并形成一个薄而光滑的壳，壳上镶嵌着90个二聚体突起。TV的总体衣壳组织和衣壳蛋白折叠与其他杯状病毒，特别是人类诺瓦克病毒（原型人类诺如病毒）的衣壳组织和衣壳蛋白折叠非常相似。这些紧密的结构相似性支持TV作为不可培养的人诺如病毒的有吸引力的替代物。TV最显著的特征是其C/C二聚体处于高度柔性的构象，其中VP 1的壳（S）结构域和突出（P）结构域之间的相互作用显著降低。比较结构分析表明，TV C/C二聚体的P结构域比其他杯状病毒的P结构域更灵活。这些观察结果，结合以前的研究其他杯状病毒，使我们假设，C/C二聚体P结构域的增强的灵活性可能需要有效的杯状病毒-宿主细胞相互作用和随之而来的脱壳和基因组释放。在S和P结构域之间的S-P1铰链中的残基可能在C/C二聚体的P结构域的柔性中起关键作用。
Tulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 Å resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 Å in diameter and consists of a T = 3 icosahedral protein capsid enclosing the RNA genome. 180 copies of the major capsid protein VP1 (∼57 KDa) are organized into two types of dimers A/B and C/C and form a thin, smooth shell studded with 90 dimeric protrusions. The overall capsid organization and the capsid protein fold of TV closely resemble that of other caliciviruses, especially of human Norwalk virus, the prototype human norovirus. These close structural similarities support TV as an attractive surrogate for the non-cultivatable human noroviruses. The most distinctive feature of TV is that its C/C dimers are in a highly flexible conformation with significantly reduced interactions between the shell (S) domain and the protruding (P) domain of VP1. A comparative structural analysis indicated that the P domains of TV C/C dimers were much more flexible than those of other caliciviruses. These observations, combined with previous studies on other caliciviruses, led us to hypothesize that the enhanced flexibility of C/C dimer P domains are likely required for efficient calicivirus-host cell interactions and the consequent uncoating and genome release. Residues in the S-P1 hinge between the S and P domain may play a critical role in the flexibility of P domains of C/C dimers.
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