Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron ciyomicroscopy
Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron ciyomicroscopy
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DOI：
10.1128/jvi.00645-06
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发表时间：
2006-08-01
影响因子：
5.4
通讯作者：
Buchmeier, Michael J.
中科院分区：
文献类型：
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作者：
Neuman, Benjamin W.;Adair, Brian D.;Buchmeier, Michael J.
冠状病毒颗粒具有包膜和多形性，因此难以结晶和对称辅助重建。将单颗粒图像分析的新方法应用于选定的病毒特征，以获得病毒结构蛋白之间的寡聚状态和空间关系的详细模型。严重急性呼吸综合征冠状病毒和其他两种冠状病毒的 S、M 和 N 结构蛋白的二维图像被细化至类似于 4 nm 的分辨率。病毒膜附近的蛋白质排列成重叠的晶格，围绕着无序的核心。三聚体糖蛋白尖峰与四种潜在核糖核蛋白密度一致。然而，尖峰对于核糖核蛋白晶格的形成来说是可有可无的。当从病毒膜释放时，核糖核蛋白颗粒呈现卷曲形状。我们的结果有助于了解冠状病毒和其他多形性病毒使用的组装途径，并提供了冠状病毒超微结构的第一个详细视图。
Coronavirus particles are enveloped and pleomorphic and are thus refractory to crystallization and symmetry-assisted reconstruction. A novel methodology of single-particle image analysis was applied to selected virus features to obtain a detailed model of the oligomeric state and spatial relationships among viral structural proteins. Two-dimensional images of the S, M, and N structural proteins of severe acute respiratory syndrome coronavirus and two other coronaviruses were refined to a resolution of similar to 4 nm. Proteins near the viral membrane were arranged in overlapping lattices surrounding a disordered core. Trimeric glycoprotein spikes were in register with four underlying ribonucleoprotein densities. However, the spikes were dispensable for ribonucleoprotein lattice formation. The ribonucleoprotein particles displayed coiled shapes when released from the viral membrane. Our results contribute to the understanding of the assembly pathway used by coronaviruses and other pleomorphic viruses and provide the first detailed view of coronavirus ultrastructure.