Pimonov Vladimir V, Konevtsova Olga V, Rochal Sergey B
Nanotechnology Department, Faculty of Physics, Southern Federal University, Zorge 5, Rostov-on-Don 344090, Russian Federation.
Acta Crystallogr A Found Adv. 2019 Jan 1;75(Pt 1):135-141. doi: 10.1107/S2053273318015656.
The development of antiviral strategies requires a clear understanding of the principles that control the protein arrangements in viral shells. Considered here are those capsids that violate the paradigmatic Caspar and Klug (CK) model, and it is shown that the important structural features of such anomalous shells from the Picobirnaviridae, Flaviviridae and Leviviridae families can be revealed by models in the form of spherical icosahedral packings of equivalent rhombic structural units (SUs). These SUs are composed of protein dimers forming the investigated capsids which, as shown here, are based on the rhombic triacontahedron (RT) geometry. How to modify the original CK approach in order to make it compatible with the considered rhombic tessellations of a sphere is also discussed. Analogies between capsids self-assembled from dimers and trimers are demonstrated. This analysis reveals the principles controlling the localization of receptor proteins (which recognize the host cell) on the capsid surface.
抗病毒策略的发展需要清楚地了解控制病毒外壳中蛋白质排列的原理。本文考虑的是那些违反典型的卡斯帕和克鲁格（CK）模型的衣壳，结果表明，来自双分病毒科、黄病毒科和丝状病毒科的此类异常外壳的重要结构特征可以通过等效菱形结构单元（SUs）的球形二十面体堆积形式的模型来揭示。这些SUs由形成所研究衣壳的蛋白质二聚体组成，本文表明，这些衣壳基于菱形三十面体（RT）几何结构。还讨论了如何修改原始的CK方法，使其与所考虑的球体菱形镶嵌兼容。展示了由二聚体和三聚体自组装的衣壳之间的类比。该分析揭示了控制受体蛋白（识别宿主细胞）在衣壳表面定位的原理。
