An assembly model of rift valley Fever virus.
An assembly model of rift valley Fever virus.
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DOI：
10.3389/fmicb.2012.00254
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发表时间：
2012
影响因子：
5.2
通讯作者：
Freiberg AN
中科院分区：
文献类型：
--
作者：
Rusu M;Bonneau R;Holbrook MR;Watowich SJ;Birmanns S;Wriggers W;Freiberg AN
裂谷热病毒（RVFV）是一种布尼亚病毒，在非洲和阿拉伯半岛流行，感染人类和牲畜。该病毒编码两种糖蛋白Gn和Gc，其代表主要的结构抗原并负责宿主细胞受体结合和融合。这两种糖蛋白在病毒表面上组织成圆柱形中空刺突，其聚集成不同的壳粒，整体组装表现出二十面体对称性。目前，没有实验的三维结构的任何完整的布尼亚病毒糖蛋白是可用的。使用折叠识别，我们生成了两种RVFV糖蛋白的分子模型，并发现RVFV Gn蛋白和流感病毒血凝素蛋白之间的显著结构匹配，以及RVFV Gc蛋白和辛德毕斯病毒包膜蛋白E1之间的单独匹配。使用这些模型，潜在的相互作用和安排的RVFV颗粒中的两种糖蛋白进行了分析，通过模拟它们的位置内的冷冻电子显微镜密度图的RVFV。我们确定了四种可能的安排的糖蛋白在病毒粒子包膜。每一种组装模型都提出Gn的胞外域形成了大多数突出的壳粒，并且Gc参与了壳粒基底的形成。此外，Gc被认为有助于壳粒间的连接。RVFV表面上两种糖蛋白的拟议排列类似于甲病毒E1-E2蛋白的描述。我们的模型将提供指导，以更好地了解白蛉病毒的组装过程，这样的结构研究也可以有助于靶向抗病毒药物的设计。
Rift Valley fever virus (RVFV) is a bunyavirus endemic to Africa and the Arabian Peninsula that infects humans and livestock. The virus encodes two glycoproteins, Gn and Gc, which represent the major structural antigens and are responsible for host cell receptor binding and fusion. Both glycoproteins are organized on the virus surface as cylindrical hollow spikes that cluster into distinct capsomers with the overall assembly exhibiting an icosahedral symmetry. Currently, no experimental three-dimensional structure for any entire bunyavirus glycoprotein is available. Using fold recognition, we generated molecular models for both RVFV glycoproteins and found significant structural matches between the RVFV Gn protein and the influenza virus hemagglutinin protein and a separate match between RVFV Gc protein and Sindbis virus envelope protein E1. Using these models, the potential interaction and arrangement of both glycoproteins in the RVFV particle was analyzed, by modeling their placement within the cryo-electron microscopy density map of RVFV. We identified four possible arrangements of the glycoproteins in the virion envelope. Each assembly model proposes that the ectodomain of Gn forms the majority of the protruding capsomer and that Gc is involved in formation of the capsomer base. Furthermore, Gc is suggested to facilitate intercapsomer connections. The proposed arrangement of the two glycoproteins on the RVFV surface is similar to that described for the alphavirus E1-E2 proteins. Our models will provide guidance to better understand the assembly process of phleboviruses and such structural studies can also contribute to the design of targeted antivirals.
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影响因子：
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