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refinement and analysis of the mature Zika virus cryo-EM structure at 3.1 Å resolution.

Refinement and Analysis of the Mature Zika Virus Cryo-EM Structure at 3.1 Å Resolution.

机构信息

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.

出版信息

Structure. 2018 Sep 4;26(9):1169-1177.e3. doi: 10.1016/j.str.2018.05.006. Epub 2018 Jun 26.

Abstract

Among the several arthropod-borne human flaviviral diseases, the recent outbreak of Zika virus (ZIKV) has caused devastating birth defects and neurological disorders, challenging the world with another major public health concern. We report here the refined structure of the mature ZIKV at a resolution of 3.1 Å as determined by cryo-electron microscopic single-particle reconstruction. The improvement in the resolution, compared with previous enveloped virus structures, was the result of optimized virus preparation methods and data processing techniques. The glycoprotein interactions and surface properties of ZIKV were compared with other mosquito-borne flavivirus structures. The largest structural differences and sequence variations occur at the glycosylation loop associated with receptor binding. Probable drug binding pockets were identified on the viral surface. These results also provide a structural basis for the design of vaccines against ZIKV.

摘要

在几种节肢动物传播的人类黄病毒疾病中,寨卡病毒(ZIKV)的最近爆发导致了毁灭性的出生缺陷和神经紊乱,给世界带来了另一个主要的公共卫生关注。我们在此报告通过冷冻电镜单颗粒重建确定的成熟 ZIKV 的分辨率为 3.1 Å 的精细结构。与以前的包膜病毒结构相比,分辨率的提高是由于优化了病毒制备方法和数据处理技术。比较了 ZIKV 的糖蛋白相互作用和表面特性与其他蚊媒黄病毒结构。最大的结构差异和序列变异发生在与受体结合相关的糖基化环上。在病毒表面鉴定了可能的药物结合口袋。这些结果也为针对 ZIKV 的疫苗设计提供了结构基础。

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