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《BioRxiv，3月7日，Cryo-electron microscopy structure of the SADS-CoV spike glycoprotein provides insights into an evolution of unique coronavirus spike proteins》

  • 来源专题：COVID-19科研动态监测
  • 编译者： zhangmin
  • 发布时间：2020-03-08

  • Cryo-electron microscopy structure of the SADS-CoV spike glycoprotein provides insights into an evolution of unique coronavirus spike proteins

    Songying Ouyang

    doi: https://doi.org/10.1101/2020.03.04.976258

    Abstract

    The outbreak of a novel betacoronavirus (SARS-CoV-2) has aroused great public health concern. As a new coronavirus which was responsible for a large-scale outbreak of fatal disease in piglets in China, swine acute diarrhea syndrome coronavirus (SADS-CoV) originated from the same genus of horseshoe bats (Rhinolophus) as SARS-CoV and possesses a broad species tropism. In addition to human cells, it can also infect cell lines from diverse species. Given the importance of the spike glycoprotein (S) protein in viral entry and host immune responses, here we report the cryo-EM structure of the SADS-CoV S in the prefusion conformation at a resolution of 3.55 angstrom. Our studies reveal that SADS-CoV S structure takes an intra-subunit quaternary packing mode where the NTD and CTD from the same subunit pack together by facing each other. The comparison of NTD and CTD with that of the other four genera gives the suggestion of the evolutionary procedure of the SADS-CoV S.

    *注，本文为预印本论文手稿，是未经同行评审的初步报告，其观点仅供科研同行交流，并不是结论性内容，请使用者谨慎使用.

  • 原文来源：https://www.biorxiv.org/content/10.1101/2020.03.04.976258v1
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