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《BioRxiv，3月17日，RBD mutations from circulating SARS-CoV-2 strains enhance the structure stability and infectivity of the spike protein》

  • 来源专题：COVID-19科研动态监测
  • 编译者： zhangmin
  • 发布时间：2020-03-18

  • RBD mutations from circulating SARS-CoV-2 strains enhance the structure stability and infectivity of the spike protein

    Junxian Ou, Zhonghua Zhou, Jing Zhang, Wendong Lan, Shan Zhao, Jianguo Wu, Donald Seto, Gong Zhang, Qiwei Zhang

    doi: https://doi.org/10.1101/2020.03.15.991844

    Abstract

    A novel zoonotic coronavirus SARS-CoV-2 is associated with the current global pandemic of Coronavirus Disease 2019 (COVID-19). Bats and pangolins are suspected as the reservoir and the intermediate host. The receptor binding domain (RBD) of the SARS-CoV-2 S protein plays the key role in the tight binding to human ACE2 for viral entry. In this study, we analyzed the worldwide RBD mutations and found 10 mutants revealed high positive selection pressure during the spread. The equilibrium dissociation constant (KD) of three RBD mutants were two orders of magnitude lower than the prototype Wuhan-Hu-1 strain due to the stabilization of the beta-sheet scaffold of the RBD.

    *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/10.1101/2020.03.15.991844v1
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  • 《BioRxiv，5月23日，Systemic Effects of Missense Mutations on SARS-CoV-2 Spike Glycoprotein Stability and Receptor Binding Affinity》
    • 来源专题：COVID-19科研动态监测
    • 编译者：zhangmin
    • 发布时间：2020-05-24
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