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《Cell，7月17日，The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity》

  • 来源专题：COVID-19科研动态监测
  • 编译者： zhangmin
  • 发布时间：2020-07-28

  • The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity

    Qianqian Li 5

    Jiajing Wu 5

    Jianhui Nie 5

    Xuguang Li

    Weijin Huang

    Youchun Wang 6

    Published:July 17, 2020DOI:https://doi.org/10.1016/j.cell.2020.07.012

    Summary

    The spike protein of SARS-CoV-2 has been undergoing mutations and is highly glycosylated. It is critically important to investigate the biological significance of these mutations. Here we investigated 80 variants and 26 glycosylation site modifications for the infectivity and reactivity to a panel of neutralizing antibodies and sera from convalescent patients. D614G, along with several variants containing both D614G and another amino acid change, were significantly more infectious. Most variants with amino acid change at receptor binding domain were less infectious but variants including A475V, L452R, V483A and F490L became resistant to some neutralizing antibodies. Moreover, the majority of glycosylation deletions were less infectious whilst deletion of both N331 and N343 glycosylation drastically reduced infectivity, revealing the importance of glycosylation for viral infectivity. Interestingly, N234Q was markedly resistant to neutralizing antibodies, whereas N165Q became more sensitive. These findings could be of value in the development of vaccine and therapeutic antibodies.

  • 原文来源：https://www.cell.com/cell/fulltext/S0092-8674(20)30877-1#
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    • 编译者：zhangmin
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