The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
- PMID: 32730807
- PMCID: PMC7366990
- DOI: 10.1016/j.cell.2020.07.012
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Abstract
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, whereas 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.
Keywords: COVID-19; SARS-CoV-2; glycosylation; mutants; pseudotyped virus; spike; variants.
Copyright © 2020 Elsevier Inc. All rights reserved.
Conflict of interest statement
Declaration of Interests The authors declare no competing interests.
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Comment in
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Profiling and characterization of SARS-CoV-2 mutants' infectivity and antigenicity.Signal Transduct Target Ther. 2020 Sep 3;5(1):185. doi: 10.1038/s41392-020-00302-8. Signal Transduct Target Ther. 2020. PMID: 32883949 Free PMC article. No abstract available.
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Cellular tropism and antigenicity of mink-derived SARS-CoV-2 variants.Signal Transduct Target Ther. 2021 May 17;6(1):196. doi: 10.1038/s41392-021-00617-0. Signal Transduct Target Ther. 2021. PMID: 34001855 Free PMC article. No abstract available.
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