tetano
Editor, Senior Moderator
Science
. 2021 Jun 24;eabi9745.
doi: 10.1126/science.abi9745. Online ahead of print.
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Yongfei Cai[SUP] 1 2 3 [/SUP], Jun Zhang[SUP] 1 2 3 [/SUP], Tianshu Xiao[SUP] 1 2 3 [/SUP], Christy L Lavine[SUP] 4 [/SUP], Shaun Rawson[SUP] 5 6 7 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Haisun Zhu[SUP] 8 [/SUP], Krishna Anand[SUP] 8 [/SUP], Pei Tong[SUP] 9 [/SUP], Avneesh Gautam[SUP] 9 [/SUP], Shen Lu[SUP] 10 [/SUP], Sarah M Sterling[SUP] 6 7 [/SUP], Richard M Walsh Jr[SUP] 6 7 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Jianming Lu[SUP] 10 11 [/SUP], Duane R Wesemann[SUP] 9 [/SUP], Wei Yang[SUP] 8 [/SUP], Michael S Seaman[SUP] 4 [/SUP], Bing Chen[SUP] 12 2 [/SUP]
Affiliations
Abstract
Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-EM structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase the accessibility of its receptor binding domain and also the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.
. 2021 Jun 24;eabi9745.
doi: 10.1126/science.abi9745. Online ahead of print.
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Yongfei Cai[SUP] 1 2 3 [/SUP], Jun Zhang[SUP] 1 2 3 [/SUP], Tianshu Xiao[SUP] 1 2 3 [/SUP], Christy L Lavine[SUP] 4 [/SUP], Shaun Rawson[SUP] 5 6 7 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Haisun Zhu[SUP] 8 [/SUP], Krishna Anand[SUP] 8 [/SUP], Pei Tong[SUP] 9 [/SUP], Avneesh Gautam[SUP] 9 [/SUP], Shen Lu[SUP] 10 [/SUP], Sarah M Sterling[SUP] 6 7 [/SUP], Richard M Walsh Jr[SUP] 6 7 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Jianming Lu[SUP] 10 11 [/SUP], Duane R Wesemann[SUP] 9 [/SUP], Wei Yang[SUP] 8 [/SUP], Michael S Seaman[SUP] 4 [/SUP], Bing Chen[SUP] 12 2 [/SUP]
Affiliations
- PMID: 34168070
- DOI: 10.1126/science.abi9745
Abstract
Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-EM structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase the accessibility of its receptor binding domain and also the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.