EMD-24126
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
EMD-24126
Single-particle4.0 Å
Deposition: 28/05/2021Map released: 07/07/2021
Last modified: 30/10/2024
Sample Organism:
Severe acute respiratory syndrome coronavirus 2
Sample: one RBD-up-3 of pre-fusion SARS-CoV-2 B.1.1.7 spike variant glycoprotein
Fitted models: 7n1x (Avg. Q-score: 0.364)
Deposition Authors: Zhang J
,
Cai YF
Sample: one RBD-up-3 of pre-fusion SARS-CoV-2 B.1.1.7 spike variant glycoprotein
Fitted models: 7n1x (Avg. Q-score: 0.364)
Deposition Authors: Zhang J
,
Cai YF
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.
Cai Y ,
Zhang J ,
Xiao T ,
Lavine CL ,
Rawson S ,
Peng H ,
Zhu H ,
Anand K,
Tong P ,
Gautam A ,
Lu S,
Sterling SM ,
Walsh Jr RM ,
Rits-Volloch S,
Lu J,
Wesemann DR ,
Yang W ,
Seaman MS ,
Chen B
(2021) Science , 373 , 642 - 648
,
Zhang J ,
Xiao T ,
Lavine CL ,
Rawson S ,
Peng H ,
Zhu H ,
Anand K,
Tong P ,
Gautam A ,
Lu S,
Sterling SM ,
Walsh Jr RM ,
Rits-Volloch S,
Lu J,
Wesemann DR ,
Yang W ,
Seaman MS ,
Chen B
(2021) Science , 373 , 642 - 648
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-electron microscopy 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 both the accessibility of its receptor binding domain and 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.
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-electron microscopy 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 both the accessibility of its receptor binding domain and 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.