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Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.

Authors :
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 RM
Rits-Volloch S
Lu J
Wesemann DR
Yang W
Seaman MS
Chen B
Source :
BioRxiv : the preprint server for biology [bioRxiv] 2021 Apr 14. Date of Electronic Publication: 2021 Apr 14.
Publication Year :
2021

Abstract

Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains that continue to fuel the COVID-19 pandemic despite intensive vaccination efforts throughout the world. 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. Mutations 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 can account for the increased transmissibility and risk of mortality as the variant may begin to infect efficiently infect additional cell types expressing low levels of ACE2. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, rendering complete resistance to some potent neutralizing antibodies. These findings provide structural details on how the wide spread of SARS-CoV-2 enables rapid evolution to enhance viral fitness and immune evasion. They may guide intervention strategies to control the pandemic.

Details

Language :
English
Database :
MEDLINE
Journal :
BioRxiv : the preprint server for biology
Accession number :
33880477
Full Text :
https://doi.org/10.1101/2021.04.13.439709