Structural Basis for Enhanced Infectivity and Immune Evasion of SARS-CoV-2 Variants

Overview

Journal Science

Specialty Science

Date 2021 Jun 25

PMID 34168070

Citations 143

Authors

Yongfei Cai

Jun Zhang

Tianshu Xiao

Christy L Lavine

Shaun Rawson

Hanqin Peng

Haisun Zhu

Krishna Anand

Pei Tong

Avneesh Gautam

Shen Lu

Sarah M Sterling

Richard M Walsh Jr

Sophia Rits-Volloch

Jianming Lu

Duane R Wesemann

Wei Yang

Michael S Seaman

Bing Chen

Affiliations

Soon will be listed here.

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.

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