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

doi:10.1126/science.abi9745

GSTDTAP > 气候变化

DOI	10.1126/science.abi9745
	Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
	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; Sophia Rits-Volloch; Jianming Lu; Duane R. Wesemann; Wei Yang; Michael S. Seaman; Bing Chen
	2021-08-06
发表期刊	Science
出版年	2021
英文摘要	As battles to contain the COVID-19 pandemic continue, attention is focused on emerging variants of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus that have been deemed variants of concern because they are resistant to antibodies elicited by infection or vaccination or they increase transmissibility or disease severity. Three papers used functional and structural studies to explore how mutations in the viral spike protein affect its ability to infect host cells and to evade host immunity. Gobeil et al. looked at a variant spike protein involved in transmission between minks and humans, as well as the B1.1.7 (alpha), B.1.351 (beta), and P1 (gamma) spike variants; Cai et al. focused on the alpha and beta variants; and McCallum et al. discuss the properties of the spike protein from the B1.1.427/B.1.429 (epsilon) variant. Together, these papers show a balance among mutations that enhance stability, those that increase binding to the human receptor ACE2, and those that confer resistance to neutralizing antibodies. Science , abi6226, abi9745, abi7994, this issue p. [641][1], p. [642][2], p. [648][3] 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. [1]: /lookup/volpage/373/641?iss=6555 [2]: /lookup/doi/10.1126/science.abi9745 [3]: /lookup/doi/10.1126/science.abi7994
领域	气候变化 ; 资源环境
URL	查看原文
引用统计
文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/335573
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Yongfei Cai,Jun Zhang,Tianshu Xiao,et al. Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants[J]. Science,2021.
APA	Yongfei Cai.,Jun Zhang.,Tianshu Xiao.,Christy L. Lavine.,Shaun Rawson.,...&Bing Chen.(2021).Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.Science.
MLA	Yongfei Cai,et al."Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants".Science (2021).