Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Author(s) -
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 RitsVolloch,
Jianming Lü,
Duane R. Wesemann,
Wei Yang,
Michael S. Seaman,
Bing Chen
Publication year - 2021
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abi9745
Subject(s) - infectivity , biology , virology , antibody , virus , immune system , spike (software development) , evasion (ethics) , coronavirus , immunity , spike protein , covid-19 , mutation , genetics , gene , disease , medicine , infectious disease (medical specialty) , management , pathology , economics
SARS-CoV-2 from alpha to epsilon 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. Gobeilet 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; Caiet al . focused on the alpha and beta variants; and McCallumet 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. —VV
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