Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants

doi:10.1126/science.abh1139

GSTDTAP > 气候变化

DOI	10.1126/science.abh1139
	Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
	Meng Yuan; Deli Huang; Chang-Chun D. Lee; Nicholas C. Wu; Abigail M. Jackson; Xueyong Zhu; Hejun Liu; Linghang Peng; Marit J. van Gils; Rogier W. Sanders; Dennis R. Burton; S. Momsen Reincke; Harald Prüss; Jakob Kreye; David Nemazee; Andrew B. Ward; Ian A. Wilson
	2021-08-13
发表期刊	Science
出版年	2021
英文摘要	Our key defense against the COVID-19 pandemic is neutralizing antibodies against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus elicited by natural infection or vaccination. Recent emerging viral variants have raised concern because of their potential to escape antibody neutralization. Wang et al. identified four antibodies from early-outbreak convalescent donors that are potent against 23 variants, including variants of concern, and characterized their binding to the spike protein of SARS-CoV-2. Yuan et al. examined the impact of emerging mutations in the receptor-binding domain of the spike protein on binding to the host receptor ACE2 and to a range of antibodies. These studies may be helpful for developing more broadly effective vaccines and therapeutic antibodies. Science , abh1766, this issue p. [eabh1766][1], abh1139, this issue p. [818][2] Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu484, Lys417, and Asn501 are mutated in variants first described in South Africa (B.1.351) and Brazil (P.1). We analyzed their effects on angiotensin-converting enzyme 2 binding, as well as the effects of two of these mutations (K417N and E484K) on nAbs isolated from COVID-19 patients. Binding and neutralization of the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2), which can both bind the RBS in alternative binding modes, are abrogated by K417N, E484K, or both. These effects can be structurally explained by their extensive interactions with RBS nAbs. However, nAbs to the more conserved, cross-neutralizing CR3022 and S309 sites were largely unaffected. The results have implications for next-generation vaccines and antibody therapies. [1]: /lookup/doi/10.1126/science.abh1766 [2]: /lookup/doi/10.1126/science.abh1139
领域	气候变化 ; 资源环境
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文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/335891
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Meng Yuan,Deli Huang,Chang-Chun D. Lee,et al. Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants[J]. Science,2021.
APA	Meng Yuan.,Deli Huang.,Chang-Chun D. Lee.,Nicholas C. Wu.,Abigail M. Jackson.,...&Ian A. Wilson.(2021).Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.Science.
MLA	Meng Yuan,et al."Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants".Science (2021).