Structural basis of a shared antibody response to SARS-CoV-2

doi:10.1126/science.abd2321

GSTDTAP > 气候变化

DOI	10.1126/science.abd2321
	Structural basis of a shared antibody response to SARS-CoV-2
	Meng Yuan; Hejun Liu; Nicholas C. Wu; Chang-Chun D. Lee; Xueyong Zhu; Fangzhu Zhao; Deli Huang; Wenli Yu; Yuanzi Hua; Henry Tien; Thomas F. Rogers; Elise Landais; Devin Sok; Joseph G. Jardine; Dennis R. Burton; Ian A. Wilson
	2020-08-28
发表期刊	Science
出版年	2020
英文摘要	In the fight against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), antibodies are a key tool, both as potential therapeutics and to guide vaccine development. Yuan et al. focused on finding shared antibody responses, in which multiple individuals develop antibodies against the same antigen using the same genetic elements and modes of recognition. The authors identified the immunoglobulin heavy-chain variable region 3-53 gene as the most frequently used among 294 antibodies that target the receptor-binding domain (RBD) of the viral spike protein. These antibodies have few somatic mutations, and crystal structures of two neutralizing antibodies bound to the RBD show that mostly germline-encoded residues are involved in binding. The minimal affinity maturation and high potency of these antibodies is promising for vaccine design. Science , this issue p. [1119][1] Molecular understanding of neutralizing antibody responses to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) could accelerate vaccine design and drug discovery. We analyzed 294 anti–SARS-CoV-2 antibodies and found that immunoglobulin G heavy-chain variable region 3-53 (IGHV3-53) is the most frequently used IGHV gene for targeting the receptor-binding domain (RBD) of the spike protein. Co-crystal structures of two IGHV3-53–neutralizing antibodies with RBD, with or without Fab CR3022, at 2.33- to 3.20-angstrom resolution revealed that the germline-encoded residues dominate recognition of the angiotensin I converting enzyme 2 (ACE2)–binding site. This binding mode limits the IGHV3-53 antibodies to short complementarity-determining region H3 loops but accommodates light-chain diversity. These IGHV3-53 antibodies show minimal affinity maturation and high potency, which is promising for vaccine design. Knowledge of these structural motifs and binding mode should facilitate the design of antigens that elicit this type of neutralizing response. [1]: /lookup/doi/10.1126/science.abd2321
领域	气候变化 ; 资源环境
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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/293232
专题	气候变化资源环境科学
推荐引用方式 GB/T 7714	Meng Yuan,Hejun Liu,Nicholas C. Wu,et al. Structural basis of a shared antibody response to SARS-CoV-2[J]. Science,2020.
APA	Meng Yuan.,Hejun Liu.,Nicholas C. Wu.,Chang-Chun D. Lee.,Xueyong Zhu.,...&Ian A. Wilson.(2020).Structural basis of a shared antibody response to SARS-CoV-2.Science.
MLA	Meng Yuan,et al."Structural basis of a shared antibody response to SARS-CoV-2".Science (2020).