Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry

Here, the authors compare the crystal structures and investigate the neutralization mechanisms of three neutralizing antibodies against SARS-CoV-2 and find that one antibody, P2C-1F11, closely mimics binding of receptor ACE2 and displays the most potent neutralizing activity in vitro, as well as con...

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Autores principales:	Jiwan Ge, Ruoke Wang, Bin Ju, Qi Zhang, Jing Sun, Peng Chen, Senyan Zhang, Yuling Tian, Sisi Shan, Lin Cheng, Bing Zhou, Shuo Song, Juanjuan Zhao, Haiyan Wang, Xuanling Shi, Qiang Ding, Lei Liu, Jincun Zhao, Zheng Zhang, Xinquan Wang, Linqi Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/838f1d2ad0e443bda1e93e6840e828b9
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spelling	oai:doaj.org-article:838f1d2ad0e443bda1e93e6840e828b92021-12-02T15:22:39ZAntibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry10.1038/s41467-020-20501-92041-1723https://doaj.org/article/838f1d2ad0e443bda1e93e6840e828b92021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20501-9https://doaj.org/toc/2041-1723Here, the authors compare the crystal structures and investigate the neutralization mechanisms of three neutralizing antibodies against SARS-CoV-2 and find that one antibody, P2C-1F11, closely mimics binding of receptor ACE2 and displays the most potent neutralizing activity in vitro, as well as conferring protection against SARS-CoV-2 infection in Ad5-hACE2-sensitized mice.Jiwan GeRuoke WangBin JuQi ZhangJing SunPeng ChenSenyan ZhangYuling TianSisi ShanLin ChengBing ZhouShuo SongJuanjuan ZhaoHaiyan WangXuanling ShiQiang DingLei LiuJincun ZhaoZheng ZhangXinquan WangLinqi ZhangNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jiwan Ge Ruoke Wang Bin Ju Qi Zhang Jing Sun Peng Chen Senyan Zhang Yuling Tian Sisi Shan Lin Cheng Bing Zhou Shuo Song Juanjuan Zhao Haiyan Wang Xuanling Shi Qiang Ding Lei Liu Jincun Zhao Zheng Zhang Xinquan Wang Linqi Zhang Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
description	Here, the authors compare the crystal structures and investigate the neutralization mechanisms of three neutralizing antibodies against SARS-CoV-2 and find that one antibody, P2C-1F11, closely mimics binding of receptor ACE2 and displays the most potent neutralizing activity in vitro, as well as conferring protection against SARS-CoV-2 infection in Ad5-hACE2-sensitized mice.
format	article
author	Jiwan Ge Ruoke Wang Bin Ju Qi Zhang Jing Sun Peng Chen Senyan Zhang Yuling Tian Sisi Shan Lin Cheng Bing Zhou Shuo Song Juanjuan Zhao Haiyan Wang Xuanling Shi Qiang Ding Lei Liu Jincun Zhao Zheng Zhang Xinquan Wang Linqi Zhang
author_facet	Jiwan Ge Ruoke Wang Bin Ju Qi Zhang Jing Sun Peng Chen Senyan Zhang Yuling Tian Sisi Shan Lin Cheng Bing Zhou Shuo Song Juanjuan Zhao Haiyan Wang Xuanling Shi Qiang Ding Lei Liu Jincun Zhao Zheng Zhang Xinquan Wang Linqi Zhang
author_sort	Jiwan Ge
title	Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
title_short	Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
title_full	Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
title_fullStr	Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
title_full_unstemmed	Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
title_sort	antibody neutralization of sars-cov-2 through ace2 receptor mimicry
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/838f1d2ad0e443bda1e93e6840e828b9
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Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry

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