作者
M Alejandra Tortorici, Nadine Czudnochowski, Tyler N Starr, Roberta Marzi, Alexandra C Walls, Fabrizia Zatta, John E Bowen, Stefano Jaconi, Julia Di Iulio, Zhaoqian Wang, Anna De Marco, Samantha K Zepeda, Dora Pinto, Zhuoming Liu, Martina Beltramello, Istvan Bartha, Michael P Housley, Florian A Lempp, Laura E Rosen, Exequiel Dellota Jr, Hannah Kaiser, Martin Montiel-Ruiz, Jiayi Zhou, Amin Addetia, Barbara Guarino, Katja Culap, Nicole Sprugasci, Christian Saliba, Eneida Vetti, Isabella Giacchetto-Sasselli, Chiara Silacci Fregni, Rana Abdelnabi, Shi-Yan Caroline Foo, Colin Havenar-Daughton, Michael A Schmid, Fabio Benigni, Elisabetta Cameroni, Johan Neyts, Amalio Telenti, Herbert W Virgin, Sean PJ Whelan, Gyorgy Snell, Jesse D Bloom, Davide Corti, David Veesler, Matteo Samuele Pizzuto
发表日期
2021/9/2
期刊
Nature
卷号
597
期号
7874
页码范围
103-108
出版商
Nature Publishing Group UK
简介
The recent emergence of SARS-CoV-2 variants of concern, , , , , , , , – and the recurrent spillovers of coronaviruses, into the human population highlight the need for broadly neutralizing antibodies that are not affected by the ongoing antigenic drift and that can prevent or treat future zoonotic infections. Here we describe a human monoclonal antibody designated S2X259, which recognizes a highly conserved cryptic epitope of the receptor-binding domain and cross-reacts with spikes from all clades of sarbecovirus. S2X259 broadly neutralizes spike-mediated cell entry of SARS-CoV-2, including variants of concern (B.1.1.7, B.1.351, P.1, and B.1.427/B.1.429), as well as a wide spectrum of human and potentially zoonotic sarbecoviruses through inhibition of angiotensin-converting enzyme 2 (ACE2) binding to the receptor-binding domain. Furthermore, deep-mutational scanning and in vitro escape selection …
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