N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
By
Matthew McCallum,
Anna De Marco,
Florian Lempp,
M. Alejandra Tortorici,
Dora Pinto,
Alexandra C Walls,
Martina Beltramello,
Alex Chen,
Zhuoming Liu,
Fabrizia Zatta,
Samantha Zepeda,
Julia di Iulio,
John E Bowen,
Martin Montiel-Ruiz,
Jiayi Zhou,
Laura Rosen,
Siro Bianchi,
Barbara Guarino,
Chiara Silacci Fregni,
Rana Abdelnabi,
Shi-Yan Caroline Foo,
Paul W Rothlauf,
Louis-Marie Bloyet,
Fabio Benigni,
Elisabetta Cameroni,
Johan Neyts,
Agostino Riva,
Gyorgy Snell,
Amalio Telenti,
Sean P.J. Whelan,
Herbert W Virgin,
Davide Corti,
Matteo Samuele Pizzuto,
David Veesler
Posted 14 Jan 2021
bioRxiv DOI: 10.1101/2021.01.14.426475
SARS-CoV-2 entry into host cells is orchestrated by the spike (S) glycoprotein that contains an immunodominant receptor-binding domain (RBD) targeted by the largest fraction of neutralizing antibodies (Abs) in COVID-19 patient plasma. Little is known about neutralizing Abs binding to epitopes outside the RBD and their contribution to protection. Here, we describe 41 human monoclonal Abs (mAbs) derived from memory B cells, which recognize the SARS-CoV-2 S N-terminal domain (NTD) and show that a subset of them neutralize SARS-CoV-2 ultrapotently. We define an antigenic map of the SARS-CoV-2 NTD and identify a supersite recognized by all known NTD-specific neutralizing mAbs. These mAbs inhibit cell-to-cell fusion, activate effector functions, and protect Syrian hamsters from SARS-CoV-2 challenge. SARS-CoV-2 variants, including the 501Y.V2 and B.1.1.7 lineages, harbor frequent mutations localized in the NTD supersite suggesting ongoing selective pressure and the importance of NTD-specific neutralizing mAbs to protective immunity.
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