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Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escape

biorxiv. 2021-04; 
Tyler N Starr, Nadine Czudnochowski, Fabrizia Zatta, Young-Jun Park, Zhuoming Liu, Amin Addetia, Dora Pinto, Martina Beltramello, Patrick Hernandez, Allison J Greaney, Roberta Marzi, William G Glass, Ivy Zhang, Adam S Dingens, John E Bowen, Jason A Wojcechowskyj, Anna De Marco, Laura E Rosen, Jiayi Zhou, Martin Montiel-Ruiz, Hannah Kaiser, Heather Tucker, Michael P Housley, Julia di Iulio, Gloria Lombardo, Maria Agostini, Nicole Sprugasci, Katja Culap, Stefano Jaconi, Marcel Meury, Exequiel Dellota, Elisabetta Cameroni, Tristan I Croll, Jay C Nix, Colin Havenar-Daughton, Amalio Telenti, Florian A Lempp, Matteo S Pizzuto, John D Chodera, Christy M Hebner, Sean P J Whelan, Herbert W Virgin, David Veesler, Davide Corti, Jesse D Bloom, Gyorgy Snell
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Recombinant Antibody Expression … SARS-CoV-2 RBD and flow cytometry to identify the EC90 of each antibody’s binding to yeast-displayed SARS-CoV-2 RBD. … from IDT, Twist, and Genscript, and cloned into our yeast … Get A Quote

摘要

An ideal anti-SARS-CoV-2 antibody would resist viral escape , have activity against diverse SARS-related coronaviruses , and be highly protective through viral neutralization and effector functions . Understanding how these properties relate to each other and vary across epitopes would aid development of antibody therapeutics and guide vaccine design. Here, we comprehensively characterize escape, breadth, and potency across a panel of SARS-CoV-2 antibodies targeting the receptor-binding domain (RBD), including S309 , the parental antibody of the late-stage clinical antibody VIR-7831. We observe a tradeoff between SARS-CoV-2 neutralization potency and breadth of binding across SARS-related coronaviruses. N... More

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