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Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2

Tânia F. Custódio, Hrishikesh Das, Daniel J. Sheward, Leo Hanke, Samuel Pažický, Joanna Pieprzyk, Michèle Sorgenfrei, Martin A. Schroer, Andrey Gruzinov, Cy M. Jeffries, Melissa A. Graewert, Dmitri I. Svergun, Nikolay Dobrev, Kim Remans, Markus A. Seeger, Gerald M. McInerney, Ben Murrell, B.M. Hallberg, Christian Löw

2020Nature Communications164 citationsDOIOpen Access PDF

Abstract

Abstract The coronavirus SARS-CoV-2 is the cause of the ongoing COVID-19 pandemic. Therapeutic neutralizing antibodies constitute a key short-to-medium term approach to tackle COVID-19. However, traditional antibody production is hampered by long development times and costly production. Here, we report the rapid isolation and characterization of nanobodies from a synthetic library, known as sybodies (Sb), that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. Several binders with low nanomolar affinities and efficient neutralization activity were identified of which Sb23 displayed high affinity and neutralized pseudovirus with an IC 50 of 0.6 µg/ml. A cryo-EM structure of the spike bound to Sb23 showed that Sb23 binds competitively in the ACE2 binding site. Furthermore, the cryo-EM reconstruction revealed an unusual conformation of the spike where two RBDs are in the ‘up’ ACE2-binding conformation. The combined approach represents an alternative, fast workflow to select binders with neutralizing activity against newly emerging viruses.

Topics & Concepts

NeutralizationSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Computational biologyCoronavirus disease 2019 (COVID-19)Neutralizing antibodyAntibodyCoronavirusBinding siteChemistry2019-20 coronavirus outbreakPlasma protein bindingBinding affinitiesPillarVirologyBiologyVirusReceptorBiochemistryGeneticsMedicineOutbreakDiseaseInfectious disease (medical specialty)EngineeringPathologyStructural engineeringSARS-CoV-2 and COVID-19 ResearchMonoclonal and Polyclonal Antibodies ResearchBacteriophages and microbial interactions
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