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TitleDiscovery of ultrapotent broadly neutralizing antibodies from SARS-CoV-2 elite neutralizers.
Journal, issue, pagesCell Host Microbe, Vol. 30, Issue 1, Page 69-82.e10, Year 2022
Publish dateJan 12, 2022
AuthorsKanika Vanshylla / Chengcheng Fan / Marie Wunsch / Nareshkumar Poopalasingam / Matthijs Meijers / Christoph Kreer / Franziska Kleipass / Denis Ruchnewitz / Meryem S Ercanoglu / Henning Gruell / Friederike Münn / Kai Pohl / Hanna Janicki / Tobias Nolden / Simone Bartl / Saskia C Stein / Max Augustin / Felix Dewald / Lutz Gieselmann / Philipp Schommers / Thomas F Schulz / Leif Erik Sander / Manuel Koch / Marta Łuksza / Michael Lässig / Pamela J Bjorkman / Florian Klein /
PubMed AbstractA fraction of COVID-19 convalescent individuals mount a potent antibody response to SARS-CoV-2 with cross-reactivity to SARS-CoV-1. To uncover their humoral response in detail, we performed single B ...A fraction of COVID-19 convalescent individuals mount a potent antibody response to SARS-CoV-2 with cross-reactivity to SARS-CoV-1. To uncover their humoral response in detail, we performed single B cell analysis from 10 SARS-CoV-2 elite neutralizers. We isolated and analyzed 126 monoclonal antibodies, many of which were sarbecovirus cross-reactive, with some displaying merbecovirus- and embecovirus-reactivity. Several isolated broadly neutralizing antibodies were effective against B.1.1.7, B.1.351, B.1.429, B.1.617, and B.1.617.2 variants and 19 prominent potential escape sites. Furthermore, assembly of 716,806 SARS-CoV-2 sequences predicted emerging escape variants, which were also effectively neutralized. One of these broadly neutralizing potent antibodies, R40-1G8, is a IGHV3-53 RBD-class-1 antibody. Remarkably, cryo-EM analysis revealed that R40-1G8 has a flexible binding mode, targeting both "up" and "down" conformations of the RBD. Given the threat of emerging SARS-CoV-2 variants, we demonstrate that elite neutralizers are a valuable source for isolating ultrapotent antibody candidates to prevent and treat SARS-CoV-2 infection.
External linksCell Host Microbe / PubMed:34973165 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

25008

7sc1

EMDB-25008, PDB-7sc1:
Structure of the SARS-CoV-2 S 6P trimer in complex with the human neutralizing antibody Fab fragment, R40-1G8
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / immune system / neutralizing antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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