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© Olivier Schwartz, Institut Pasteur
Publication : Proceedings of the National Academy of Sciences of the United States of America

Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody.

Team: Humoral Immunology
Member: Hugo Mouquet
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 17 May 2022

Torres JL, Ozorowski G, Andreano E, Liu H, Copps J, Piccini G, Donnici L, Conti M, Planchais C, Planas D, Manganaro N, Pantano E, Paciello I, Pileri P, Bruel T, Montomoli E, Mouquet H, Schwartz O, Sala C, De Francesco R, Wilson IA, Rappuoli R, Ward AB,

Link to Pubmed [PMID] – 35549549

Link to DOI – 10.1073/pnas.2120976119

Proc Natl Acad Sci U S A 2022 May; 119(20): e2120976119

SignificanceClinical candidate monoclonal antibody J08 binds the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) S-protein independent of known escape mutations and is able to potently neutralize most variants of concern (VoCs). Here, we explore these properties using cell-based assays and structural studies. A relatively small epitope footprint high on the receptor binding domain (RBD) ridge and the ability to bind multiple conformational states of the S-protein contribute to strong neutralization across several variants.