| Structural highlights
Publication Abstract from PubMed
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.
Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody.,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 Proc Natl Acad Sci U S A. 2022 May 17;119(20):e2120976119. doi:, 10.1073/pnas.2120976119. Epub 2022 May 12. PMID:35549549[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ 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. Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody. Proc Natl Acad Sci U S A. 2022 May 17;119(20):e2120976119. doi:, 10.1073/pnas.2120976119. Epub 2022 May 12. PMID:35549549 doi:http://dx.doi.org/10.1073/pnas.2120976119
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