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. 2020 Nov 13;11:5752. doi: 10.1038/s41467-020-19568-1

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a The binding abilities of MW05 and MW07 to SARS-CoV-2 RBD recombinant protein were assessed by ELISA. b, c The abilities of MW05 and MW07 to block SARS-CoV-2 RBD interaction with ACE2 were evaluated by competition ELISA. d The binding of MW05 and MW07 to SARS-CoV-2 S protein expressed on HEK293 cells was measured by FACS. e The dissociation constants (K_d) of MW05 and MW07 to SARS-CoV-2 S1 recombinant protein were measured using a BIAcore S200 system. f The cross-reactivities of MW05 and MW07 to SARS-CoV-CoV-2, SARS-CoV, and MERS-CoV recombinant S1 subunit of spike proteins (S1) were tested by ELISA. g The binding of MW05 and MW07 to RBD recombinant proteins of SARS-CoV-2-mutated strains.