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. 2022 Apr 21;8:36. doi: 10.1038/s41421-022-00401-6

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© The Author(s) 2022

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 Binding of five mAbs isolated from COVID-19 patients to the RBD proteins of SARS-CoV-2, RaTG13, GD-Pangolin, GX-Pangolin, and SARS-CoV in ELISA. b Binding affinity of GW01 to RBD proteins of SARS-CoV-2, RaTG13, GD-Pangolin, GX-Pangolin, or SARS-CoV was measured by bilayer interferometry experiments. c Neutralization of mAbs against pseudovirus of SARS-CoV-2 and its variants B.1.1.7, B.1.351, B.1.617.1, B.1.617.2, B.1.1.529, and C.37, SARS-CoV, and bat SARSr-CoVs (WIV1 and Rs3367). d Neutralization summary of GW01, S309, and other NAbs against pseudoviruses. e Neutralization of GW01 against authentic SARS-CoV-2 and its variants B.1.1.7, B.1.351, B.1.617.2, and B.1.525. f Neutralization of GW01 against authentic bat SARSr-CoVs (WIV1 and SHC014). g IC₅₀s of GW01 against seven authentic viruses.