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. 2022 May 28;19:96. doi: 10.1186/s12985-022-01827-w

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — A pair of noncompeting mAbs binding to the SARS-CoV-2 and SARS-CoV NPs. a Binding affinities of P301-F7 and P301-H5 to NPs of SARS-CoV-2 (upper) and SARS-CoV (lower) by SPR. The data are means of three independent experiments. b Gene family analysis of P301-F7 and P301-H5. c P301-F7 and P301-H5 bound to two distinct epitopes on the SARS-CoV-2 NP (upper) and SARS-CoV NP (lower) by competition SPR. The experiment was performed twice and one representative result was shown. d Predicted model of the SARS-CoV-2 NP recognized by P301-F7 (brown) and P301-H5 (purple). The model was predicted using Alphafold 2.0 based on the N-terminal and C-terminal molecular structures (PDB codes: 7CDZ and 7CE0)