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. 2021 Apr 24;6:166. doi: 10.1038/s41392-021-00573-9

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© The Author(s) 2021

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 — The epitope profiling database constructed by using a peptide-based SARS-CoV-2 proteome microarray and its application. a Schematic illustration of epitope mapping using a peptide-based SARS-CoV-2 proteome microarray. b, c Distribution of antibody epitopes within the N and S proteins respectively. The x-axis represents the protein sequence. The y-axis represents the identification (ID) number (#number), host (mouse = M, rabbit = R, human = H) and clonality of the antibody (polyclonal antibody = PAb, monoclonal antibody = MAb). d, e Detection of the purified, full-length recombinant N protein using ELISA prepared with two antibody pairs selected from epitope mapping analyses. f, g Detection of the N protein from inactivated SARS-CoV-2 in cell culture using ELISA prepared with two antibody pairs selected from epitope mapping analyses. h The neutralization activity of antibody #26 using an S-RBD-ACE2 inhibition assay. i Structural analysis of the antibody #26 epitopes on SARS-CoV-2 RBD (PDB ID: 6m0j). j Neutralization activities of antibody #26 using a pseudovirus assay