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. 2022 Jul 22;7:81. doi: 10.1038/s41541-022-00486-w

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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. 6 — A SDS-PAGE under denaturating conditions, all proteins show monomeric structures at an expected size of ~60 kDa. BSA was included as a monomer control. B SDS-PAGE using a BS3 crosslinker. N1-MPP, N2-MPP and B-NA-MPP show tetrameric structures at around 240 kDa. BSA was included as a monomer control. C ELISA against rec. N2-MPP using a broad panel of human anti-N2 mAbs to verify correct presentation of epitopes. D ELISA against rec. B-NA-MPP using a broad panel of human anti-B-NA mAbs to verify correct presentation of epitopes. E Enzymatic activity of N1-MPP, N2-MPP, B-NA-MPP was determined via NA-Star assay. Assays in C to E were run once in duplicates and the duplicates were used to calculate one area under the curve (AUC) value.