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. 2022 Nov 10;32(12):1068–1085. doi: 10.1038/s41422-022-00746-3

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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 Amino acid sequence of HR121. HR1 and HR2 peptide sequences were derived from the HR1 and HR2 domains, respectively, in the S protein of the prototype SARS-CoV-2 Wuhan-Hu-1 strain. HR121 monomer consists of HR1–linker 1–HR2–linker 2–HR1 segments (linker 1: GGSGG; linker 2: SGGRGG). Signal peptide (SP), N-terminal domain (NTD), and receptor-binding domain (RBD) in S1 subunit, and fusion peptide (FP), HR1 (aa 912–988), HR2 (aa 1163–1206), transmembrane domain (TM) and cytoplasmic domain (CP) in S2 subunit, were marked in the schematic diagram. b Purification of HR121. HR121 protein was purified using a Superdex 200 Increase 10/300 GL column; the profiles of the representative elution, SDS-PAGE and Native-PAGE were presented (the red arrows point the band of HR121 in SDS-PAGE and Native-PAGE gels); mAU in y-axis means milli-absorbance units. c, d Surface and cartoon representation of the atomic model of HR121 dimer. HR121 dimer consists of four HR1 (α1–α4) and two HR2. Front view (c) displayed the inner HR1 trimer (α1, α3 and α4) surrounded by two HR2s and one HR1 (α2), and back view (d) showed the two dominant-negative interfaces (between α2 and α3, α2 and α4) formed in the outer HR1 trimer (α2, α3 and α4). e GST pull-down assay showed that HR121 selectively bound to HR2, but not to HR1 (the red arrow at upper position points the band of GST-HR121, while red arrow at lower position points the band of HR2 or HR1). f Surface plasmon resonance recorded the profile of a real-time affinity of HR2 to HR121. g CD spectroscopic analysis showed that HR121 could interact with HR2 to form a more stable α-helix.