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. 2022 Sep 17;13:5459. doi: 10.1038/s41467-022-33209-9

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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 The schematic representation of the SARS-CoV-2 Delta variant spike protein. Our RBD-HR/trimer protein includes a RBD (320–545 aa) derived from the Delta variant (containing L452R and T478K mutations) and HR1 (916–966 aa) and HR2 (1157–1203 aa) domain in subunit S2 of spike protein. SP signal peptide, NTD N-terminal domain, RBD receptor binding domain. HR1 and HR2 heptad repeats 1 and 2, TM transmembrane domain, CP cytoplasmic domain. b A representative elution chromatograph of the recombinant RBD-HR/trimer protein using a calibrated Superdex Increase 200 column. The SDS-PAGE and Western blotting analyses of the eluted RBD-HR/trimer protein were shown. mAU milli-absorbance units, M marker; 1, the eluted sample of the ascending part of the protein peak; 2, the eluted sample of the descending part of the peak. c Transmission electron micrographs (left) and a molecular model (right) of the RBD-HR/trimer protein with a bouquet-like shape. RBD-Delta is displayed in blue, HR1 in purple, and HR2 in green. d The analytical ultracentrifugation (AUC) assay of the recombinant RBD-HR/trimer protein. e The real-time binding profile between purified RBD-HR/trimer protein and receptor ACE2 was performed by surface plasmon resonance (Biacore). Scale bar represents 50 nm in (c). Source data are provided as a Source Data file.