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. 2023 Jul 28;9:78. doi: 10.1038/s41421-023-00581-9

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© The Author(s) 2023

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. 5 — a Left: trimeric structures of BANAL-20-236, BANAL-20-52, and omicron BA.2.75S proteins, S1 of protomer A and S2 of protomer B were shown as ribbon, the rest of trimer was shown as surface presentation. Top, BANAL-20-236; middle, omicron BA.2.75; bottom, BANAL-20-52. Right: surface presentation of the S1 of protomer A (dark green) and the S2 of protomer B (gray). Omicron S PDB ID: 7YQW. b Magnified open flat book view of interface interaction of S1 of protomer A and S2 of protomer B. The first column: the side view of S1-S2 interface; the second and third columns: Open flat book view of interface interactions of S1 and S2 in the first column. Bright yellow, amino acid residues forming hydrogen bonds; red, amino acid residues involved in salt bridges; green, amino acid residues involved in hydrophobic interactions. c Top: the buried surface areas of all “closed” trimeric S proteins of BANAL-20-236, BANAL-20-52 and Omicron BA.2.75 at pH 5.5. Trimer: all buried surface areas; S1: areas of the interaction interface between S1 subunits only; S2: areas of the interaction interface between S2 subunits only; Trimer-(S1 + S2): Trimer column-S1 column-S2 column; S1 with S2: areas of interaction interface between S1 and S2. Bottom: the number of the residues involved in hydrogen bonding, salt bridge, and hydrophobic interaction at the interface of S1 and S2 interaction. Omicron BA.2.75S PDB ID: 7YQW. d Structural comparison of the 630 loop (rose) (BANAL-20-236: residues 611–641, BANAL-20-52: residues 615–645, Omicron: residues 615–645) and FPPR (green) (fusion peptide proximal region) (BANAL-20-236: residues 818–849, BANAL-20-52: residues 822–853, Omicron: residues 824–857). Dashed lines indicate the missing gaps. Omicron S PDB ID: 7YQW. e Top views of the trimeric S proteins of BANAL-20-236 and BANAL-20-52. The NAG moiety at N370 of S proteins was shown in red.