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. 2022 Nov 9;12:19089. doi: 10.1038/s41598-022-23342-2

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Stereo pair view of spike protein receptor trimer illustrating the locations of all Omicron spike protein mutations (excepting RBD contact surface mutations present in Fig. 5). Monomer A is blue, monomer B is salmon and monomer C is aquamarine. All mutated residues are rendered as CPK models. Yellow residues (S371L, S373P, S375F, K417N) are located in the RBD where they may alter domain packing and/or monomer–monomer interactions. Green residues (T547K, N764K, N856K, Q954H, N969K, L981F, I1081V) are located at or near monomer–monomer interfaces in the receptor trimer assembly. Red residues (A67V, T95I) are located in the interior of the N-terminal domain. Purple residues (N655Y, A701V, D796Y) are located on the exterior surface of the trimer assembly in regions that are potential antibody binding sites. The homology model is based on reference spike protein trimer structure PDB ID: 7KRS.