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. 2023 Jan 13;87(12-13):1662–1678. doi: 10.1134/S0006297922120215

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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 https://creativecommons.org/licenses/by/4.0/.

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Fig. 7. — Domain organization of S protein and its participation in the fusion of a viral particle with a cell. 3D (a) and primary (b) structure of the SARS-CoV-2 S protein. The following domains are recognized within the S1 and S2 subunits: NTD, N-terminal domain; RBD, receptor-binding domain; FP fusion peptide; HR1 and HR2 domains; transmembrane and cytoplasmic domains. c) Scheme of interaction between a cell and a coronavirus particle. S protein located on the surface of the viral membrane finds the corresponding receptor on the cell membrane. After their interaction with each other, cellular protease cleaves the S protein at the S1/S2 and S2′ sites. This results in the release of the activated S2 subunit with the FP fusion peptide protruding towards the cell. The peptide is integrated into the cell membrane, the HR1 and HR2 domains interact with each other, “pulling” both membranes close to each other.