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. 2024 Jul 30;14:17476. doi: 10.1038/s41598-024-68678-z

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Molecular interactions of wild-type and mutated structures with host cell receptors. (A) Interaction of wild-type RBD with ACE2. (B) Interaction of N481K mutated RBD with ACE2. (C) Interaction of wild-type RBD with CD147. (D) Interaction of R403K mutated RBD with CD147. (E) Interaction of wild-type RBD with CD209L. (F) Interaction of R403K mutated RBD with CD209L. (G) Interaction of wild-type NTD with AXL. (H) Interaction of R158G mutated NTD with AXL. (I) Interaction of L216F mutated NTD with AXL. Footnotes: ACE2 angiotensin-converting enzyme-2, NTD N-terminal domain, RBD receptor binding domain. AXL is a tyrosine-protein kinase receptor, with potential oncogenic properties; CD147 is an alternate receptor for SARS-CoV-2 entry into host cells with low ACE2 expression; CD209L can also act as a receptor for SARS-CoV-2 entry into susceptible host cells.