Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/200287
Title: | Omicron Mutations Increase Interdomain Interactions and Reduce Epitope Exposure in the SARS-CoV-2 Spike |
Author: | Wieczór, Milosz Tang, Phu K. Orozco López, Modesto Cossio, Pilar |
Keywords: | SARS-CoV-2 Bioinformàtica SARS-CoV-2 Bioinformatics |
Issue Date: | 17-Feb-2023 |
Publisher: | Cell Press |
Abstract: | Omicron BA.1 is a highly infectious variant of SARS-CoV-2 that carries more than thirty mutations on the spike protein in comparison to the Wuhan wild type (WT). Some of the Omicron mutations, located on the receptor binding domain (RBD), are exposed to the surrounding solvent and are known to help evade immunity. However, the impact of buried mutations on the RBD conformations and on the mechanics of the spike opening is less evident. Here, we use all-atom molecular dynamics (MD) simulations with metadynamics to characterize the thermodynamic RBD-opening ensemble, identifying significant differences between WT and Omicron. Specifically, the Omicron mutations S371L, S373P, and S375F make more RBD interdomain contacts during the spike's opening. Moreover, Omicron takes longer to reach the transition state than WT. It stabilizes up-state conformations with fewer RBD epitopes exposed to the solvent, potentially favoring immune or antibody evasion.© 2023 The Author(s). |
Note: | Reproducció del document publicat a: https://doi.org/10.1016/j.isci.2023.105981 |
It is part of: | Iscience, 2023, vol 26, num. 2 |
URI: | http://hdl.handle.net/2445/200287 |
Related resource: | https://doi.org/10.1016/j.isci.2023.105981 |
ISSN: | 2589-0042 |
Appears in Collections: | Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona)) |
Files in This Item:
File | Description | Size | Format | |
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Wieczor_Orozco et al_iScience_2023.pdf | 2.65 MB | Adobe PDF | View/Open |
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