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Basic Characteristics of Mutations
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Mutation Site
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P373S |
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Mutation Site Sentence
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Moreover, we built OmicronRBD(L371S) and OmicronRBD(P373S), in which the mutation found in Omicron is reverted back to the residues present in the wtRBD while keeping all other mutations. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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RBD |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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Omicron(BA.1) |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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Cell line
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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37502147
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Title
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S373P Mutation Stabilizes the Receptor-Binding Domain of the Spike Protein in Omicron and Promotes Binding
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Author
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Zheng B,Xiao Y,Tong B,Mao Y,Ge R,Tian F,Dong X,Zheng P
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Journal
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JACS Au
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Journal Info
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2023 Jun 22;3(7):1902-1910
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Abstract
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A cluster of several newly occurring mutations on Omicron is found at the beta-core region of the spike protein's receptor-binding domain (RBD), where mutation rarely happened before. Notably, the binding of SARS-CoV-2 to human receptor ACE2 via RBD happens in a dynamic airway environment, where mechanical force caused by coughing or sneezing occurs. Thus, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the stability of RBDs and found that the mechanical stability of Omicron RBD increased by approximately 20% compared with the wild type. Molecular dynamics (MD) simulations revealed that Omicron RBD showed more hydrogen bonds in the beta-core region due to the closing of the alpha-helical motif caused primarily by the S373P mutation. In addition to a higher unfolding force, we showed a higher dissociation force between Omicron RBD and ACE2. This work reveals the mechanically stabilizing effect of the conserved mutation S373P for Omicron and the possible evolution trend of the beta-core region of RBD.
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Sequence Data
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-
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