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Basic Characteristics of Mutations
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Mutation Site
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D405N |
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Mutation Site Sentence
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The D405N mutation on the Omicron subvariant spike proteins, resulting in an RGN motif, has recently been shown to inhibit binding to integrin alphaVbeta3. |
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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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S |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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Omicron |
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Viral Reference
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P0DTC2
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Functional Impact and Mechanisms
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Disease
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COVID-19
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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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37178506
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Title
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SARS-CoV-2 Omicron subvariant spike N405 unlikely to rapidly deamidate
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Author
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Beaudoin CA,Petsolari E,Hamaia SW,Hala S,Alofi FS,Pandurangan AP,Blundell TL,Chaitanya Vedithi S,Huang CL,Jackson AP
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Journal
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Biochemical and biophysical research communications
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Journal Info
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2023 Jul 23;666:61-67
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Abstract
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The RGD motif on the SARS-CoV-2 spike protein has been suggested to interact with RGD-binding integrins alphaVbeta3 and alpha5beta1 to enhance viral cell entry and alter downstream signaling cascades. The D405N mutation on the Omicron subvariant spike proteins, resulting in an RGN motif, has recently been shown to inhibit binding to integrin alphaVbeta3. Deamidation of asparagines in protein ligand RGN motifs has been demonstrated to generate RGD and RGisoD motifs that permit binding to RGD-binding integrins. Two asparagines, N481 and N501, on the Wild-type spike receptor-binding domain have been previously shown to have deamidation half-lives of 16.5 and 123 days, respectively, which may occur during the viral life cycle. Deamidation of Omicron subvariant N405 may recover the ability to interact with RGD-binding integrins. Thus, herein, all-atom molecular dynamics simulations of the Wild-type and Omicron subvariant spike protein receptor-binding domains were conducted to investigate the potential for asparagines, the Omicron subvariant N405 in particular, to assume the optimized geometry for deamidation to occur. In summary, the Omicron subvariant N405 was primarily found to be stabilized in a state unfavourable for deamidation after hydrogen bonding with downstream E406. Nevertheless, a small number of RGD or RGisoD motifs on the Omicron subvariant spike proteins may restore the ability to interact with RGD-binding integrins. The simulations also provided structural clarification regarding the deamidation rates of Wild-type N481 and N501 and highlighted the utility of tertiary structure dynamics information in predicting asparagine deamidation. Further work is needed to characterize the effects of deamidation on spike-integrin interactions.
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Sequence Data
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Delta (QUD52764);Omicron BA.1 (UFO69279);Omicron BA.2 (UJP23605); BA.4 (UPP14409);BA.5 (UOZ45804); XBB.1.5 (WBG51102)
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