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Basic Characteristics of Mutations
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Mutation Site
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S206A |
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Mutation Site Sentence
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We found that R203M, present in the SARS-CoV-2 Delta variant, and R203K and R203K/G204R, found in all lineage B.1.1 variants, reduced phosphorylation in this assay to a level equivalent to S206A, suggesting a substantial decrease in N protein phosphorylation in these variants (Figs 1C, 1D, and S1A). |
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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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N |
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Standardized Encoding Gene
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N
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Genotype/Subtype
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- |
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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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39571001
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Title
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SARS-CoV-2 evolution balances conflicting roles of N protein phosphorylation
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Author
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Syed AM,Ciling A,Chen IP,Carlson CR,Adly AN,Martin HS,Taha TY,Khalid MM,Price N,Bouhaddou M,Ummadi MR,Moen JM,Krogan NJ,Morgan DO,Ott M,Doudna JA
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Journal
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PLoS pathogens
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Journal Info
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2024 Nov 21;20(11):e1012741
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Abstract
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All lineages of SARS-CoV-2, the coronavirus responsible for the COVID-19 pandemic, contain mutations between amino acids 199 and 205 in the nucleocapsid (N) protein that are associated with increased infectivity. The effects of these mutations have been difficult to determine because N protein contributes to both viral replication and viral particle assembly during infection. Here, we used single-cycle infection and virus-like particle assays to show that N protein phosphorylation has opposing effects on viral assembly and genome replication. Ancestral SARS-CoV-2 N protein is densely phosphorylated, leading to higher levels of genome replication but 10-fold lower particle assembly compared to evolved variants with low N protein phosphorylation, such as Delta (N:R203M), Iota (N:S202R), and B.1.2 (N:P199L). A new open reading frame encoding a truncated N protein called N*, which occurs in the B.1.1 lineage and subsequent lineages of the Alpha, Gamma, and Omicron variants, supports high levels of both assembly and replication. Our findings help explain the enhanced fitness of viral variants of concern and a potential avenue for continued viral selection.
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Sequence Data
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-
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