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Basic Characteristics of Mutations
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Mutation Site
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I138V |
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Mutation Site Sentence
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The mutations exchanged codons AGG (7944 to 7946), ATA (8056 to 8058), and AGC (8161 to 8163) to AAG, GTG, and GGC, generating the amino acid changes NS5 R101K, I138V, and S173G, respectively. |
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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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NS5 |
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Standardized Encoding Gene
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NS5
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Genotype/Subtype
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South America I |
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Viral Reference
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KY885000
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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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IFNA1
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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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Brazil |
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Literature Information
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PMID
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36680231
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Title
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Amino Acid Polymorphisms on the Brazilian Strain of Yellow Fever Virus Methyltransferase Are Related to the Host's Immune Evasion Mediated by Type I Interferon
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Author
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Furtado ND,de Mello IS,de Godoy AS,Noske GD,Oliva G,Canard B,Decroly E,Bonaldo MC
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Journal
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Viruses
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Journal Info
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2023 Jan 10;15(1):191
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Abstract
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Since late 2016, a yellow fever virus (YFV) variant carrying a set of nine amino acid variations has circulated in South America. Three of them were mapped on the methyltransferase (MTase) domain of viral NS5 protein. To assess whether these changes affected viral infectivity, we synthesized YFV carrying the MTase of circulating lineage as well as its isoform with the residues of the previous strains (NS5 K101R, NS5 V138I, and NS5 G173S). We observed a slight difference in viral growth properties and plaque phenotype between the two synthetic YFVs. However, the MTase polymorphisms associated with the Brazilian strain of YFV (2016-2019) confer more susceptibility to the IFN-I. In addition, in vitro MTase assay revealed that the interaction between the YFV MTase and the methyl donor molecule (SAM) is altered in the Brazilian MTase variant. Altogether, the results reported here describe that the MTase carrying the molecular signature of the Brazilian YFV circulating since 2016 might display a slight decrease in its catalytic activity but virtually no effect on viral fitness in the parameters comprised in this study. The most marked influence of these residues stands in the immune escape against the antiviral response mediated by IFN-I.
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Sequence Data
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-
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