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Basic Characteristics of Mutations
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Mutation Site
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D43V |
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Mutation Site Sentence
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These results indicated that the D43V substitution also affected the nuclear export of vRNPs, despite not being positioned within the NES. |
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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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Standardized Encoding Gene
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Genotype/Subtype
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H1N1 |
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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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Influenza A
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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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39817904
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Title
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Probing the functional constraints of influenza A virus NEP by deep mutational scanning
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Author
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Teo QW,Wang Y,Lv H,Oade MS,Mao KJ,Tan TJC,Huan YW,Rivera-Cardona J,Shao EK,Choi D,Wang C,Tavakoli Dargani Z,Brooke CB,Te Velthuis AJW,Wu NC
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Journal
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Cell reports
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Journal Info
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2025 Jan 28;44(1):115196
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Abstract
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The influenza A virus nuclear export protein (NEP) is a multifunctional protein that is essential for the viral life cycle and has very high sequence conservation. However, since the open reading frame of NEP largely overlaps with that of another influenza viral protein, non-structural protein 1, it is difficult to infer the functional constraints of NEP based on sequence conservation analysis. In addition, the N-terminal of NEP is structurally disordered, which further complicates the understanding of its function. Here, we systematically measure the replication fitness effects of >1,800 mutations of NEP. Our results show that the N-terminal domain has high mutational tolerance. Additional experiments show that N-terminal domain mutations affect viral transcription and replication dynamics, host cellular responses, and mammalian adaptation of avian influenza virus. Overall, our study not only advances the functional understanding of NEP but also provides insights into its evolutionary constraints.
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Sequence Data
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-
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