Abstract
We demonstrate that novel bat HL17NL10 and HL18NL11 influenza virus NS1 proteins are effective interferon antagonists but do not block general host gene expression. Solving the RNA-binding domain structures revealed the canonical NS1 symmetrical homodimer, and RNA binding required conserved basic residues in this domain. Interferon antagonism was strictly dependent on RNA binding, and chimeric bat influenza viruses expressing NS1s defective in this activity were highly attenuated in interferon-competent cells but not in cells unable to establish antiviral immunity.
Copyright © 2015, American Society for Microbiology. All Rights Reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chiroptera / virology*
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Gene Expression Regulation
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Host-Pathogen Interactions
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Immunity, Innate
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Influenza A virus / genetics*
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Influenza A virus / immunology
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Interferon-beta / genetics
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Interferon-beta / immunology
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Models, Molecular
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Orthomyxoviridae Infections / genetics
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Orthomyxoviridae Infections / immunology
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Orthomyxoviridae Infections / veterinary*
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Orthomyxoviridae Infections / virology
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Protein Binding
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / immunology
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Protein Structure, Secondary
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Protein Structure, Tertiary
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RNA, Double-Stranded / chemistry*
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RNA, Double-Stranded / immunology
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RNA, Double-Stranded / metabolism
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / immunology
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Signal Transduction
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Viral Nonstructural Proteins / chemistry*
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Viral Nonstructural Proteins / genetics
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Viral Nonstructural Proteins / immunology
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Virus Replication
Substances
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INS1 protein, influenza virus
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Protein Isoforms
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RNA, Double-Stranded
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RNA-Binding Proteins
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Viral Nonstructural Proteins
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Interferon-beta