Abstract
Viruses evolve multiple ways to interfere with NF-κB signaling, a key regulator of innate and adaptive immunity. Enterovirus 71 (EV71) is one of primary pathogens that cause hand-foot-mouth disease. Here, we identify RelA(p65) as a novel binding partner for EV71 2C protein from yeast two-hybrid screen. By interaction with IPT domain of p65, 2C reduces the formation of heterodimer p65/p50, the predominant form of NF-κB. We also show that picornavirus 2C family proteins inhibit NF-κB activation and associate with p65 and IKKβ. Our findings provide a novel mechanism how EV71 antagonizes innate immunity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites / genetics
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Carrier Proteins / metabolism*
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Cell Line, Tumor
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Enterovirus A, Human / metabolism*
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Enzyme Activation
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HEK293 Cells
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Humans
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I-kappa B Kinase / metabolism
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Immune Evasion / immunology*
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Immune Evasion / physiology
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NF-kappa B p50 Subunit / metabolism*
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Protein Binding / physiology
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Saccharomyces cerevisiae / genetics
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Transcription Factor RelA / metabolism*
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Two-Hybrid System Techniques
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Viral Nonstructural Proteins / metabolism*
Substances
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Carrier Proteins
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NF-kappa B p50 Subunit
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Transcription Factor RelA
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Viral Nonstructural Proteins
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I-kappa B Kinase
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2C protein, viral