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Basic Characteristics of Mutations
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Mutation Site
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N118K |
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Mutation Site Sentence
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Two amino acid substitutions of HBx were introduced to wild-type pHBV1.3 (gtB) and pHBV3.8 (gtC) plasmids to produce HBV variants, that is, HBV gtB mutant (N118K, E119D) and HBV gtC mutant (K118N, D119E). |
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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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X |
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Standardized Encoding Gene
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X
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Genotype/Subtype
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B;C |
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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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-
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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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31706164
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Title
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Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling
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Author
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Wang F,Shen F,Wang Y,Li Z,Chen J,Yuan Z
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Journal
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Virology
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Journal Info
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2020 Jan 2;539:92-103
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Abstract
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Hepatitis B virus (HBV) X protein (HBx) has been reported to counteract the innate immune responses through interfering with the pattern recognition receptors signaling activated by retinoic acid-inducible gene-I (RIG-I)-mitochondrial antiviral signaling protein (MAVS). Here, we showed that, compared to the HBx derived from genotype (gt) A, C and D, HBx of gtB exhibited more potent inhibitory activity on the RIG-I-MAVS-mediated interferon-beta promoter activation. Functional analysis of the genotype-associated differences in amino acid sequence and the reciprocal mutation experiments in transient-transfection and infection cell models revealed that HBx with asparagine (N) and glutamic acid (E) at 118-119 positions inhibited RIG-I signaling and interacted with MAVS more efficiently than that with lysine (K) and aspartic acid (D). An impaired RIG-I-induced MAVS aggregation was observed in the presence of HBx-118N119E while MAVS-TRAF3 interaction was not affected. These results implicated that HBx gene heterogeneity may affect the innate immune responses to HBV infection.
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Sequence Data
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-
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