Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling
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, compare...
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| Autor*in: |
Wang, Fan [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
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| Schlagwörter: |
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| Umfang: |
12 |
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| Übergeordnetes Werk: |
Enthalten in: Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions - Xie, Bingyang ELSEVIER, 2022, San Diego, Calif. [u.a.] |
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| Übergeordnetes Werk: |
volume:539 ; year:2020 ; day:2 ; month:01 ; pages:92-103 ; extent:12 |
| Links: |
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| DOI / URN: |
10.1016/j.virol.2019.10.009 |
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| 245 | 1 | 0 | |a 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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| 520 | |a 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-β 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. | ||
| 520 | |a 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-β 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. | ||
| 650 | 7 | |a PRR signaling |2 Elsevier | |
| 650 | 7 | |a Genotype |2 Elsevier | |
| 650 | 7 | |a Interferon |2 Elsevier | |
| 650 | 7 | |a HBV |2 Elsevier | |
| 650 | 7 | |a HBx |2 Elsevier | |
| 700 | 1 | |a Shen, Fang |4 oth | |
| 700 | 1 | |a Wang, Yang |4 oth | |
| 700 | 1 | |a Li, Ze |4 oth | |
| 700 | 1 | |a Chen, Jieliang |4 oth | |
| 700 | 1 | |a Yuan, Zhenghong |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Xie, Bingyang ELSEVIER |t Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions |d 2022 |g San Diego, Calif. [u.a.] |w (DE-627)ELV008536686 |
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10.1016/j.virol.2019.10.009 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001292.pica (DE-627)ELV048555088 (ELSEVIER)S0042-6822(19)30299-5 DE-627 ger DE-627 rakwb eng 600 690 VZ 51.00 bkl 51.32 bkl Wang, Fan verfasserin aut Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling 2020transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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-β 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. 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-β 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. PRR signaling Elsevier Genotype Elsevier Interferon Elsevier HBV Elsevier HBx Elsevier Shen, Fang oth Wang, Yang oth Li, Ze oth Chen, Jieliang oth Yuan, Zhenghong oth Enthalten in Elsevier Xie, Bingyang ELSEVIER Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions 2022 San Diego, Calif. [u.a.] (DE-627)ELV008536686 volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 https://doi.org/10.1016/j.virol.2019.10.009 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.00 Werkstoffkunde: Allgemeines VZ 51.32 Werkstoffmechanik VZ AR 539 2020 2 0102 92-103 12 |
| spelling |
10.1016/j.virol.2019.10.009 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001292.pica (DE-627)ELV048555088 (ELSEVIER)S0042-6822(19)30299-5 DE-627 ger DE-627 rakwb eng 600 690 VZ 51.00 bkl 51.32 bkl Wang, Fan verfasserin aut Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling 2020transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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-β 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. 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-β 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. PRR signaling Elsevier Genotype Elsevier Interferon Elsevier HBV Elsevier HBx Elsevier Shen, Fang oth Wang, Yang oth Li, Ze oth Chen, Jieliang oth Yuan, Zhenghong oth Enthalten in Elsevier Xie, Bingyang ELSEVIER Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions 2022 San Diego, Calif. [u.a.] (DE-627)ELV008536686 volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 https://doi.org/10.1016/j.virol.2019.10.009 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.00 Werkstoffkunde: Allgemeines VZ 51.32 Werkstoffmechanik VZ AR 539 2020 2 0102 92-103 12 |
| allfields_unstemmed |
10.1016/j.virol.2019.10.009 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001292.pica (DE-627)ELV048555088 (ELSEVIER)S0042-6822(19)30299-5 DE-627 ger DE-627 rakwb eng 600 690 VZ 51.00 bkl 51.32 bkl Wang, Fan verfasserin aut Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling 2020transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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-β 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. 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-β 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. PRR signaling Elsevier Genotype Elsevier Interferon Elsevier HBV Elsevier HBx Elsevier Shen, Fang oth Wang, Yang oth Li, Ze oth Chen, Jieliang oth Yuan, Zhenghong oth Enthalten in Elsevier Xie, Bingyang ELSEVIER Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions 2022 San Diego, Calif. [u.a.] (DE-627)ELV008536686 volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 https://doi.org/10.1016/j.virol.2019.10.009 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.00 Werkstoffkunde: Allgemeines VZ 51.32 Werkstoffmechanik VZ AR 539 2020 2 0102 92-103 12 |
| allfieldsGer |
10.1016/j.virol.2019.10.009 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001292.pica (DE-627)ELV048555088 (ELSEVIER)S0042-6822(19)30299-5 DE-627 ger DE-627 rakwb eng 600 690 VZ 51.00 bkl 51.32 bkl Wang, Fan verfasserin aut Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling 2020transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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-β 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. 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-β 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. PRR signaling Elsevier Genotype Elsevier Interferon Elsevier HBV Elsevier HBx Elsevier Shen, Fang oth Wang, Yang oth Li, Ze oth Chen, Jieliang oth Yuan, Zhenghong oth Enthalten in Elsevier Xie, Bingyang ELSEVIER Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions 2022 San Diego, Calif. [u.a.] (DE-627)ELV008536686 volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 https://doi.org/10.1016/j.virol.2019.10.009 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.00 Werkstoffkunde: Allgemeines VZ 51.32 Werkstoffmechanik VZ AR 539 2020 2 0102 92-103 12 |
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10.1016/j.virol.2019.10.009 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001292.pica (DE-627)ELV048555088 (ELSEVIER)S0042-6822(19)30299-5 DE-627 ger DE-627 rakwb eng 600 690 VZ 51.00 bkl 51.32 bkl Wang, Fan verfasserin aut Residues Asn118 and Glu119 of hepatitis B virus X protein are critical for HBx-mediated inhibition of RIG-I-MAVS signaling 2020transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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-β 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. 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-β 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. PRR signaling Elsevier Genotype Elsevier Interferon Elsevier HBV Elsevier HBx Elsevier Shen, Fang oth Wang, Yang oth Li, Ze oth Chen, Jieliang oth Yuan, Zhenghong oth Enthalten in Elsevier Xie, Bingyang ELSEVIER Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions 2022 San Diego, Calif. [u.a.] (DE-627)ELV008536686 volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 https://doi.org/10.1016/j.virol.2019.10.009 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.00 Werkstoffkunde: Allgemeines VZ 51.32 Werkstoffmechanik VZ AR 539 2020 2 0102 92-103 12 |
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Enthalten in Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions San Diego, Calif. [u.a.] volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 |
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Enthalten in Resistive switching in 2D bismuth oxyhalide nanosheets for nonvolatile memory and emulation of leaky integrate-and-fire functions San Diego, Calif. [u.a.] volume:539 year:2020 day:2 month:01 pages:92-103 extent:12 |
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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 |
| abstract |
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-β 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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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-β 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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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-β 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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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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