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ifnar1  (Sino Biological)


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    Structured Review

    Sino Biological ifnar1
    Ifnar1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+anti+ifnar1/IFNAR1+Antibody%2C+Rabbit+MAb/us12274725-562-91-92
    Average 93 stars, based on 6 article reviews
    ifnar1 - by Bioz Stars, 2026-09
    93/100 stars

    Images

    Related Articles

    Expressing:

    Article Title: Antiviral Functions of Type I and Type III Interferons in the Olfactory Epithelium.
    Article Snippet: OE and OB were cryoprotected in 30% sucrose, embedded in an optimal cutting temperature (OCT) compound, and sectioned at a thickness of 14 µm. .. The antibodies used were: chicken anti-OMP (custom, 1:1000), goat anti-GFP (Rockland (Baltimore, MD, USA), 2.2 µg/mL), rabbit anti-IFNAR1 (Sino Biological (Beijing, China), 1:20), goat anti-IFNLR1 (Novus Biologicals (Centennial, CO, USA), 10 µg/mL), and rabbit anti-pSTAT1 (Abcam, 3.0 µg/mL). .. The images were captured using an Olympus FV3000 confocal microscope.

    Article Title: Antiviral Functions of Type I and Type III Interferons in the Olfactory Epithelium
    Article Snippet: OE and OB were cryoprotected in 30% sucrose, embedded in an optimal cutting temperature (OCT) compound, and sectioned at a thickness of 14 μm. .. The antibodies used were: chicken anti-OMP (custom, 1:1000), goat anti-GFP (Rockland (Baltimore, MD, USA), 2.2 µg/mL), rabbit anti-IFNAR1 (Sino Biological (Beijing, China), 1:20), goat anti-IFNLR1 (Novus Biologicals (Centennial, CO, USA), 10 μg/mL), and rabbit anti-pSTAT1 (Abcam, 3.0 µg/mL). .. The images were captured using an Olympus FV3000 confocal microscope.

    Article Title: Antiviral functions of type I and type III interferons in the olfactory epithelium
    Article Snippet: and OB were cryoprotected in 30% sucrose, embedded in optimal cutting temperature (OCT) compound and sectioned at a thickness of 14 µm. .. Antibodies used are: Chicken anti-OMP (custom, 1:1000), Goat anti-GFP (Rockland, 1:500), Rabbit anti-IFNAR1 (Sino Biological, 1:20), Goat anti-IFNLR1 (Novagus, 1:100), Rabbit anti-pSTAT1 (Abcam, 1:100). .. Images were captured using Olympus FV1000 and FV3000 Confocal.

    Quantitative RT-PCR:

    Article Title: Antiviral Functions of Type I and Type III Interferons in the Olfactory Epithelium.
    Article Snippet: OE and OB were cryoprotected in 30% sucrose, embedded in an optimal cutting temperature (OCT) compound, and sectioned at a thickness of 14 µm. .. The antibodies used were: chicken anti-OMP (custom, 1:1000), goat anti-GFP (Rockland (Baltimore, MD, USA), 2.2 µg/mL), rabbit anti-IFNAR1 (Sino Biological (Beijing, China), 1:20), goat anti-IFNLR1 (Novus Biologicals (Centennial, CO, USA), 10 µg/mL), and rabbit anti-pSTAT1 (Abcam, 3.0 µg/mL). .. The images were captured using an Olympus FV3000 confocal microscope.

    Article Title: Antiviral Functions of Type I and Type III Interferons in the Olfactory Epithelium
    Article Snippet: OE and OB were cryoprotected in 30% sucrose, embedded in an optimal cutting temperature (OCT) compound, and sectioned at a thickness of 14 μm. .. The antibodies used were: chicken anti-OMP (custom, 1:1000), goat anti-GFP (Rockland (Baltimore, MD, USA), 2.2 µg/mL), rabbit anti-IFNAR1 (Sino Biological (Beijing, China), 1:20), goat anti-IFNLR1 (Novus Biologicals (Centennial, CO, USA), 10 μg/mL), and rabbit anti-pSTAT1 (Abcam, 3.0 µg/mL). .. The images were captured using an Olympus FV3000 confocal microscope.

    Article Title: Antiviral functions of type I and type III interferons in the olfactory epithelium
    Article Snippet: and OB were cryoprotected in 30% sucrose, embedded in optimal cutting temperature (OCT) compound and sectioned at a thickness of 14 µm. .. Antibodies used are: Chicken anti-OMP (custom, 1:1000), Goat anti-GFP (Rockland, 1:500), Rabbit anti-IFNAR1 (Sino Biological, 1:20), Goat anti-IFNLR1 (Novagus, 1:100), Rabbit anti-pSTAT1 (Abcam, 1:100). .. Images were captured using Olympus FV1000 and FV3000 Confocal.

    Immunostaining:

    Article Title: Antiviral Functions of Type I and Type III Interferons in the Olfactory Epithelium.
    Article Snippet: OE and OB were cryoprotected in 30% sucrose, embedded in an optimal cutting temperature (OCT) compound, and sectioned at a thickness of 14 µm. .. The antibodies used were: chicken anti-OMP (custom, 1:1000), goat anti-GFP (Rockland (Baltimore, MD, USA), 2.2 µg/mL), rabbit anti-IFNAR1 (Sino Biological (Beijing, China), 1:20), goat anti-IFNLR1 (Novus Biologicals (Centennial, CO, USA), 10 µg/mL), and rabbit anti-pSTAT1 (Abcam, 3.0 µg/mL). .. The images were captured using an Olympus FV3000 confocal microscope.

    Article Title: Antiviral Functions of Type I and Type III Interferons in the Olfactory Epithelium
    Article Snippet: OE and OB were cryoprotected in 30% sucrose, embedded in an optimal cutting temperature (OCT) compound, and sectioned at a thickness of 14 μm. .. The antibodies used were: chicken anti-OMP (custom, 1:1000), goat anti-GFP (Rockland (Baltimore, MD, USA), 2.2 µg/mL), rabbit anti-IFNAR1 (Sino Biological (Beijing, China), 1:20), goat anti-IFNLR1 (Novus Biologicals (Centennial, CO, USA), 10 μg/mL), and rabbit anti-pSTAT1 (Abcam, 3.0 µg/mL). .. The images were captured using an Olympus FV3000 confocal microscope.

    Article Title: Antiviral functions of type I and type III interferons in the olfactory epithelium
    Article Snippet: and OB were cryoprotected in 30% sucrose, embedded in optimal cutting temperature (OCT) compound and sectioned at a thickness of 14 µm. .. Antibodies used are: Chicken anti-OMP (custom, 1:1000), Goat anti-GFP (Rockland, 1:500), Rabbit anti-IFNAR1 (Sino Biological, 1:20), Goat anti-IFNLR1 (Novagus, 1:100), Rabbit anti-pSTAT1 (Abcam, 1:100). .. Images were captured using Olympus FV1000 and FV3000 Confocal.



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    (A) A diagram showing that IFN-I-induced <t>IFNAR1</t> degradation mediated by PARP11 and β-TrCP leads to a shift in IFN-I antiviral efficiency from “Efficiency Display” to “Efficiency Loss”. (B and C) Flow cytometry analysis of cytoplasmic membrane IFNAR1 levels (B) or RT-qPCR analysis of Ifit1 mRNA (C) in PBMCs from chronic hepatitis-B (CHB) patients before and 6 h after Pegylated (Peg)-IFN treatment (180 μg each person). B: before treatment; A: after treatment. (D) IFNAR1 (wild-type,WT; S535A mutants) constructs were stably transfected in Ifnar1 -/- HEK293T cells. RT-qPCR was used to analyze Ifit1 mRNA in these cells treated with IFNα (1,000 IU/ml) for indicated times. (E) ChIP-qPCR analysis of the binding of cellular IRF9 proteins to the ISRE promoters of the representative ISG ( Ifit1 ) gene in HEK293T cells treated with IFNα (1,000 IU/ml) for indicated times. (F) Western blot analysis of IRF9 in HT1080 cells treated with IFNα (1,000 IU/ml) for indicated times. (G) ChIP-qPCR analysis of the binding of IRF9 proteins to the ISRE of Ifit1 in HEK293T cells treated with PTP inhibitor I (10 μM) and (or) IFNα (1,000 IU/ml) as indicated. (H) RT-qPCR analysis of Ifit1 mRNA in HEK293T cells treated with PTP inhibitor I (10 μM) and (or) IFNα (1,000 IU/ml) as indicated. NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). Data are shown as means ± SD of three biological replicates (B-E, G, H), or are representative of three independent experiments (F).
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    Image Search Results


    (A) HEK293T cells were cotransfected with the plasmids expressing HA-IFNAR1 or HA-IFNAR2, and Flag-p22 or the empty vector pRK (Vec) and then lysed and analyzed using co-IP with the anti-Flag MAb, followed by western blotting analysis using the indicated antibodies. (B) PAMs were infected with ASFV-WT or ASFV-ΔP (MOI = 3). The cells were lysed for co-IP using the anti-p22 MAb at 24 hpi, followed by western blotting analysis using the indicated antibodies. (C) IBRS-2 cells were cotransfected with the plasmids expressing Myc-IFNAR1 and Flag-p22 and then fixed with 4% paraformaldehyde. IFNAR1 and p22 were immunoblotted using anti-Myc and anti-Flag antibodies, respectively. The nuclei were stained with DAPI and subjected to confocal microscopy. The colocalization of p22 and IFNAR1 was analyzed using the Coloc2 tool in the ImageJ software (National Institutes of Health, Bethesda, MD, USA), and they are represented as Pearson’s R value (R). Scale bar = 10 μm. (D) HEK293T cells were cotransfected with the HA- β -actin-, Flag-p22-, and HA-IFNAR1- or HA-IFNAR2-expressing plasmid, followed by western blotting analysis using the indicated antibodies at 24 hpt. (E) HEK293T cells were transfected with different amounts of the Flag-p22-expressing plasmid, followed by western blotting analysis using the indicated antibodies at 24 hpt. (F) PAMs were infected with ASFV-WT or ASFV-ΔKP177R (MOI = 3). At 18 and 24 hpi, the cells were lysed to perform western blotting analysis using the indicated antibodies.

    Journal: PLOS Pathogens

    Article Title: The African swine fever virus p22 inhibits the JAK-STAT signaling pathway by promoting the TAX1BP1-mediated degradation of the type I interferon receptor

    doi: 10.1371/journal.ppat.1013319

    Figure Lengend Snippet: (A) HEK293T cells were cotransfected with the plasmids expressing HA-IFNAR1 or HA-IFNAR2, and Flag-p22 or the empty vector pRK (Vec) and then lysed and analyzed using co-IP with the anti-Flag MAb, followed by western blotting analysis using the indicated antibodies. (B) PAMs were infected with ASFV-WT or ASFV-ΔP (MOI = 3). The cells were lysed for co-IP using the anti-p22 MAb at 24 hpi, followed by western blotting analysis using the indicated antibodies. (C) IBRS-2 cells were cotransfected with the plasmids expressing Myc-IFNAR1 and Flag-p22 and then fixed with 4% paraformaldehyde. IFNAR1 and p22 were immunoblotted using anti-Myc and anti-Flag antibodies, respectively. The nuclei were stained with DAPI and subjected to confocal microscopy. The colocalization of p22 and IFNAR1 was analyzed using the Coloc2 tool in the ImageJ software (National Institutes of Health, Bethesda, MD, USA), and they are represented as Pearson’s R value (R). Scale bar = 10 μm. (D) HEK293T cells were cotransfected with the HA- β -actin-, Flag-p22-, and HA-IFNAR1- or HA-IFNAR2-expressing plasmid, followed by western blotting analysis using the indicated antibodies at 24 hpt. (E) HEK293T cells were transfected with different amounts of the Flag-p22-expressing plasmid, followed by western blotting analysis using the indicated antibodies at 24 hpt. (F) PAMs were infected with ASFV-WT or ASFV-ΔKP177R (MOI = 3). At 18 and 24 hpi, the cells were lysed to perform western blotting analysis using the indicated antibodies.

    Article Snippet: Rabbit anti-IFNAR1 polyclonal antibodies (PAb) (a1715), rabbit anti- β -actin MAb (AC026), rabbit anti-LC3B MAb (A19665), rabbit anti-LAMP1 pAb (A16894, lysosomes), rabbit anti-TOM20 pAb (A6774, mitochondria), rabbit anti-PSMA1 pAb (A3460, proteasomes), and rabbit anti-GM130 pAb (A11408, Golgi apparatus) were obtained from ABclonal (Wuhan, China).

    Techniques: Expressing, Plasmid Preparation, Co-Immunoprecipitation Assay, Western Blot, Infection, Staining, Confocal Microscopy, Software, Transfection

    (A) HEK293T cells were cotransfected with the plasmids expressing HA-IFNAR1, HA- β -actin, and Flag-p22 or pRK (Vec). Then, the cells were treated with DMSO, MG132, or CQ at 24 hpt, followed by western blotting analysis using the indicated antibodies. (B) HEK293T cells were transfected with the plasmids pFlag-KP177R or pRK (Vec). Then, the cells were treated with DMSO, SBI, 3-MA, or CQ at 24 hpt, followed by western blotting analysis using the indicated antibodies. (C) HEK293T cells were transfected with the different amounts of the Flag-p22-expressing plasmid with pHA-IFNAR1 and pHA- β -actin, followed by western blotting analysis using the indicated antibodies at 24 hpt. (D) IBRS-2 cells were cotransfected with the plasmids expressing EGFP-LC3, Myc-IFNAR1, and Flag-p22, and then fixed with 4% paraformaldehyde. IFNAR1 and p22 were immunoblotted using anti-Myc and -Flag antibodies, respectively. The nuclei were stained with DAPI and analyzed using confocal microscopy. The colocalization of LC3 and IFNAR1 was analyzed using the Coloc2 tool in ImageJ and are shown as Pearson’s R value (R). Scale bar = 10 μm. (E) PAMs were infected with ASFV-WT or ASFV-ΔKP177R for the indicated duration (MOI = 3), followed by western blotting analysis using the indicated antibodies. (F) The ATG5-knockout HeLa cells or the WT HeLa cells were transfected with the different amounts of the Flag-p22-expressing plasmid with pHA-IFNAR1 and pHA- β -actin, followed by western blotting analysis using the indicated antibodies at 24 hpt. The densitometric analysis of the protein expression levels was performed using the ImageJ software.

    Journal: PLOS Pathogens

    Article Title: The African swine fever virus p22 inhibits the JAK-STAT signaling pathway by promoting the TAX1BP1-mediated degradation of the type I interferon receptor

    doi: 10.1371/journal.ppat.1013319

    Figure Lengend Snippet: (A) HEK293T cells were cotransfected with the plasmids expressing HA-IFNAR1, HA- β -actin, and Flag-p22 or pRK (Vec). Then, the cells were treated with DMSO, MG132, or CQ at 24 hpt, followed by western blotting analysis using the indicated antibodies. (B) HEK293T cells were transfected with the plasmids pFlag-KP177R or pRK (Vec). Then, the cells were treated with DMSO, SBI, 3-MA, or CQ at 24 hpt, followed by western blotting analysis using the indicated antibodies. (C) HEK293T cells were transfected with the different amounts of the Flag-p22-expressing plasmid with pHA-IFNAR1 and pHA- β -actin, followed by western blotting analysis using the indicated antibodies at 24 hpt. (D) IBRS-2 cells were cotransfected with the plasmids expressing EGFP-LC3, Myc-IFNAR1, and Flag-p22, and then fixed with 4% paraformaldehyde. IFNAR1 and p22 were immunoblotted using anti-Myc and -Flag antibodies, respectively. The nuclei were stained with DAPI and analyzed using confocal microscopy. The colocalization of LC3 and IFNAR1 was analyzed using the Coloc2 tool in ImageJ and are shown as Pearson’s R value (R). Scale bar = 10 μm. (E) PAMs were infected with ASFV-WT or ASFV-ΔKP177R for the indicated duration (MOI = 3), followed by western blotting analysis using the indicated antibodies. (F) The ATG5-knockout HeLa cells or the WT HeLa cells were transfected with the different amounts of the Flag-p22-expressing plasmid with pHA-IFNAR1 and pHA- β -actin, followed by western blotting analysis using the indicated antibodies at 24 hpt. The densitometric analysis of the protein expression levels was performed using the ImageJ software.

    Article Snippet: Rabbit anti-IFNAR1 polyclonal antibodies (PAb) (a1715), rabbit anti- β -actin MAb (AC026), rabbit anti-LC3B MAb (A19665), rabbit anti-LAMP1 pAb (A16894, lysosomes), rabbit anti-TOM20 pAb (A6774, mitochondria), rabbit anti-PSMA1 pAb (A3460, proteasomes), and rabbit anti-GM130 pAb (A11408, Golgi apparatus) were obtained from ABclonal (Wuhan, China).

    Techniques: Expressing, Western Blot, Transfection, Plasmid Preparation, Staining, Confocal Microscopy, Infection, Knock-Out, Software

    (A) HEK293T cells were cotransfected with the plasmids expressing the Myc-IFNAR1, HA- β -actin, HA-TAX1BP1, and Flag-p22, followed by western blotting analysis using the indicated antibodies. (B) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA- β -actin, and HA-TAX1BP1. Then, the cells were treated with DMSO, SBI, 3-MA, or CQ at 24 hpt, followed by western blotting analysis using the indicated antibodies. (C) HEK293T cells were transfected with different amounts of the TAX1BP1- or TAX1BP1-ΔUBD-expressing plasmids with pMyc-IFNAR1 and pHA- β -actin, followed by western blotting analysis using the indicated antibodies at 24 hpt. (D) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA- β -actin, Flag-p22, and HA-TAX1BP1 or HA-TAX1BP1-ΔUBD, followed by western blotting analysis using the indicated antibodies. (E) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA-Ub, and Flag-p22, and then lysed for co-IP using anti-Myc MAb, followed by western blotting analysis using the indicated antibodies. (F) HEK293T cells were transfected with different amounts of the p22-expressing plasmid with pMyc-IFNAR1 and pHA-TAX1BP1, and then lysed for co-IP using anti-HA MAb at 24 hpt, followed by western blotting analysis using the indicated antibodies.

    Journal: PLOS Pathogens

    Article Title: The African swine fever virus p22 inhibits the JAK-STAT signaling pathway by promoting the TAX1BP1-mediated degradation of the type I interferon receptor

    doi: 10.1371/journal.ppat.1013319

    Figure Lengend Snippet: (A) HEK293T cells were cotransfected with the plasmids expressing the Myc-IFNAR1, HA- β -actin, HA-TAX1BP1, and Flag-p22, followed by western blotting analysis using the indicated antibodies. (B) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA- β -actin, and HA-TAX1BP1. Then, the cells were treated with DMSO, SBI, 3-MA, or CQ at 24 hpt, followed by western blotting analysis using the indicated antibodies. (C) HEK293T cells were transfected with different amounts of the TAX1BP1- or TAX1BP1-ΔUBD-expressing plasmids with pMyc-IFNAR1 and pHA- β -actin, followed by western blotting analysis using the indicated antibodies at 24 hpt. (D) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA- β -actin, Flag-p22, and HA-TAX1BP1 or HA-TAX1BP1-ΔUBD, followed by western blotting analysis using the indicated antibodies. (E) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA-Ub, and Flag-p22, and then lysed for co-IP using anti-Myc MAb, followed by western blotting analysis using the indicated antibodies. (F) HEK293T cells were transfected with different amounts of the p22-expressing plasmid with pMyc-IFNAR1 and pHA-TAX1BP1, and then lysed for co-IP using anti-HA MAb at 24 hpt, followed by western blotting analysis using the indicated antibodies.

    Article Snippet: Rabbit anti-IFNAR1 polyclonal antibodies (PAb) (a1715), rabbit anti- β -actin MAb (AC026), rabbit anti-LC3B MAb (A19665), rabbit anti-LAMP1 pAb (A16894, lysosomes), rabbit anti-TOM20 pAb (A6774, mitochondria), rabbit anti-PSMA1 pAb (A3460, proteasomes), and rabbit anti-GM130 pAb (A11408, Golgi apparatus) were obtained from ABclonal (Wuhan, China).

    Techniques: Expressing, Western Blot, Transfection, Co-Immunoprecipitation Assay, Plasmid Preparation

    (A) Schematic illustration of the domain structures of p22, IFNAR1, and TAX1BP1, and the construction strategy of their truncation mutants. (B) HEK293T cells were cotransfected with plasmids pSTAT1-Fluc and pFlag-KP177R or plasmids expressing the truncated versions at 24 hpt and luciferase assay was conducted. (C) IBRS-2 cells were transfected with pFlag-KP177R or pFlag-KP177R-ΔECD, and treated with 200 ng/mL IFN- β , followed by total RNA extraction and the subsequent RT-qPCR analysis. (D) IBRS-2 cells were transfected with pFlag-KP177R or pFlag-KP177R-ΔECD and treated with 200 ng/mL IFN- β for the indicated hours and subjected to western blotting analysis using the indicated antibodies. (E) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA- β -actin, and Flag-p22 or the truncated versions of p22 and subjected to western blotting analysis using the indicated antibodies. The densitometric analysis of the protein expression levels was performed using the ImageJ software.

    Journal: PLOS Pathogens

    Article Title: The African swine fever virus p22 inhibits the JAK-STAT signaling pathway by promoting the TAX1BP1-mediated degradation of the type I interferon receptor

    doi: 10.1371/journal.ppat.1013319

    Figure Lengend Snippet: (A) Schematic illustration of the domain structures of p22, IFNAR1, and TAX1BP1, and the construction strategy of their truncation mutants. (B) HEK293T cells were cotransfected with plasmids pSTAT1-Fluc and pFlag-KP177R or plasmids expressing the truncated versions at 24 hpt and luciferase assay was conducted. (C) IBRS-2 cells were transfected with pFlag-KP177R or pFlag-KP177R-ΔECD, and treated with 200 ng/mL IFN- β , followed by total RNA extraction and the subsequent RT-qPCR analysis. (D) IBRS-2 cells were transfected with pFlag-KP177R or pFlag-KP177R-ΔECD and treated with 200 ng/mL IFN- β for the indicated hours and subjected to western blotting analysis using the indicated antibodies. (E) HEK293T cells were cotransfected with the plasmids expressing Myc-IFNAR1, HA- β -actin, and Flag-p22 or the truncated versions of p22 and subjected to western blotting analysis using the indicated antibodies. The densitometric analysis of the protein expression levels was performed using the ImageJ software.

    Article Snippet: Rabbit anti-IFNAR1 polyclonal antibodies (PAb) (a1715), rabbit anti- β -actin MAb (AC026), rabbit anti-LC3B MAb (A19665), rabbit anti-LAMP1 pAb (A16894, lysosomes), rabbit anti-TOM20 pAb (A6774, mitochondria), rabbit anti-PSMA1 pAb (A3460, proteasomes), and rabbit anti-GM130 pAb (A11408, Golgi apparatus) were obtained from ABclonal (Wuhan, China).

    Techniques: Expressing, Luciferase, Transfection, RNA Extraction, Quantitative RT-PCR, Western Blot, Software

    The selective autophagy receptor TAX1BP1 interacts with and degrades IFNAR1 via autophagy. The transmembrane region of the ASFV p22 enhances the binding of TAX1BP1 to IFNAR1, thereby promoting the degradation of IFNAR1. This leads to a decrease in the transcriptional levels of antiviral genes, ultimately inhibiting the host IFN responses. Created with BioRender.com.

    Journal: PLOS Pathogens

    Article Title: The African swine fever virus p22 inhibits the JAK-STAT signaling pathway by promoting the TAX1BP1-mediated degradation of the type I interferon receptor

    doi: 10.1371/journal.ppat.1013319

    Figure Lengend Snippet: The selective autophagy receptor TAX1BP1 interacts with and degrades IFNAR1 via autophagy. The transmembrane region of the ASFV p22 enhances the binding of TAX1BP1 to IFNAR1, thereby promoting the degradation of IFNAR1. This leads to a decrease in the transcriptional levels of antiviral genes, ultimately inhibiting the host IFN responses. Created with BioRender.com.

    Article Snippet: Rabbit anti-IFNAR1 polyclonal antibodies (PAb) (a1715), rabbit anti- β -actin MAb (AC026), rabbit anti-LC3B MAb (A19665), rabbit anti-LAMP1 pAb (A16894, lysosomes), rabbit anti-TOM20 pAb (A6774, mitochondria), rabbit anti-PSMA1 pAb (A3460, proteasomes), and rabbit anti-GM130 pAb (A11408, Golgi apparatus) were obtained from ABclonal (Wuhan, China).

    Techniques: Binding Assay

    Main immunohistochemical findings in the study groups

    Journal: Respiratory Research

    Article Title: Expression of human Interferon Regulatory Factor 3 (IRF-3) in alveolar macrophages relates to clinical and functional traits in COPD.

    doi: 10.1186/s12931-024-02952-6

    Figure Lengend Snippet: Main immunohistochemical findings in the study groups

    Article Snippet: Briefly, formalin-fixed paraffin embedded lung sections were treated for 60 min with primary antibodies rabbit anti-human IFNAR1 and IFNAR2 (GTX54322 and GTX54289 from GeneTex, Irvine CA, USA), MDA-5 (700360 from Invitrogen, Carlsbad CA, USA) and murine anti-human IRF-3 (sc-376455 from Santa Cruz Dallas TX, USA).

    Techniques: Immunohistochemical staining

    Additional immunohistochemical findings (intensity score in alveolar walls and bronchiolar epithelium)

    Journal: Respiratory Research

    Article Title: Expression of human Interferon Regulatory Factor 3 (IRF-3) in alveolar macrophages relates to clinical and functional traits in COPD.

    doi: 10.1186/s12931-024-02952-6

    Figure Lengend Snippet: Additional immunohistochemical findings (intensity score in alveolar walls and bronchiolar epithelium)

    Article Snippet: Briefly, formalin-fixed paraffin embedded lung sections were treated for 60 min with primary antibodies rabbit anti-human IFNAR1 and IFNAR2 (GTX54322 and GTX54289 from GeneTex, Irvine CA, USA), MDA-5 (700360 from Invitrogen, Carlsbad CA, USA) and murine anti-human IRF-3 (sc-376455 from Santa Cruz Dallas TX, USA).

    Techniques: Immunohistochemical staining

    Main immunohistochemical findings in the study groups

    Journal: Respiratory Research

    Article Title: Expression of human Interferon Regulatory Factor 3 (IRF-3) in alveolar macrophages relates to clinical and functional traits in COPD.

    doi: 10.1186/s12931-024-02952-6

    Figure Lengend Snippet: Main immunohistochemical findings in the study groups

    Article Snippet: Briefly, formalin-fixed paraffin embedded lung sections were treated for 60 min with primary antibodies rabbit anti-human IFNAR1 and IFNAR2 (GTX54322 and GTX54289 from GeneTex, Irvine CA, USA), MDA-5 (700360 from Invitrogen, Carlsbad CA, USA) and murine anti-human IRF-3 (sc-376455 from Santa Cruz Dallas TX, USA).

    Techniques: Immunohistochemical staining

    Additional immunohistochemical findings (intensity score in alveolar walls and bronchiolar epithelium)

    Journal: Respiratory Research

    Article Title: Expression of human Interferon Regulatory Factor 3 (IRF-3) in alveolar macrophages relates to clinical and functional traits in COPD.

    doi: 10.1186/s12931-024-02952-6

    Figure Lengend Snippet: Additional immunohistochemical findings (intensity score in alveolar walls and bronchiolar epithelium)

    Article Snippet: Briefly, formalin-fixed paraffin embedded lung sections were treated for 60 min with primary antibodies rabbit anti-human IFNAR1 and IFNAR2 (GTX54322 and GTX54289 from GeneTex, Irvine CA, USA), MDA-5 (700360 from Invitrogen, Carlsbad CA, USA) and murine anti-human IRF-3 (sc-376455 from Santa Cruz Dallas TX, USA).

    Techniques: Immunohistochemical staining

    (A) A diagram showing that IFN-I-induced IFNAR1 degradation mediated by PARP11 and β-TrCP leads to a shift in IFN-I antiviral efficiency from “Efficiency Display” to “Efficiency Loss”. (B and C) Flow cytometry analysis of cytoplasmic membrane IFNAR1 levels (B) or RT-qPCR analysis of Ifit1 mRNA (C) in PBMCs from chronic hepatitis-B (CHB) patients before and 6 h after Pegylated (Peg)-IFN treatment (180 μg each person). B: before treatment; A: after treatment. (D) IFNAR1 (wild-type,WT; S535A mutants) constructs were stably transfected in Ifnar1 -/- HEK293T cells. RT-qPCR was used to analyze Ifit1 mRNA in these cells treated with IFNα (1,000 IU/ml) for indicated times. (E) ChIP-qPCR analysis of the binding of cellular IRF9 proteins to the ISRE promoters of the representative ISG ( Ifit1 ) gene in HEK293T cells treated with IFNα (1,000 IU/ml) for indicated times. (F) Western blot analysis of IRF9 in HT1080 cells treated with IFNα (1,000 IU/ml) for indicated times. (G) ChIP-qPCR analysis of the binding of IRF9 proteins to the ISRE of Ifit1 in HEK293T cells treated with PTP inhibitor I (10 μM) and (or) IFNα (1,000 IU/ml) as indicated. (H) RT-qPCR analysis of Ifit1 mRNA in HEK293T cells treated with PTP inhibitor I (10 μM) and (or) IFNα (1,000 IU/ml) as indicated. NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). Data are shown as means ± SD of three biological replicates (B-E, G, H), or are representative of three independent experiments (F).

    Journal: medRxiv

    Article Title: Aspirin improves both reactivity and durability of type-I interferon signaling to achieve functional cure of chronic hepatitis B

    doi: 10.1101/2024.06.14.24308555

    Figure Lengend Snippet: (A) A diagram showing that IFN-I-induced IFNAR1 degradation mediated by PARP11 and β-TrCP leads to a shift in IFN-I antiviral efficiency from “Efficiency Display” to “Efficiency Loss”. (B and C) Flow cytometry analysis of cytoplasmic membrane IFNAR1 levels (B) or RT-qPCR analysis of Ifit1 mRNA (C) in PBMCs from chronic hepatitis-B (CHB) patients before and 6 h after Pegylated (Peg)-IFN treatment (180 μg each person). B: before treatment; A: after treatment. (D) IFNAR1 (wild-type,WT; S535A mutants) constructs were stably transfected in Ifnar1 -/- HEK293T cells. RT-qPCR was used to analyze Ifit1 mRNA in these cells treated with IFNα (1,000 IU/ml) for indicated times. (E) ChIP-qPCR analysis of the binding of cellular IRF9 proteins to the ISRE promoters of the representative ISG ( Ifit1 ) gene in HEK293T cells treated with IFNα (1,000 IU/ml) for indicated times. (F) Western blot analysis of IRF9 in HT1080 cells treated with IFNα (1,000 IU/ml) for indicated times. (G) ChIP-qPCR analysis of the binding of IRF9 proteins to the ISRE of Ifit1 in HEK293T cells treated with PTP inhibitor I (10 μM) and (or) IFNα (1,000 IU/ml) as indicated. (H) RT-qPCR analysis of Ifit1 mRNA in HEK293T cells treated with PTP inhibitor I (10 μM) and (or) IFNα (1,000 IU/ml) as indicated. NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). Data are shown as means ± SD of three biological replicates (B-E, G, H), or are representative of three independent experiments (F).

    Article Snippet: The antibodies in this study are listed here: Anti-IRF9 (Santa Cruz, Cat #sc-365893), Anti-pan-pY (Cell Signalling Technology, Cat #8954), Anti-Flag (Sigma, Cat #F7425), Anti-Tubulin (Proteintech, Cat #66031-1-Ig), Anti-GFP (Santa Cruz, Cat #sc-9996), Anti-p-STAT1(Y701) (Cell Signalling Technology, Cat #9167), Anti-STAT1 (Cell Signalling Technology, Cat #9176), Anti-PTP1B (Proteintech, Cat #11334-1-AP), Anti-β-Actin (Proteintech, Cat #66009), Anti-Myc (Abmart, Cat #M20002), Anti-HA (Abcam, Cat #ab9110), Anti-IFNAR1-PE (Invitrogen, Cat #MA5-23630), Anti-IFNAR1 (Sino Biological, Cat #13222-T20), Anti-β-Trcp (Cell Signalling Technology, Cat #11984),Anti-pan-AcK (Santa Cruz, Cat #sc-32268), Anti-Viperin (Abcam, Cat #107359), Anti-IFIT1 (Santa Cruz, Cat #sc-134948), Anti-HA (H1N1) (Sino Biological, Cat #11684-T56), Anti-p-STAT1 (S727) (Cell Signalling Technology, Cat #8826), Anti-p-STAT2 (Y690) (Cell Signalling Technology, Cat #88410), Anti-VSV-G (Abcam, Cat #ab1874), Anti-PKR (Cell Signalling Technology, Cat #3072S) and Anti-GAPDH (Goodhere Biological Technology, Cat #AB-M-M001).

    Techniques: Flow Cytometry, Membrane, Quantitative RT-PCR, Construct, Stable Transfection, Transfection, Binding Assay, Western Blot, Two Tailed Test

    (A) Western blot analysis of pY701-STAT1 in HEK293T cells treated with Aspirin (100 μg/ml) and (or) IFNα (1,000 IU/ml) as indicated. (B) Western blot analysis of Flag-IFNAR1 or HA-IFNAR2 in HEK293T cells transfected with either Flag-IFNAR1 (left) or HA-IFNAR2 (right) and then treated with Aspirin (100 μg/ml) as indicated. (C) RT-qPCR analysis of Ifnar1 mRNA in HEK293T cells treated with Aspirin (100 μg/ml) for indicated times. (D and E) Western blot analysis of IFNAR1 in HEK293T cells pre-treated with Aspirin (100 μg/ml) (D) or Salicylate (100 μg/ml) (E) for 2 h and then treated with IFNα (2,000 IU/ml) for 60, 90 and 120 min. (F) HEK293T cells transfected with HA-tagged ubiquitin (Ub) were pre-treated with Aspirin (100 μg/ml, 2 h) and then treated with IFNα (2,000 IU/ml) for 2 h. IP-IB was performed to analyze IFNAR1 ubiquitination in cells. (G and H) Western blot analysis of β-TrCP in HEK293T cells treated with Aspirin for 6 h as indicated (G) or Aspirin (100 μg/ml) for indicated times (H). (I) RT-qPCR analysis of β-TrCP mRNA in HEK293T cells treated with Aspirin (100 μg/ml) for indicated times. (J) RT-qPCR analysis of Parp11 mRNA in HEK293T cells treated with Aspirin (100 μg/ml) (left) or Salicylate (100 μg/ml) (right) for indicated times. (K) RT-qPCR analysis of Ifit1 mRNA in HEK293T cells pre-treated with Aspirin (100 μg/ml) for 2 h and then treated with IFNα (1,000 IU/ml) as indicated. NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). Data are shown as means ± SD of at least three biological replicates (C, I-K), or are representative of three independent experiments (A, B, D-H).

    Journal: medRxiv

    Article Title: Aspirin improves both reactivity and durability of type-I interferon signaling to achieve functional cure of chronic hepatitis B

    doi: 10.1101/2024.06.14.24308555

    Figure Lengend Snippet: (A) Western blot analysis of pY701-STAT1 in HEK293T cells treated with Aspirin (100 μg/ml) and (or) IFNα (1,000 IU/ml) as indicated. (B) Western blot analysis of Flag-IFNAR1 or HA-IFNAR2 in HEK293T cells transfected with either Flag-IFNAR1 (left) or HA-IFNAR2 (right) and then treated with Aspirin (100 μg/ml) as indicated. (C) RT-qPCR analysis of Ifnar1 mRNA in HEK293T cells treated with Aspirin (100 μg/ml) for indicated times. (D and E) Western blot analysis of IFNAR1 in HEK293T cells pre-treated with Aspirin (100 μg/ml) (D) or Salicylate (100 μg/ml) (E) for 2 h and then treated with IFNα (2,000 IU/ml) for 60, 90 and 120 min. (F) HEK293T cells transfected with HA-tagged ubiquitin (Ub) were pre-treated with Aspirin (100 μg/ml, 2 h) and then treated with IFNα (2,000 IU/ml) for 2 h. IP-IB was performed to analyze IFNAR1 ubiquitination in cells. (G and H) Western blot analysis of β-TrCP in HEK293T cells treated with Aspirin for 6 h as indicated (G) or Aspirin (100 μg/ml) for indicated times (H). (I) RT-qPCR analysis of β-TrCP mRNA in HEK293T cells treated with Aspirin (100 μg/ml) for indicated times. (J) RT-qPCR analysis of Parp11 mRNA in HEK293T cells treated with Aspirin (100 μg/ml) (left) or Salicylate (100 μg/ml) (right) for indicated times. (K) RT-qPCR analysis of Ifit1 mRNA in HEK293T cells pre-treated with Aspirin (100 μg/ml) for 2 h and then treated with IFNα (1,000 IU/ml) as indicated. NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). Data are shown as means ± SD of at least three biological replicates (C, I-K), or are representative of three independent experiments (A, B, D-H).

    Article Snippet: The antibodies in this study are listed here: Anti-IRF9 (Santa Cruz, Cat #sc-365893), Anti-pan-pY (Cell Signalling Technology, Cat #8954), Anti-Flag (Sigma, Cat #F7425), Anti-Tubulin (Proteintech, Cat #66031-1-Ig), Anti-GFP (Santa Cruz, Cat #sc-9996), Anti-p-STAT1(Y701) (Cell Signalling Technology, Cat #9167), Anti-STAT1 (Cell Signalling Technology, Cat #9176), Anti-PTP1B (Proteintech, Cat #11334-1-AP), Anti-β-Actin (Proteintech, Cat #66009), Anti-Myc (Abmart, Cat #M20002), Anti-HA (Abcam, Cat #ab9110), Anti-IFNAR1-PE (Invitrogen, Cat #MA5-23630), Anti-IFNAR1 (Sino Biological, Cat #13222-T20), Anti-β-Trcp (Cell Signalling Technology, Cat #11984),Anti-pan-AcK (Santa Cruz, Cat #sc-32268), Anti-Viperin (Abcam, Cat #107359), Anti-IFIT1 (Santa Cruz, Cat #sc-134948), Anti-HA (H1N1) (Sino Biological, Cat #11684-T56), Anti-p-STAT1 (S727) (Cell Signalling Technology, Cat #8826), Anti-p-STAT2 (Y690) (Cell Signalling Technology, Cat #88410), Anti-VSV-G (Abcam, Cat #ab1874), Anti-PKR (Cell Signalling Technology, Cat #3072S) and Anti-GAPDH (Goodhere Biological Technology, Cat #AB-M-M001).

    Techniques: Western Blot, Transfection, Quantitative RT-PCR, Two Tailed Test

    (A) Mice (n = 5) were injected intraperitoneally ( i.p. ) with PBS or Aspirin (50 μg per gram body mouse). Two hours after injection, mice were injected with mouse IFNβ (1,000 IU/g, i.p. ) and then mouse tissues were collected for further analysis 6 h after IFNβ injection. (B) RT-qPCR analysis of Ifit1 , Isg15 and Mx1 mRNA in mouse spleen tissues from (A). (C) RT-qPCR analysis of Ifit1 mRNA in mouse heart, liver, lung and kidney tissues from (A). (D and E) Western blot analysis of pY112-IRF9 (D) and IFNAR1 (E) in the livers of mice (n=4) injected with Aspirin and IFNβ as (A). (F) CHB patients were recruited and the IA (IFN-I + Aspirin) therapy was performed. Aspirin (0.2 g, qw) was taken orally before Peg-IFN injection and then Peg-IFN (180 μg, qw) was injected subcutaneously in the abdomen. The PBMCs from CHB patients were collected for analysis before injection and 6 h after injection. B: before injection. A: 6 h after injection. (G) Flow cytometry analysis of IFNAR1 in PBMCs of CHB patients from (F). (H) Western blot analysis of pY112-IRF9 in PBMCs of CHB patients from (F). (I) RT-qPCR analysis of Ifit1 mRNA in PBMCs of CHB patients from (F). NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). All graphs show the mean ± SEM for five individual mice (B, C). Data are shown as means ± SD of three biological replicates (G, I), or are representative of three independent experiments (D, E, H).

    Journal: medRxiv

    Article Title: Aspirin improves both reactivity and durability of type-I interferon signaling to achieve functional cure of chronic hepatitis B

    doi: 10.1101/2024.06.14.24308555

    Figure Lengend Snippet: (A) Mice (n = 5) were injected intraperitoneally ( i.p. ) with PBS or Aspirin (50 μg per gram body mouse). Two hours after injection, mice were injected with mouse IFNβ (1,000 IU/g, i.p. ) and then mouse tissues were collected for further analysis 6 h after IFNβ injection. (B) RT-qPCR analysis of Ifit1 , Isg15 and Mx1 mRNA in mouse spleen tissues from (A). (C) RT-qPCR analysis of Ifit1 mRNA in mouse heart, liver, lung and kidney tissues from (A). (D and E) Western blot analysis of pY112-IRF9 (D) and IFNAR1 (E) in the livers of mice (n=4) injected with Aspirin and IFNβ as (A). (F) CHB patients were recruited and the IA (IFN-I + Aspirin) therapy was performed. Aspirin (0.2 g, qw) was taken orally before Peg-IFN injection and then Peg-IFN (180 μg, qw) was injected subcutaneously in the abdomen. The PBMCs from CHB patients were collected for analysis before injection and 6 h after injection. B: before injection. A: 6 h after injection. (G) Flow cytometry analysis of IFNAR1 in PBMCs of CHB patients from (F). (H) Western blot analysis of pY112-IRF9 in PBMCs of CHB patients from (F). (I) RT-qPCR analysis of Ifit1 mRNA in PBMCs of CHB patients from (F). NS, not significant (p > 0.05), *p < 0.05, **p < 0.01, ***p < 0.001 (two-tailed unpaired Student’s t -test). All graphs show the mean ± SEM for five individual mice (B, C). Data are shown as means ± SD of three biological replicates (G, I), or are representative of three independent experiments (D, E, H).

    Article Snippet: The antibodies in this study are listed here: Anti-IRF9 (Santa Cruz, Cat #sc-365893), Anti-pan-pY (Cell Signalling Technology, Cat #8954), Anti-Flag (Sigma, Cat #F7425), Anti-Tubulin (Proteintech, Cat #66031-1-Ig), Anti-GFP (Santa Cruz, Cat #sc-9996), Anti-p-STAT1(Y701) (Cell Signalling Technology, Cat #9167), Anti-STAT1 (Cell Signalling Technology, Cat #9176), Anti-PTP1B (Proteintech, Cat #11334-1-AP), Anti-β-Actin (Proteintech, Cat #66009), Anti-Myc (Abmart, Cat #M20002), Anti-HA (Abcam, Cat #ab9110), Anti-IFNAR1-PE (Invitrogen, Cat #MA5-23630), Anti-IFNAR1 (Sino Biological, Cat #13222-T20), Anti-β-Trcp (Cell Signalling Technology, Cat #11984),Anti-pan-AcK (Santa Cruz, Cat #sc-32268), Anti-Viperin (Abcam, Cat #107359), Anti-IFIT1 (Santa Cruz, Cat #sc-134948), Anti-HA (H1N1) (Sino Biological, Cat #11684-T56), Anti-p-STAT1 (S727) (Cell Signalling Technology, Cat #8826), Anti-p-STAT2 (Y690) (Cell Signalling Technology, Cat #88410), Anti-VSV-G (Abcam, Cat #ab1874), Anti-PKR (Cell Signalling Technology, Cat #3072S) and Anti-GAPDH (Goodhere Biological Technology, Cat #AB-M-M001).

    Techniques: Injection, Quantitative RT-PCR, Western Blot, Flow Cytometry, Two Tailed Test

    Aspirin and its metabolite Salicylate maintain IFNAR1 protein stability and IRF9 tyrosine phosphorylation, respectively, thus enhancing both the reactivity and durability of IFN-I signaling, which eventually promotes a functional cure of chronic HBV infection.

    Journal: medRxiv

    Article Title: Aspirin improves both reactivity and durability of type-I interferon signaling to achieve functional cure of chronic hepatitis B

    doi: 10.1101/2024.06.14.24308555

    Figure Lengend Snippet: Aspirin and its metabolite Salicylate maintain IFNAR1 protein stability and IRF9 tyrosine phosphorylation, respectively, thus enhancing both the reactivity and durability of IFN-I signaling, which eventually promotes a functional cure of chronic HBV infection.

    Article Snippet: The antibodies in this study are listed here: Anti-IRF9 (Santa Cruz, Cat #sc-365893), Anti-pan-pY (Cell Signalling Technology, Cat #8954), Anti-Flag (Sigma, Cat #F7425), Anti-Tubulin (Proteintech, Cat #66031-1-Ig), Anti-GFP (Santa Cruz, Cat #sc-9996), Anti-p-STAT1(Y701) (Cell Signalling Technology, Cat #9167), Anti-STAT1 (Cell Signalling Technology, Cat #9176), Anti-PTP1B (Proteintech, Cat #11334-1-AP), Anti-β-Actin (Proteintech, Cat #66009), Anti-Myc (Abmart, Cat #M20002), Anti-HA (Abcam, Cat #ab9110), Anti-IFNAR1-PE (Invitrogen, Cat #MA5-23630), Anti-IFNAR1 (Sino Biological, Cat #13222-T20), Anti-β-Trcp (Cell Signalling Technology, Cat #11984),Anti-pan-AcK (Santa Cruz, Cat #sc-32268), Anti-Viperin (Abcam, Cat #107359), Anti-IFIT1 (Santa Cruz, Cat #sc-134948), Anti-HA (H1N1) (Sino Biological, Cat #11684-T56), Anti-p-STAT1 (S727) (Cell Signalling Technology, Cat #8826), Anti-p-STAT2 (Y690) (Cell Signalling Technology, Cat #88410), Anti-VSV-G (Abcam, Cat #ab1874), Anti-PKR (Cell Signalling Technology, Cat #3072S) and Anti-GAPDH (Goodhere Biological Technology, Cat #AB-M-M001).

    Techniques: Functional Assay, Infection