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  1. AU="Mukawera, Espérance"
  2. AU=Almaqwashi Ali A.
  3. AU="Workman, R L"
  4. AU="Gordini, Giovanni"
  5. AU=Beck Andrew H.
  6. AU="Aybar, N"
  7. AU="Majidian Ba, Mandy"
  8. AU=Botero-Rodriguez Felipe AU=Botero-Rodriguez Felipe
  9. AU="Pozo, Franco Andres Del"
  10. AU="Ohno, Hideaki"
  11. AU="Mohit"
  12. AU="Jzerman, Hans I"
  13. AU="Deepali Jain"
  14. AU=Cimen S.
  15. AU="Laskey, Daniel"
  16. AU="Pérez, Noelia"
  17. AU="Shaf Keshavjee"
  18. AU=Stewart J. D.
  19. AU="Victor Daka"
  20. AU="Iglesias, C"
  21. AU="Williams, Howard L."
  22. AU=Tilmann Christopher
  23. AU=Stefansson Steingrimur
  24. AU="Schindler, Tobias"
  25. AU="Araújo, Cristina de O"
  26. AU=Goda Jayant S.
  27. AU="Peditto, Piera"
  28. AU="Dünn, Hans-Wilhelm"
  29. AU=Tyznik Aaron J.
  30. AU="Siddiqui, Fasih Sami"
  31. AU="Abt, S."
  32. AU="Sultana, Sufia"
  33. AU="Yuan, Shengwang"
  34. AU="Sedehizadeh, Saam"
  35. AU=Jeon Young-Woo
  36. AU=Narayanan Navaneeth
  37. AU=Beckwith Kyle A.
  38. AU=Anderson Robert H
  39. AU=Trindade P A
  40. AU=Gohil R
  41. AU="Zhengyi, Wu"
  42. AU=Wessels J A M
  43. AU="Porter, Lavinia"
  44. AU=Al-Mayman Sulaiman

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  1. Artikel ; Online: Ozone inactivation of airborne influenza and lack of resistance of respiratory syncytial virus to aerosolization and sampling processes.

    Dubuis, Marie-Eve / Racine, Étienne / Vyskocil, Jonathan M / Turgeon, Nathalie / Tremblay, Christophe / Mukawera, Espérance / Boivin, Guy / Grandvaux, Nathalie / Duchaine, Caroline

    PloS one

    2021  Band 16, Heft 7, Seite(n) e0253022

    Abstract: Influenza and RSV are human viruses responsible for outbreaks in hospitals, long-term care facilities and nursing homes. The present study assessed an air treatment using ozone at two relative humidity conditions (RHs) in order to reduce the infectivity ... ...

    Abstract Influenza and RSV are human viruses responsible for outbreaks in hospitals, long-term care facilities and nursing homes. The present study assessed an air treatment using ozone at two relative humidity conditions (RHs) in order to reduce the infectivity of airborne influenza. Bovine pulmonary surfactant (BPS) and synthetic tracheal mucus (STM) were used as aerosols protectants to better reflect the human aerosol composition. Residual ozone concentration inside the aerosol chamber was also measured. RSV's sensitivity resulted in testing its resistance to aerosolization and sampling processes instead of ozone exposure. The results showed that without supplement and with STM, a reduction in influenza A infectivity of four orders of magnitude was obtained with an exposure to 1.70 ± 0.19 ppm of ozone at 76% RH for 80 min. Consequently, ozone could be considered as a virucidal disinfectant for airborne influenza A. RSV did not withstand the aerosolization and sampling processes required for the use of the experimental setup. Therefore, ozone exposure could not be performed for this virus. Nonetheless, this study provides great insight for the efficacy of ozone as an air treatment for the control of nosocomial influenza A outbreaks.
    Mesh-Begriff(e) Aerosols ; Air Microbiology ; Cross Infection/prevention & control ; Disinfection/methods ; Humans ; Influenza A virus/drug effects ; Influenza, Human/prevention & control ; Ozone/administration & dosage ; Ozone/pharmacology ; Real-Time Polymerase Chain Reaction ; Respiratory Syncytial Virus Infections/prevention & control ; Respiratory Syncytial Viruses/drug effects ; Virus Inactivation/drug effects
    Chemische Substanzen Aerosols ; Ozone (66H7ZZK23N)
    Sprache Englisch
    Erscheinungsdatum 2021-07-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0253022
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Redox-modulating agents target NOX2-dependent IKKε oncogenic kinase expression and proliferation in human breast cancer cell lines.

    Mukawera, Espérance / Chartier, Stefany / Williams, Virginie / Pagano, Patrick J / Lapointe, Réjean / Grandvaux, Nathalie

    Redox biology

    2015  Band 6, Seite(n) 9–18

    Abstract: Oxidative stress is considered a causative factor in carcinogenesis, but also in the development of resistance to current chemotherapies. The appropriate usage of redox-modulating compounds is limited by the lack of knowledge of their impact on specific ... ...

    Abstract Oxidative stress is considered a causative factor in carcinogenesis, but also in the development of resistance to current chemotherapies. The appropriate usage of redox-modulating compounds is limited by the lack of knowledge of their impact on specific molecular pathways. Increased levels of the IKKε kinase, as a result of gene amplification or aberrant expression, are observed in a substantial number of breast carcinomas. IKKε not only plays a key role in cell transformation and invasiveness, but also in the development of resistance to tamoxifen. Here, we studied the effect of in vitro treatment with the redox-modulating triphenylmethane dyes, Gentian Violet and Brilliant Green, and nitroxide Tempol on IKKε expression and cell proliferation in the human breast cancer epithelial cell lines exhibiting amplification of IKKε, MCF-7 and ZR75.1. We show that Gentian Violet, Brilliant Green and Tempol significantly decrease intracellular superoxide anion levels and inhibit IKKε expression and cell viability. Treatment with Gentian Violet and Brilliant Green was associated with a reduced cyclin D1 expression and activation of caspase 3 and/or 7. Tempol decreased cyclin D1 expression in both cell lines, while activation of caspase 7 was only observed in MCF-7 cells. Silencing of the superoxide-generating NOX2 NADPH oxidase expressed in breast cancer cells resulted in the significant reduction of IKKε expression. Taken together, our results suggest that redox-modulating compounds targeting NOX2 could present a particular therapeutic interest in combination therapy against breast carcinomas exhibiting IKKε amplification.
    Mesh-Begriff(e) Caspase 3/genetics ; Caspase 3/metabolism ; Caspase 7/genetics ; Caspase 7/metabolism ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Cyclic N-Oxides/pharmacology ; Cyclin D1/genetics ; Cyclin D1/metabolism ; Female ; Gene Expression Regulation, Neoplastic ; Gentian Violet/pharmacology ; Humans ; I-kappa B Kinase/antagonists & inhibitors ; I-kappa B Kinase/genetics ; I-kappa B Kinase/metabolism ; MCF-7 Cells ; Membrane Glycoproteins/antagonists & inhibitors ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; NADPH Oxidase 2 ; NADPH Oxidases/antagonists & inhibitors ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Oxidation-Reduction/drug effects ; Quaternary Ammonium Compounds/pharmacology ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Signal Transduction ; Spin Labels ; Superoxides/antagonists & inhibitors ; Superoxides/metabolism
    Chemische Substanzen CCND1 protein, human ; Cyclic N-Oxides ; Membrane Glycoproteins ; Quaternary Ammonium Compounds ; RNA, Small Interfering ; Spin Labels ; Superoxides (11062-77-4) ; Cyclin D1 (136601-57-5) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; I-kappa B Kinase (EC 2.7.11.10) ; CASP3 protein, human (EC 3.4.22.-) ; CASP7 protein, human (EC 3.4.22.-) ; Caspase 3 (EC 3.4.22.-) ; Caspase 7 (EC 3.4.22.-) ; brilliant green (G0L543D370) ; Gentian Violet (J4Z741D6O5) ; tempol (U78ZX2F65X)
    Sprache Englisch
    Erscheinungsdatum 2015-06-23
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2213-2317
    ISSN (online) 2213-2317
    DOI 10.1016/j.redox.2015.06.010
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: The Combination of IFN β and TNF Induces an Antiviral and Immunoregulatory Program via Non-Canonical Pathways Involving STAT2 and IRF9.

    Mariani, Mélissa K / Dasmeh, Pouria / Fortin, Audray / Caron, Elise / Kalamujic, Mario / Harrison, Alexander N / Hotea, Diana I / Kasumba, Dacquin M / Cervantes-Ortiz, Sandra L / Mukawera, Espérance / Serohijos, Adrian W R / Grandvaux, Nathalie

    Cells

    2019  Band 8, Heft 8

    Abstract: Interferon (IFN) β and Tumor Necrosis Factor (TNF) are key players in immunity against viruses. Compelling evidence has shown that the antiviral and inflammatory transcriptional response induced by IFNβ is reprogrammed by crosstalk with TNF. IFNβ mainly ... ...

    Abstract Interferon (IFN) β and Tumor Necrosis Factor (TNF) are key players in immunity against viruses. Compelling evidence has shown that the antiviral and inflammatory transcriptional response induced by IFNβ is reprogrammed by crosstalk with TNF. IFNβ mainly induces interferon-stimulated genes by the Janus kinase (JAK)/signal transducer and activator of transcription (STAT) pathway involving the canonical ISGF3 transcriptional complex, composed of STAT1, STAT2, and IRF9. The signaling pathways engaged downstream of the combination of IFNβ and TNF remain elusive, but previous observations suggested the existence of a response independent of STAT1. Here, using genome-wide transcriptional analysis by RNASeq, we observed a broad antiviral and immunoregulatory response initiated in the absence of STAT1 upon IFNβ and TNF costimulation. Additional stratification of this transcriptional response revealed that STAT2 and IRF9 mediate the expression of a wide spectrum of genes. While a subset of genes was regulated by the concerted action of STAT2 and IRF9, other gene sets were independently regulated by STAT2 or IRF9. Collectively, our data supports a model in which STAT2 and IRF9 act through non-canonical parallel pathways to regulate distinct pool of antiviral and immunoregulatory genes in conditions with elevated levels of both IFNβ and TNF.
    Mesh-Begriff(e) A549 Cells ; Humans ; Interferon-Stimulated Gene Factor 3, gamma Subunit/metabolism ; Interferon-beta/physiology ; STAT2 Transcription Factor/metabolism ; Tumor Necrosis Factor-alpha/physiology ; Vesicular Stomatitis/immunology ; Vesicular stomatitis Indiana virus/immunology
    Chemische Substanzen IRF9 protein, human ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; STAT2 Transcription Factor ; STAT2 protein, human ; Tumor Necrosis Factor-alpha ; Interferon-beta (77238-31-4)
    Sprache Englisch
    Erscheinungsdatum 2019-08-17
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells8080919
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Respiratory syncytial virus-mediated NF-kappa B p65 phosphorylation at serine 536 is dependent on RIG-I, TRAF6, and IKK beta.

    Yoboua, Fabrice / Martel, Alexis / Duval, Annick / Mukawera, Espérance / Grandvaux, Nathalie

    Journal of virology

    2010  Band 84, Heft 14, Seite(n) 7267–7277

    Abstract: Respiratory syncytial virus (RSV) is the etiological agent of acute respiratory diseases, such as bronchiolitis and pneumonia. The exacerbated production of proinflammatory cytokines and chemokines in the airways in response to RSV is an important pillar ...

    Abstract Respiratory syncytial virus (RSV) is the etiological agent of acute respiratory diseases, such as bronchiolitis and pneumonia. The exacerbated production of proinflammatory cytokines and chemokines in the airways in response to RSV is an important pillar in the development of these pathologies. As such, a keen understanding of the mechanisms that modulate the inflammatory response during RSV infection is of pivotal importance to developing effective treatment. The NF-kappaB transcription factor is a major regulator of proinflammatory cytokine and chemokine genes. However, RSV-mediated activation of NF-kappaB is far from characterized. We recently demonstrated that aside from the well-characterized IkappaBalpha phosphorylation and degradation, the phosphorylation of p65 at Ser536 is an essential event regulating the RSV-mediated NF-kappaB-dependent promoter transactivation. In the present study, using small interfering RNA and pharmacological inhibitors, we now demonstrate that RSV sensing by the RIG-I cytoplasmic receptor triggers a signaling cascade involving the MAVS and TRAF6 adaptors that ultimately leads to p65ser536 phosphorylation by the IKKbeta kinase. In a previous study, we highlighted a critical role of the NOX2-containing NADPH oxidase enzyme as an upstream regulator of both the IkappaBalphaSer32 and p65Ser536 in human airway epithelial cells. Here, we demonstrate that inhibition of NOX2 significantly decreases IKKbeta activation. Taken together, our data identify a new RIG-I/MAVS/TRAF6/IKKbeta/p65Ser536 pathway placed under the control of NOX2, thus characterizing a novel regulatory pathway involved in NF-kappaB-driven proinflammatory response in the context of RSV infection.
    Mesh-Begriff(e) Animals ; Cell Line ; DEAD Box Protein 58 ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Humans ; I-kappa B Kinase/genetics ; I-kappa B Kinase/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; NADPH Oxidase 2 ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Phosphorylation ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Receptors, Immunologic ; Respiratory Syncytial Viruses/physiology ; Serine/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 6/genetics ; TNF Receptor-Associated Factor 6/metabolism ; Transcription Factor RelA/genetics ; Transcription Factor RelA/metabolism ; Virus Replication
    Chemische Substanzen Membrane Glycoproteins ; RNA, Small Interfering ; RNA, Viral ; Receptors, Immunologic ; TNF Receptor-Associated Factor 6 ; Transcription Factor RelA ; Serine (452VLY9402) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; I-kappa B Kinase (EC 2.7.11.10) ; RIGI protein, human (EC 3.6.1.-) ; DEAD Box Protein 58 (EC 3.6.4.13) ; DEAD-box RNA Helicases (EC 3.6.4.13)
    Sprache Englisch
    Erscheinungsdatum 2010-04-21
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.00142-10
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

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  5. Artikel ; Online: DUSP1 regulates apoptosis and cell migration, but not the JIP1-protected cytokine response, during Respiratory Syncytial Virus and Sendai Virus infection.

    Robitaille, Alexa C / Caron, Elise / Zucchini, Nicolas / Mukawera, Espérance / Adam, Damien / Mariani, Mélissa K / Gélinas, Anaïs / Fortin, Audray / Brochiero, Emmanuelle / Grandvaux, Nathalie

    Scientific reports

    2017  Band 7, Heft 1, Seite(n) 17388

    Abstract: The host antiviral response involves the induction of interferons and proinflammatory cytokines, but also the activation of cell death pathways, including apoptosis, to limit viral replication and spreading. This host defense is strictly regulated to ... ...

    Abstract The host antiviral response involves the induction of interferons and proinflammatory cytokines, but also the activation of cell death pathways, including apoptosis, to limit viral replication and spreading. This host defense is strictly regulated to eliminate the infection while limiting tissue damage that is associated with virus pathogenesis. Post-translational modifications, most notably phosphorylation, are key regulators of the antiviral defense implying an important role of protein phosphatases. Here, we investigated the role of the dual-specificity phosphatase 1 (DUSP1) in the host defense against human respiratory syncytial virus (RSV), a pathogenic virus of the Pneumoviridae family, and Sendai virus (SeV), a model virus being developed as a vector for anti-RSV vaccine. We found that DUSP1 is upregulated before being subjected to proteasomal degradation. DUSP1 does not inhibit the antiviral response, but negatively regulates virus-induced JNK/p38 MAPK phosphorylation. Interaction with the JNK-interacting protein 1 scaffold protein prevents dephosphorylation of JNK by DUSP1, likely explaining that AP-1 activation and downstream cytokine production are protected from DUSP1 inhibition. Importantly, DUSP1 promotes SeV-induced apoptosis and suppresses cell migration in RSV-infected cells. Collectively, our data unveils a previously unrecognized selective role of DUSP1 in the regulation of tissue damage and repair during infections by RSV and SeV.
    Mesh-Begriff(e) A549 Cells ; Adaptor Proteins, Signal Transducing/metabolism ; Apoptosis ; Cell Movement ; Dual Specificity Phosphatase 1/genetics ; Dual Specificity Phosphatase 1/metabolism ; Gene Expression Regulation ; Humans ; MAP Kinase Signaling System ; Respiratory Syncytial Virus Infections/genetics ; Respiratory Syncytial Virus Infections/metabolism ; Respiratory Syncytial Virus, Human ; Respirovirus Infections/genetics ; Respirovirus Infections/metabolism ; Sendai virus
    Chemische Substanzen Adaptor Proteins, Signal Transducing ; MAPK8IP1 protein, human ; DUSP1 protein, human (EC 3.1.3.48) ; Dual Specificity Phosphatase 1 (EC 3.1.3.48)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2017-12-12
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-17689-0
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: IFNβ/TNFα synergism induces a non-canonical STAT2/IRF9-dependent pathway triggering a novel DUOX2 NADPH oxidase-mediated airway antiviral response.

    Fink, Karin / Martin, Lydie / Mukawera, Esperance / Chartier, Stéfany / De Deken, Xavier / Brochiero, Emmanuelle / Miot, Françoise / Grandvaux, Nathalie

    Cell research

    2013  Band 23, Heft 5, Seite(n) 673–690

    Abstract: Airway epithelial cells are key initial innate immune responders in the fight against respiratory viruses, primarily via the secretion of antiviral and proinflammatory cytokines that act in an autocrine/paracrine fashion to trigger the establishment of ... ...

    Abstract Airway epithelial cells are key initial innate immune responders in the fight against respiratory viruses, primarily via the secretion of antiviral and proinflammatory cytokines that act in an autocrine/paracrine fashion to trigger the establishment of an antiviral state. It is currently thought that the early antiviral state in airway epithelial cells primarily relies on IFNβ secretion and the subsequent activation of the interferon-stimulated gene factor 3 (ISGF3) transcription factor complex, composed of STAT1, STAT2 and IRF9, which regulates the expression of a panoply of interferon-stimulated genes encoding proteins with antiviral activities. However, the specific pathways engaged by the synergistic action of different cytokines during viral infections, and the resulting physiological outcomes are still ill-defined. Here, we unveil a novel delayed antiviral response in the airways, which is initiated by the synergistic autocrine/paracrine action of IFNβ and TNFα, and signals through a non-canonical STAT2- and IRF9-dependent, but STAT1-independent cascade. This pathway ultimately leads to the late induction of the DUOX2 NADPH oxidase expression. Importantly, our study uncovers that the development of the antiviral state relies on DUOX2-dependent H2O2 production. Key antiviral pathways are often targeted by evasion strategies evolved by various pathogenic viruses. In this regard, the importance of the novel DUOX2-dependent antiviral pathway is further underlined by the observation that the human respiratory syncytial virus is able to subvert DUOX2 induction.
    Mesh-Begriff(e) Antiviral Agents/pharmacology ; Autocrine Communication/drug effects ; Cell Line ; Drug Synergism ; Dual Oxidases ; Humans ; Hydrogen Peroxide/metabolism ; Immunity, Innate/drug effects ; Interferon-Stimulated Gene Factor 3, gamma Subunit/metabolism ; Interferon-beta/genetics ; Interferon-beta/metabolism ; Interferon-beta/pharmacology ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Paracrine Communication/drug effects ; RNA Interference ; RNA, Messenger/metabolism ; RNA, Small Cytoplasmic/metabolism ; Receptor, Interferon alpha-beta/antagonists & inhibitors ; Receptor, Interferon alpha-beta/genetics ; Receptor, Interferon alpha-beta/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics ; Recombinant Proteins/pharmacology ; Respiratory Syncytial Viruses/metabolism ; STAT1 Transcription Factor/metabolism ; STAT2 Transcription Factor/metabolism ; Sendai virus/metabolism ; Signal Transduction ; Tumor Necrosis Factor-alpha/genetics ; Tumor Necrosis Factor-alpha/metabolism ; Tumor Necrosis Factor-alpha/pharmacology
    Chemische Substanzen Antiviral Agents ; IFNAR1 protein, human ; IRF9 protein, human ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; RNA, Messenger ; RNA, Small Cytoplasmic ; Recombinant Proteins ; STAT1 Transcription Factor ; STAT2 Transcription Factor ; Tumor Necrosis Factor-alpha ; Receptor, Interferon alpha-beta (156986-95-7) ; Interferon-beta (77238-31-4) ; Hydrogen Peroxide (BBX060AN9V) ; Dual Oxidases (EC 1.11.1.-) ; NADPH Oxidases (EC 1.6.3.-) ; DUOX2 protein, human (EC 1.6.3.1)
    Sprache Englisch
    Erscheinungsdatum 2013-04-02
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/cr.2013.47
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 5283: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Artikel ; Online: DUSP1 regulates apoptosis and cell migration, but not the JIP1-protected cytokine response, during Respiratory Syncytial Virus and Sendai Virus infection

    Robitaille, Alexa C. / Caron, Elise / Zucchini, Nicolas / Mukawera, Espérance / Adam, Damien / Mariani, Mélissa K. / Gélinas, Anaïs / Fortin, Audray / Brochiero, Emmanuelle / Grandvaux, Nathalie

    bioRxiv

    Abstract: The host antiviral response involves the induction of interferons and proinflammatory cytokines, but also the activation of cell death pathways, including apoptosis, to limit viral replication and spreading. This host defense is strictly regulated to ... ...

    Abstract The host antiviral response involves the induction of interferons and proinflammatory cytokines, but also the activation of cell death pathways, including apoptosis, to limit viral replication and spreading. This host defense is strictly regulated to eliminate the infection while limiting tissue damage that is associated with virus pathogenesis. Post-translational modifications, most notably phosphorylation, are key regulators of the antiviral defense implying an important role of protein phosphatases. Here, we investigated the role of the dual-specificity phosphatase 1 (DUSP1) in the host defense against human respiratory syncytial virus (RSV), a pathogenic virus of the Pneumoviridae family, and Sendai virus (SeV), a model virus being developed as a vector for anti-RSV vaccine. We found that DUSP1 is upregulated before being subjected to proteasomal degradation. DUSP1 does not inhibit the antiviral response, but negatively regulates virus-induced JNK/p38 MAPK phosphorylation. Interaction with the JNK-interacting protein 1 scaffold protein prevents dephosphorylation of JNK by DUSP1, likely explaining that AP-1 activation and downstream cytokine production are protected from DUSP1 inhibition. Importantly, DUSP1 promotes SeV-induced apoptosis and suppresses cell migration in RSV-infected cells. Collectively, our data unveil a previously unrecognized selective role of DUSP1 in the regulation of tissue damage and repair during infections by RSV and SeV.
    Schlagwörter covid19
    Verlag BioRxiv; MedRxiv
    Dokumenttyp Artikel ; Online
    DOI 10.1101/163360
    Datenquelle COVID19

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  8. Artikel ; Online: Requirement of NOX2 and reactive oxygen species for efficient RIG-I-mediated antiviral response through regulation of MAVS expression.

    Soucy-Faulkner, Anton / Mukawera, Espérance / Fink, Karin / Martel, Alexis / Jouan, Loubna / Nzengue, Yves / Lamarre, Daniel / Vande Velde, Christine / Grandvaux, Nathalie

    PLoS pathogens

    2010  Band 6, Heft 6, Seite(n) e1000930

    Abstract: The innate immune response is essential to the host defense against viruses, through restriction of virus replication and coordination of the adaptive immune response. Induction of antiviral genes is a tightly regulated process initiated mainly through ... ...

    Abstract The innate immune response is essential to the host defense against viruses, through restriction of virus replication and coordination of the adaptive immune response. Induction of antiviral genes is a tightly regulated process initiated mainly through sensing of invading virus nucleic acids in the cytoplasm by RIG-I like helicases, RIG-I or Mda5, which transmit the signal through a common mitochondria-associated adaptor, MAVS. Although major breakthroughs have recently been made, much remains unknown about the mechanisms that translate virus recognition into antiviral genes expression. Beside the reputed detrimental role, reactive oxygen species (ROS) act as modulators of cellular signaling and gene regulation. NADPH oxidase (NOX) enzymes are a main source of deliberate cellular ROS production. Here, we found that NOX2 and ROS are required for the host cell to trigger an efficient RIG-I-mediated IRF-3 activation and downstream antiviral IFNbeta and IFIT1 gene expression. Additionally, we provide evidence that NOX2 is critical for the expression of the central mitochondria-associated adaptor MAVS. Taken together these data reveal a new facet to the regulation of the innate host defense against viruses through the identification of an unrecognized role of NOX2 and ROS.
    Mesh-Begriff(e) Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Blotting, Western ; Bronchi/cytology ; Bronchi/immunology ; Bronchi/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cells, Cultured ; DEAD Box Protein 58 ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Gene Expression Regulation ; Humans ; Immunity, Innate ; Interferon Regulatory Factor-3/genetics ; Interferon Regulatory Factor-3/metabolism ; Interleukin-6/genetics ; Interleukin-6/metabolism ; Luciferases/metabolism ; Lung Neoplasms/immunology ; Lung Neoplasms/metabolism ; Lung Neoplasms/virology ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; NADPH Oxidase 2 ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; RNA, Messenger/genetics ; RNA-Binding Proteins ; Reactive Oxygen Species/metabolism ; Receptors, Immunologic ; Respirovirus Infections/immunology ; Respirovirus Infections/metabolism ; Respirovirus Infections/virology ; Reverse Transcriptase Polymerase Chain Reaction ; Sendai virus/physiology ; Signal Transduction
    Chemische Substanzen Adaptor Proteins, Signal Transducing ; Carrier Proteins ; IFIT1 protein, human ; Interferon Regulatory Factor-3 ; Interleukin-6 ; MAVS protein, human ; Membrane Glycoproteins ; RNA, Messenger ; RNA-Binding Proteins ; Reactive Oxygen Species ; Receptors, Immunologic ; Luciferases (EC 1.13.12.-) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; RIGI protein, human (EC 3.6.1.-) ; DEAD Box Protein 58 (EC 3.6.4.13) ; DEAD-box RNA Helicases (EC 3.6.4.13)
    Sprache Englisch
    Erscheinungsdatum 2010-06-03
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1000930
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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