Interferon-Stimulated Response Element (ISRE)-Binding Protein Complex DRAF1 Is Activated in Sindbis Virus (HR)-Infected Cells

Behr, Matthias; Schieferdecker, Kerstin; Bühr, Patrick; Büter, M.; Petsophonsakul, Wilaiwan; Sirirungsi, Wasna; Redmann-Müller, Ingrid; Müller, Ulrike; Prempracha, Nalinee; Jungwirth, C.

doi:10.1089/107999001753289596

Cited by 10 publications

(5 citation statements)

References 51 publications

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“…IFNαβR −/− mice on the 129/SV/Pas background were initially obtained from M. Aguet, Swiss Institute of Experimental Cancer Research (Epalinges, Switzerland) ( Behr et al., 2001 , Dunn et al., 2005 ). CCHFV-L(1–1325) transgenic mice were generated at the WUSM Pathology Microinjection Core by microinjecting a linearized construct derived from pCAGGS-HA-L(1–1325) into B6 oocytes.…”

Section: Methodsmentioning

confidence: 99%

Ovarian Tumor Domain-Containing Viral Proteases Evade Ubiquitin- and ISG15-Dependent Innate Immune Responses

Frias-Stäheli

Giannakopoulos

Kikkert

et al. 2007

Cell Host & Microbe

318

431

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Ubiquitin (Ub) and interferon-stimulated gene product 15 (ISG15) reversibly conjugate to proteins and mediate important innate antiviral responses. The ovarian tumor (OTU) domain represents a superfamily of predicted proteases found in eukaryotic, bacterial, and viral proteins, some of which have Ub-deconjugating activity. We show that the OTU domain-containing proteases from nairoviruses and arteriviruses, two unrelated groups of RNA viruses, hydrolyze Ub and ISG15 from cellular target proteins. This broad activity contrasts with the target specificity of known mammalian OTU domain-containing proteins. Expression of a viral OTU domain-containing protein antagonizes the antiviral effects of ISG15 and enhances susceptibility to Sindbis virus infection in vivo. We also show that viral OTU domain-containing proteases inhibit NF-kappaB-dependent signaling. Thus, the deconjugating activity of viral OTU proteases represents a unique viral strategy to inhibit Ub- and ISG15-dependent antiviral pathways.

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Section: Methodsmentioning

confidence: 99%

Ovarian Tumor Domain-Containing Viral Proteases Evade Ubiquitin- and ISG15-Dependent Innate Immune Responses

Frias-Stäheli

Giannakopoulos

Kikkert

et al. 2007

Cell Host & Microbe

318

431

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“…ISG15 expression is almost undetectable under normal conditions but is strongly up-regulated during viral infections such as human cytomegalovirus (HCMV), herpes simplex virus (HSV), Sindbis virus (SV) and hepatitis C virus (HCV) [19],[20],[21],[22],[23],[24]. It has been speculated that the ISG15 up-regulation following viral infection is involved in different strategies of the antiviral response [25],[26].…”

Section: Introductionmentioning

confidence: 99%

Vaccinia Virus E3 Protein Prevents the Antiviral Action of ISG15

et al. 2008

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The ubiquitin-like modifier ISG15 is one of the most predominant proteins induced by type I interferons (IFN). In this study, murine embryo fibroblast (MEFs) and mice lacking the gene were used to demonstrate a novel role of ISG15 as a host defense molecule against vaccinia virus (VACV) infection. In MEFs, the growth of replication competent Western Reserve (WR) VACV strain was affected by the absence of ISG15, but in addition, virus lacking E3 protein (VVΔE3L) that is unable to grow in ISG15+/+ cells replicated in ISG15-deficient cells. Inhibiting ISG15 with siRNA or promoting its expression in ISG15−/− cells with a lentivirus vector showed that VACV replication was controlled by ISG15. Immunoprecipitation analysis revealed that E3 binds ISG15 through its C-terminal domain. The VACV antiviral action of ISG15 and its interaction with E3 are events independent of PKR (double-stranded RNA-dependent protein kinase). In mice lacking ISG15, infection with VVΔE3L caused significant disease and mortality, an effect not observed in VVΔE3L-infected ISG15+/+ mice. Pathogenesis in ISG15-deficient mice infected with VVΔE3L or with an E3L deletion mutant virus lacking the C-terminal domain triggered an enhanced inflammatory response in the lungs compared with ISG15+/+-infected mice. These findings showed an anti-VACV function of ISG15, with the virus E3 protein suppressing the action of the ISG15 antiviral factor.

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“…IRF-1, -3 and -7 are known to bind ISRE after dsRNA induction (Bandyopadhyay et al, 1995;Behr et al, 2001). The amount of IRF-1 bound to the ISRE probe (Probe 2) was markedly increased only after 4 h of dsRNA treatment (Figure 4b, lane 8).…”

mentioning

confidence: 97%

The exonuclease ISG20 is directly induced by synthetic dsRNA via NF-κB and IRF1 activation

et al. 2004

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Many interferon (IFN)-stimulated genes are also induced by double-stranded RNA (dsRNA), a component closely associated with the IFN system in the context of virushost interactions. Recently, we demonstrated that the IFN-induced 3 0 -5 0 exonuclease ISG20 possesses antiviral activities against RNA viruses. Here we show that ISG20 induction by synthetic dsRNA (pIpC) is stronger and faster than its induction by IFN. Two families of transcription factors are implicated in the transcriptional activation of ISG20 by dsRNA. Initially, the NF-kB factors p50 and p65 bind and activate the kB element of the Isg20 promoter. This is followed by IRF1 binding to the ISRE. As pIpC often induces protein movements in the cells, we questioned whether it could influence ISG20 localization. Interestingly and contrary to IFN, dsRNA induces a nuclear matrix enrichment of the ISG20 protein. dsRNA induction of ISG20 via NF-kB and its antiviral activity led us to suggest that ISG20 could participate in the cellular response to virus infection.

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Interferon-Stimulated Response Element (ISRE)-Binding Protein Complex DRAF1 Is Activated in Sindbis Virus (HR)-Infected Cells

Cited by 10 publications

References 51 publications

Ovarian Tumor Domain-Containing Viral Proteases Evade Ubiquitin- and ISG15-Dependent Innate Immune Responses

Ovarian Tumor Domain-Containing Viral Proteases Evade Ubiquitin- and ISG15-Dependent Innate Immune Responses

Vaccinia Virus E3 Protein Prevents the Antiviral Action of ISG15

The exonuclease ISG20 is directly induced by synthetic dsRNA via NF-κB and IRF1 activation

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