Interferon regulatory factor 3 from sea perch (Lateolabrax japonicus) exerts antiviral function against nervous necrosis virus infection

2018 ◽  
Vol 88 ◽  
pp. 200-205 ◽  
Author(s):  
Wanwan Zhang ◽  
Zelin Li ◽  
Peng Jia ◽  
Wei Liu ◽  
Meisheng Yi ◽  
...  
Keyword(s):  
Virus Infection ◽  
Interferon Regulatory Factor ◽  
Nervous Necrosis Virus ◽  
Regulatory Factor ◽  
Necrosis Virus ◽  
Lateolabrax Japonicus ◽  
Interferon Regulatory Factor 3 ◽  
Antiviral Function ◽  
Sea Perch

Fish DDX3X exerts antiviral function against grouper nervous necrosis virus infection

2017 ◽  
Vol 71 ◽  
pp. 95-104 ◽  
Author(s):  
Jiaxin Liu ◽  
Xiaohong Huang ◽  
Yepin Yu ◽  
Jingcheng Zhang ◽  
Songwei Ni ◽  
...  
Keyword(s):  
Virus Infection ◽  
Nervous Necrosis Virus ◽  
Necrosis Virus ◽  
Antiviral Function

scholarly journals Inhibition of Beta Interferon Induction by Severe Acute Respiratory Syndrome Coronavirus Suggests a Two-Step Model for Activation of Interferon Regulatory Factor 3

2005 ◽  
Vol 79 (4) ◽  
pp. 2079-2086 ◽  
Author(s):  
Martin Spiegel ◽  
Andreas Pichlmair ◽  
Luis Martínez-Sobrido ◽  
Jerome Cros ◽  
Adolfo García-Sastre ◽  
...  
Keyword(s):  
Virus Infection ◽  
Severe Acute Respiratory Syndrome ◽  
Promoter Activity ◽  
Nuclear Transport ◽  
Interferon Regulatory Factor ◽  
Creb Binding Protein ◽  
Regulatory Factor ◽  
Interferon Regulatory Factor 3 ◽  
Control Virus ◽  
Novel Coronavirus

ABSTRACT Severe acute respiratory syndrome (SARS) is caused by a novel coronavirus termed SARS-CoV. We and others have previously shown that the replication of SARS-CoV can be suppressed by exogenously added interferon (IFN), a cytokine which is normally synthesized by cells as a reaction to virus infection. Here, we demonstrate that SARS-CoV escapes IFN-mediated growth inhibition by preventing the induction of IFN-β. In SARS-CoV-infected cells, no endogenous IFN-β transcripts and no IFN-β promoter activity were detected. Nevertheless, the transcription factor interferon regulatory factor 3 (IRF-3), which is essential for IFN-β promoter activity, was transported from the cytoplasm to the nucleus early after infection with SARS-CoV. However, at a later time point in infection, IRF-3 was again localized in the cytoplasm. By contrast, IRF-3 remained in the nucleus of cells infected with the IFN-inducing control virus Bunyamwera delNSs. Other signs of IRF-3 activation such as hyperphosphorylation, homodimer formation, and recruitment of the coactivator CREB-binding protein (CBP) were found late after infection with the control virus but not with SARS-CoV. Our data suggest that nuclear transport of IRF-3 is an immediate-early reaction to virus infection and may precede its hyperphosphorylation, homodimer formation, and binding to CBP. In order to escape activation of the IFN system, SARS-CoV appears to block a step after the early nuclear transport of IRF-3.

scholarly journals Transcriptional Profiling of Interferon Regulatory Factor 3 Target Genes: Direct Involvement in the Regulation of Interferon-Stimulated Genes

2002 ◽  
Vol 76 (11) ◽  
pp. 5532-5539 ◽  
Author(s):  
Nathalie Grandvaux ◽  
Marc J. Servant ◽  
Benjamin tenOever ◽  
Ganes C. Sen ◽  
Siddarth Balachandran ◽  
...  
Keyword(s):  
Virus Infection ◽  
Target Genes ◽  
Expression Profiles ◽  
Expression System ◽  
Active Form ◽  
Interferon Regulatory Factor ◽  
Inducible Expression ◽  
Immediate Early ◽  
Regulatory Factor ◽  
Interferon Regulatory Factor 3

ABSTRACT Ubiquitously expressed interferon regulatory factor 3 (IRF-3) is directly activated after virus infection and functions as a key activator of the immediate-early alpha/beta interferon (IFN) genes, as well as the RANTES chemokine gene. In the present study, a tetracycline-inducible expression system expressing a constitutively active form of IRF-3 (IRF-3 5D) was combined with DNA microarray analysis to identify target genes regulated by IRF-3. Changes in mRNA expression profiles of 8,556 genes were monitored after Tet-inducible expression of IRF-3 5D. Among the genes upregulated by IRF-3 were transcripts for several known IFN-stimulated genes (ISGs). Subsequent analysis revealed that IRF-3 directly induced the expression of ISG56 in an IFN-independent manner through the IFN-stimulated responsive elements (ISREs) of the ISG56 promoter. These results demonstrate that, in addition to its role in the formation of a functional immediate-early IFN-β enhanceosome, IRF-3 is able to discriminate among ISRE-containing genes involved in the establishment of the antiviral state as a direct response to virus infection.

scholarly journals Structural and Functional Analysis of Interferon Regulatory Factor 3: Localization of the Transactivation and Autoinhibitory Domains

1999 ◽  
Vol 19 (4) ◽  
pp. 2465-2474 ◽  
Author(s):  
Rongtuan Lin ◽  
Yael Mamane ◽  
John Hiscott
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Virus Infection ◽  
Nuclear Translocation ◽  
Sendai Virus ◽  
Interferon Regulatory Factor ◽  
Phosphorylation Sites ◽  
Transactivation Domain ◽  
Regulatory Factor ◽  
Interferon Regulatory Factor 3

ABSTRACT The interferon regulatory factor 3 (IRF-3) gene encodes a 55-kDa protein which is expressed constitutively in all tissues. In unstimulated cells, IRF-3 is present in an inactive cytoplasmic form; following Sendai virus infection, IRF-3 is posttranslationally modified by protein phosphorylation at multiple serine and threonine residues located in the carboxy terminus. Virus-induced phosphorylation of IRF-3 leads to cytoplasmic to nuclear translocation of phosphorylated IRF-3, association with the transcriptional coactivator CBP/p300, and stimulation of DNA binding and transcriptional activities of virus-inducible genes. Using yeast and mammalian one-hybrid analysis, we now demonstrate that an extended, atypical transactivation domain is located in the C terminus of IRF-3 between amino acids (aa) 134 and 394. We also show that the C-terminal domain of IRF-3 located between aa 380 and 427 participates in the autoinhibition of IRF-3 activity via an intramolecular association with the N-terminal region between aa 98 and 240. After Sendai virus infection, an intermolecular association between IRF-3 proteins is detected, demonstrating a virus-dependent formation of IRF-3 homodimers; this interaction is also observed in the absence of virus infection with a constitutively activated form of IRF-3. Substitution of the C-terminal Ser-Thr phosphorylation sites with the phosphomimetic Asp in the region ISNSHPLSLTSDQ between amino acids 395 and 407 [IRF-3(5D)], but not the adjacent S385 and S386 residues, generates a constitutively activated DNA binding form of IRF-3. In contrast, substitution of S385 and S386 with either Ala or Asp inhibits both DNA binding and transactivation activities of the IRF-3(5D) protein. These studies thus define the transactivation domain of IRF-3, two domains that participate in the autoinhibition of IRF-3 activity, and the regulatory phosphorylation sites controlling IRF-3 dimer formation, DNA binding activity, and association with the CBP/p300 coactivator.

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