About: NSs Protein of Sandfly Fever Sicilian Phlebovirus Counteracts Interferon (IFN) Induction by Masking the DNA-Binding Domain of IFN Regulatory Factor 3

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About: NSs Protein of Sandfly Fever Sicilian Phlebovirus Counteracts Interferon (IFN) Induction by Masking the DNA-Binding Domain of IFN Regulatory Factor 3 Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	NSs Protein of Sandfly Fever Sicilian Phlebovirus Counteracts Interferon (IFN) Induction by Masking the DNA-Binding Domain of IFN Regulatory Factor 3
Creator	Weber, Friedemann Pichlmair, Andreas Habjan, Matthias Superti-Furga, Giulio Wulle, Julia Wuerth, Jennifer
Source	PMC
abstract	Sandfly fever Sicilian virus (SFSV) is one of the most widespread and frequently identified members of the genus Phlebovirus (order Bunyavirales, family Phenuiviridae) infecting humans. Being transmitted by Phlebotomus sandflies, SFSV causes a self-limiting, acute, often incapacitating febrile disease (“sandfly fever,” “Pappataci fever,” or “dog disease”) that has been known since at least the beginning of the 20th century. We show that, similarly to other pathogenic phleboviruses, SFSV suppresses the induction of the antiviral type I interferon (IFN) system in an NSs-dependent manner. SFSV NSs interfered with the TBK1-interferon regulatory factor 3 (IRF3) branch of the RIG-I signaling pathway but not with NF-κB activation. Consistently, we identified IRF3 as a host interactor of SFSV NSs. In contrast to IRF3, neither the IFN master regulator IRF7 nor any of the related transcription factors IRF2, IRF5, and IRF9 were bound by SFSV NSs. In spite of this specificity for IRF3, NSs did not inhibit its phosphorylation, dimerization, or nuclear accumulation, and the interaction was independent of the IRF3 activation or multimerization state. In further studies, we identified the DNA-binding domain of IRF3 (amino acids 1 to 113) as sufficient for NSs binding and found that SFSV NSs prevented the association of activated IRF3 with the IFN-β promoter. Thus, unlike highly virulent phleboviruses, which either destroy antiviral host factors or sequester whole signaling chains into inactive aggregates, SFSV modulates type I IFN induction by directly masking the DNA-binding domain of IRF3. IMPORTANCE Phleboviruses are receiving increased attention due to the constant discovery of new species and the ongoing spread of long-known members of the genus. Outbreaks of sandfly fever were reported in the 19th century, during World War I, and during World War II. Currently, SFSV is recognized as one of the most widespread phleboviruses, exhibiting high seroprevalence rates in humans and domestic animals and causing a self-limiting but incapacitating disease predominantly in immunologically naive troops and travelers. We show how the nonstructural NSs protein of SFSV counteracts the upregulation of the antiviral interferon (IFN) system. SFSV NSs specifically inhibits promoter binding by IFN transcription factor 3 (IRF3), a molecular strategy which is unique among phleboviruses and, to our knowledge, among human pathogenic RNA viruses in general. This IRF3-specific and stoichiometric mechanism, greatly distinct from the ones exhibited by the highly virulent phleboviruses, correlates with the intermediate level of pathogenicity of SFSV.
has issue date	2018-11-12(xsd:dateTime)
bibo:doi	10.1128/jvi.01202-18
bibo:pmid	30232186
has license	cc-by
sha1sum (hex)	d39a4fdb4c67a86c47496bef56c34f732817b4bf
schema:url	https://doi.org/10.1128/jvi.01202-18
resource representing a document's title	NSs Protein of Sandfly Fever Sicilian Phlebovirus Counteracts Interferon (IFN) Induction by Masking the DNA-Binding Domain of IFN Regulatory Factor 3
has PubMed Central identifier	PMC6232482
has PubMed identifier	30232186
schema:publication	J Virol
resource representing a document's body	covid:d39a4fdb4c67a86c47496bef56c34f732817b4bf#body_text
is schema:about of	named entity 'induction' named entity 'DNA-binding domain' named entity 'IFN' named entity 'pathogenicity' named entity 'pathogenic' named entity 'aggregates' covid:arg/d39a4fdb4c67a86c47496bef56c34f732817b4bf named entity 'mechanism' named entity 'activation' named entity 'prevented' named entity 'IFN' named entity 'order' named entity 'type I IFN' named entity 'members' named entity 'masking' named entity 'nuclear' named entity 'IFN' named entity 'IRF3' named entity 'members' named entity 'IFN' named entity 'J Virol' named entity 'identified' named entity 'highly' named entity 'genus' named entity 'infecting' named entity 'activation' named entity 'promoter' named entity 'receiving' named entity 'acute' named entity 'DNA-Binding Domain' named entity 'IRF3' named entity 'IRF3' named entity 'Phlebotomus' named entity 'SFSV' named entity 'SFSV' named entity 'SFSV' named entity 'TBK1' named entity 'phosphorylation' named entity 'protein' named entity 'RNA viruses' named entity 'dimerization' named entity 'RIG-I' named entity 'IRF3' named entity 'interferon regulatory factor 3' named entity 'IRF2' named entity 'SFSV' named entity 'interferon' named entity 'Interferon' named entity 'Phlebovirus' named entity 'IFN' named entity 'signaling pathway' named entity 'plasmid' named entity 'transcription factors' named entity 'proline' named entity 'IFN' named entity 'virulence factors' named entity 'eGFP' named entity 'reverse transcriptase quantitative PCR' named entity 'FCS' named entity 'herpes simplex virus 1' named entity 'antibody' named entity 'dipteran' named entity 'L-alanine' named entity 'MAVS' named entity 'viruses' named entity 'HEK293' named entity 'virus' named entity 'master regulator' named entity 'nucleocapsid protein' named entity 'transcription' named entity 'IFN' named entity 'RVFV' named entity 'PTV' named entity 'IFN' named entity 'nucleus' named entity 'RVFV'

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