title: Novel Bat Influenza Virus NS1 Proteins Bind Double-Stranded RNA and Antagonize Host Innate Immunity.
abstract: We demonstrate that novel bat HL17NL10 and HL18NL11 influenza virus NS1 proteins are effective interferon antagonists but do not block general host gene expression. Solving the RNA-binding domain structures revealed the canonical NS1 symmetrical homodimer, and RNA binding required conserved basic residues in this domain. Interferon antagonism was strictly dependent on RNA binding, and chimeric bat influenza viruses expressing NS1s defective in this activity were highly attenuated in interferon-competent cells but not in cells unable to establish antiviral immunity.
authors.affiliation: Institute of Medical Virology, University of Zurich, Zurich, Switzerland.
authors.forename: Hannah L
authors.initials: HL
authors.lastname: Turkington
authors.affiliation: Institute of Virology, Center for Microbiology and Hygiene, University Medical Center Freiburg, Freiburg, Germany.
authors.forename: Mindaugas
authors.initials: M
authors.lastname: Juozapaitis
authors.affiliation: Biomedical Sciences Research Complex, University of St. Andrews, St. Andrews, Fife, United Kingdom.
authors.forename: Philip S
authors.initials: PS
authors.lastname: Kerry
authors.affiliation: Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Teresa
authors.initials: T
authors.lastname: Aydillo
authors.affiliation: Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Juan
authors.initials: J
authors.lastname: Ayllon
authors.affiliation: Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA Department of Medicine, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, New York, USA Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Adolfo
authors.initials: A
authors.lastname: García-Sastre
authors.affiliation: Institute of Virology, Center for Microbiology and Hygiene, University Medical Center Freiburg, Freiburg, Germany martin.schwemmle@uniklinik-freiburg.de hale.ben@virology.uzh.ch.
authors.forename: Martin
authors.initials: M
authors.lastname: Schwemmle
authors.affiliation: Institute of Medical Virology, University of Zurich, Zurich, Switzerland martin.schwemmle@uniklinik-freiburg.de hale.ben@virology.uzh.ch.
authors.forename: Benjamin G
authors.identifier: http://orcid.org/0000-0002-3891-9480
authors.initials: BG
authors.lastname: Hale
mesh_terms: D000818:Animals; D002685:Chiroptera / Q000821:virology*; D005786:Gene Expression Regulation; D054884:Host-Pathogen Interactions; D007113:Immunity, Innate; D009980:Influenza A virus / Q000235:genetics* / Q000276:immunology; D016899:Interferon-beta / Q000235:genetics / Q000276:immunology; D008958:Models, Molecular; D009976:Orthomyxoviridae Infections / Q000235:genetics / Q000276:immunology / Q000662:veterinary* / Q000821:virology; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012330:RNA, Double-Stranded / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D015398:Signal Transduction; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D014779:Virus Replication
chemical_list: C085820:INS1 protein, influenza virus; D020033:Protein Isoforms; D012330:RNA, Double-Stranded; D016601:RNA-Binding Proteins; D017361:Viral Nonstructural Proteins; D016899:Interferon-beta