Suppression of the antiviral response by an influenza histone mimic

Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of in...

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Published in	Nature (London) Vol. 483; no. 7390; pp. 428 - 433
Main Authors	Marazzi, Ivan, Ho, Jessica S. Y., Kim, Jaehoon, Manicassamy, Balaji, Dewell, Scott, Albrecht, Randy A., Seibert, Chris W., Schaefer, Uwe, Jeffrey, Kate L., Prinjha, Rab K., Lee, Kevin, García-Sastre, Adolfo, Roeder, Robert G., Tarakhovsky, Alexander
Format	Journal Article
Language	English
Published	London Nature Publishing Group UK 22.03.2012 Nature Publishing Group
Subjects	631/250/2499 631/326/596 692/699/255/1578 Amino Acid Sequence Amino acids Biological and medical sciences Epigenetics Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation - immunology Genomes Histones - chemistry Histones - metabolism Humanities and Social Sciences Humans Influenza Influenza A Virus, H3N2 Subtype - genetics Influenza A Virus, H3N2 Subtype - metabolism Influenza A Virus, H3N2 Subtype - pathogenicity Influenza virus Influenza, Human - genetics Influenza, Human - immunology Influenza, Human - pathology Influenza, Human - virology Microbiology Molecular Mimicry Molecular Sequence Data multidisciplinary Nuclear Proteins - antagonists & inhibitors Nuclear Proteins - metabolism Peptides Protein Binding Proteins Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Science Science (multidisciplinary) Transcription, Genetic - immunology Viral Nonstructural Proteins - chemistry Viral Nonstructural Proteins - metabolism Virology Virus Deoxyribonucleoproteins Basic protein Orthomyxoviridae Antiviral Host agent relation Histone Influenzavirus Nuclear protein
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Abstract	Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by the virus to target the human PAF1 transcription elongation complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C depends on the NS1 histone mimic and results in suppression of hPAF1C-mediated transcriptional elongation. Furthermore, human PAF1 has a crucial role in the antiviral response. Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. We propose that the histone mimic in NS1 enables the influenza virus to affect inducible gene expression selectively, thus contributing to suppression of the antiviral response. The H3N2 influenza virus immunomodulatory protein NS1 carries a sequence that mimics the histone H3 tail; this sequence interferes with the host antiviral response via binding to the cellular regulator of RNA elongation, hPAF1C. Flu-virus mimicry Histone proteins are essential regulators of gene function. The amino-terminal domain of the histone H2, or the histone 'tail', can be post-translationally modified, and it acts as a scaffold for the assembly of protein complexes that control gene function. Ivan Marazzi and colleagues now show that the immunosuppressive NS1 protein of the influenza virus carries a histone-like sequence that mimics key features of histone H3, including binding to key transcriptional regulators, so that the virus can hijack the host transcriptional machinery. Interaction between NS1 and transcriptional elongation complex PAF1C is shown to be crucial to the host antiviral response, validating PAF1 protein as a candidate for anti-inflammatory therapy using synthetic PAF1 antagonists.
AbstractList	Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by the virus to target the human PAF1 transcription elongation complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C depends on the NS1 histone mimic and results in suppression of hPAF1C-mediated transcriptional elongation. Furthermore, human PAF1 has a crucial role in the antiviral response. Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. We propose that the histone mimic in NS1 enables the influenza virus to affect inducible gene expression selectively, thus contributing to suppression of the antiviral response. [PUBLICATION ABSTRACT] Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by the virus to target the human PAF1 transcription elongation complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C depends on the NS1 histone mimic and results in suppression of hPAF1C-mediated transcriptional elongation. Furthermore, human PAF1 has a crucial role in the antiviral response. Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. We propose that the histone mimic in NS1 enables the influenza virus to affect inducible gene expression selectively, thus contributing to suppression of the antiviral response. The H3N2 influenza virus immunomodulatory protein NS1 carries a sequence that mimics the histone H3 tail; this sequence interferes with the host antiviral response via binding to the cellular regulator of RNA elongation, hPAF1C. Flu-virus mimicry Histone proteins are essential regulators of gene function. The amino-terminal domain of the histone H2, or the histone 'tail', can be post-translationally modified, and it acts as a scaffold for the assembly of protein complexes that control gene function. Ivan Marazzi and colleagues now show that the immunosuppressive NS1 protein of the influenza virus carries a histone-like sequence that mimics key features of histone H3, including binding to key transcriptional regulators, so that the virus can hijack the host transcriptional machinery. Interaction between NS1 and transcriptional elongation complex PAF1C is shown to be crucial to the host antiviral response, validating PAF1 protein as a candidate for anti-inflammatory therapy using synthetic PAF1 antagonists. Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by the virus to target the human PAF1 transcription elongation complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C depends on the NS1 histone mimic and results in suppression of hPAF1C-mediated transcriptional elongation. Furthermore, human PAF1 has a crucial role in the antiviral response. Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. We propose that the histone mimic in NS1 enables the influenza virus to affect inducible gene expression selectively, thus contributing to suppression of the antiviral response.Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by the virus to target the human PAF1 transcription elongation complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C depends on the NS1 histone mimic and results in suppression of hPAF1C-mediated transcriptional elongation. Furthermore, human PAF1 has a crucial role in the antiviral response. Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. We propose that the histone mimic in NS1 enables the influenza virus to affect inducible gene expression selectively, thus contributing to suppression of the antiviral response. Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host cells through the interaction of influenza non-structural protein 1 (NS1) with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by the virus to target the human PAF1 transcription elongation complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C depends on the NS1 histone mimic and results in suppression of hPAF1C-mediated transcriptional elongation. Furthermore, human PAF1 has a crucial role in the antiviral response. Loss of hPAF1C binding by NS1 attenuates influenza infection, whereas hPAF1C deficiency reduces antiviral gene expression and renders cells more susceptible to viruses. We propose that the histone mimic in NS1 enables the influenza virus to affect inducible gene expression selectively, thus contributing to suppression of the antiviral response.
Author	Lee, Kevin García-Sastre, Adolfo Ho, Jessica S. Y. Albrecht, Randy A. Schaefer, Uwe Roeder, Robert G. Tarakhovsky, Alexander Dewell, Scott Manicassamy, Balaji Prinjha, Rab K. Kim, Jaehoon Seibert, Chris W. Marazzi, Ivan Jeffrey, Kate L.
AuthorAffiliation	3 Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA 4 Global Health and Infectious Pathogens Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA 6 Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre, Gunnels Wood Road, Stevenage SG1 2NY, UK 7 Department of Medicine, Division of Infectious Diseases, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA 1 Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA 2 Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA 5 Genomics Resource Center, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
AuthorAffiliation_xml	– name: 4 Global Health and Infectious Pathogens Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – name: 3 Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – name: 5 Genomics Resource Center, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – name: 7 Department of Medicine, Division of Infectious Diseases, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – name: 1 Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – name: 6 Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre, Gunnels Wood Road, Stevenage SG1 2NY, UK – name: 2 Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
Author_xml	– sequence: 1 givenname: Ivan surname: Marazzi fullname: Marazzi, Ivan email: imarazzi@rockefeller.edu organization: Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 2 givenname: Jessica S. Y. surname: Ho fullname: Ho, Jessica S. Y. organization: Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 3 givenname: Jaehoon surname: Kim fullname: Kim, Jaehoon organization: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 4 givenname: Balaji surname: Manicassamy fullname: Manicassamy, Balaji organization: Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA, Global Health and Infectious Pathogens Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – sequence: 5 givenname: Scott surname: Dewell fullname: Dewell, Scott organization: Genomics Resource Center, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 6 givenname: Randy A. surname: Albrecht fullname: Albrecht, Randy A. organization: Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA, Global Health and Infectious Pathogens Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – sequence: 7 givenname: Chris W. surname: Seibert fullname: Seibert, Chris W. organization: Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – sequence: 8 givenname: Uwe surname: Schaefer fullname: Schaefer, Uwe organization: Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 9 givenname: Kate L. surname: Jeffrey fullname: Jeffrey, Kate L. organization: Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 10 givenname: Rab K. surname: Prinjha fullname: Prinjha, Rab K. organization: Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre, Gunnels Wood Road, Stevenage SG1 2NY, UK – sequence: 11 givenname: Kevin surname: Lee fullname: Lee, Kevin organization: Epinova DPU, Immuno-Inflammation Centre of Excellence for Drug Discovery, GlaxoSmithKline, Medicines Research Centre, Gunnels Wood Road, Stevenage SG1 2NY, UK – sequence: 12 givenname: Adolfo surname: García-Sastre fullname: García-Sastre, Adolfo organization: Department of Microbiology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA, Global Health and Infectious Pathogens Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA, Department of Medicine, Division of Infectious Diseases, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1124, New York, New York 10029, USA – sequence: 13 givenname: Robert G. surname: Roeder fullname: Roeder, Robert G. organization: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA – sequence: 14 givenname: Alexander surname: Tarakhovsky fullname: Tarakhovsky, Alexander email: tarakho@rockefeller.edu organization: Laboratory of Immune Cell Epigenetics and Signaling, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
BackLink	http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25618834$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/22419161$$D View this record in MEDLINE/PubMed
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Snippet	Viral infection is commonly associated with virus-driven hijacking of host proteins. Here we describe a novel mechanism by which influenza virus affects host...
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SubjectTerms	631/250/2499 631/326/596 692/699/255/1578 Amino Acid Sequence Amino acids Biological and medical sciences Epigenetics Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation - immunology Genomes Histones - chemistry Histones - metabolism Humanities and Social Sciences Humans Influenza Influenza A Virus, H3N2 Subtype - genetics Influenza A Virus, H3N2 Subtype - metabolism Influenza A Virus, H3N2 Subtype - pathogenicity Influenza virus Influenza, Human - genetics Influenza, Human - immunology Influenza, Human - pathology Influenza, Human - virology Microbiology Molecular Mimicry Molecular Sequence Data multidisciplinary Nuclear Proteins - antagonists & inhibitors Nuclear Proteins - metabolism Peptides Protein Binding Proteins Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Science Science (multidisciplinary) Transcription, Genetic - immunology Viral Nonstructural Proteins - chemistry Viral Nonstructural Proteins - metabolism Virology
Title	Suppression of the antiviral response by an influenza histone mimic
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