Organization of the Influenza Virus Replication Machinery
Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the e...
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| Published in | Science (American Association for the Advancement of Science) Vol. 338; no. 6114; pp. 1631 - 1634 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Washington, DC
American Association for the Advancement of Science
21.12.2012
The American Association for the Advancement of Science |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template. |
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| AbstractList | Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template. Influenza RevealedInfluenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication and transcription, is central to the virus life-cycle and to viral host adaptation (see the Perspective by Tao and Zheng). Structural characterization of the viral RNP has been challenging, but Moeller et al. (p. 1631, published online 22 November) and Arranz et al. (p. 1634, published online 22 November) now report the structure and assembly of this complex, using cryo-electron microscopy and negative-stain electron microscopy. The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP providing insight into mechanisms for influenza genome replication and transcription. Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication and transcription, is central to the virus life-cycle and to viral host adaptation (see the Perspective by Tao and Zheng ). Structural characterization of the viral RNP has been challenging, but Moeller et al. (p. 1631, published online 22 November) and Arranz et al. (p. 1634, published online 22 November) now report the structure and assembly of this complex, using cryo-electron microscopy and negative-stain electron microscopy. The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP providing insight into mechanisms for influenza genome replication and transcription. [PUBLICATION ABSTRACT] Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template. [PUBLICATION ABSTRACT] Influenza Revealed Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication and transcription, is central to the virus life-cycle and to viral host adaptation (see the Perspective by Tao and Zheng). Structural characterization of the viral RNP has been challenging, but Moeller et al. (p. 1631, published online 22 November) and Arranz et al. (p. 1634, published online 22 November) now report the structure and assembly of this complex, using cryo-electron microscopy and negative-stain electron microscopy. The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP providing insight into mechanisms for influenza genome replication and transcription. Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by cryo-electron microscopy. The cryo-EM structure reveals the architecture and organization of the native RNP, thereby defining the attributes of its largely helical structure and how polymerase interacts with NP and the viral genome. Observations of branched-RNP structures in negative stain EM and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template. Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex, which carries out viral replication and transcription, is central to the virus life-cycle and to viral host adaptation (see the Perspective by Tao and Zheng ). Structural characterization of the viral RNP has been challenging, but Moeller et al. (p. 1631 , published online 22 November) and Arranz et al. (p. 1634 , published online 22 November) now report the structure and assembly of this complex, using cryo-electron microscopy and negative-stain electron microscopy. The structures reveal how the viral polymerase, RNA genome, and nucleoprotein interact in the RNP providing insight into mechanisms for influenza genome replication and transcription. Electron microscopic analysis of a reconstituted RNA-protein complex outlines pathways of transcription. Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template. Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template.Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template. |
| Author | Kirchdoerfer, Robert N. Wilson, Ian A. Moeller, Arne Carragher, Bridget Potter, Clinton S. |
| AuthorAffiliation | 2 Department of Molecular Biology La Jolla, California 92037, United States 3 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States 1 National Resource for Automated Molecular Microscopy, Department of Cell Biology, La Jolla, California 92037, United States |
| AuthorAffiliation_xml | – name: 3 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States – name: 1 National Resource for Automated Molecular Microscopy, Department of Cell Biology, La Jolla, California 92037, United States – name: 2 Department of Molecular Biology La Jolla, California 92037, United States |
| Author_xml | – sequence: 1 givenname: Arne surname: Moeller fullname: Moeller, Arne – sequence: 2 givenname: Robert N. surname: Kirchdoerfer fullname: Kirchdoerfer, Robert N. – sequence: 3 givenname: Clinton S. surname: Potter fullname: Potter, Clinton S. – sequence: 4 givenname: Bridget surname: Carragher fullname: Carragher, Bridget – sequence: 5 givenname: Ian A. surname: Wilson fullname: Wilson, Ian A. |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26762274$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/23180774$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | Copyright © 2012 American Association for the Advancement of Science 2014 INIST-CNRS Copyright © 2012, American Association for the Advancement of Science |
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| Issue | 6114 |
| Keywords | Virus Anatomic pathology Ribonucleoprotein Orthomyxoviridae Virus replication cycle Exploration Replication Electron microscopy Influenzavirus |
| Language | English |
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| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this work |
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| Snippet | Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral... Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza ribonucleoprotein (RNP) complex,... Influenza RevealedInfluenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza... Influenza Revealed Influenza virus, a single-stranded RNA virus, is responsible for substantial morbidity and mortality worldwide. The influenza... |
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| SubjectTerms | Active sites Assembly Biological and medical sciences cryo-electron microscopy Cryoelectron Microscopy Crystallography, X-Ray Electron microscopy genome Genome, Viral Genomes Genomics Image Processing, Computer-Assisted Influenza Influenza A virus Influenza A Virus, H1N1 Subtype - chemistry Influenza A Virus, H1N1 Subtype - genetics Influenza A Virus, H1N1 Subtype - physiology Influenza A Virus, H1N1 Subtype - ultrastructure Influenza virus Medical sciences Microscopy Microscopy, Electron Models, Molecular morbidity Mortality Nucleic Acid Conformation Nucleoproteins Online Orthomyxoviridae Pharmacology. Drug treatments Protein Conformation Protein Subunits - chemistry Protein Subunits - metabolism Replication Ribonucleic acids ribonucleoproteins Ribonucleoproteins - chemistry Ribonucleoproteins - genetics Ribonucleoproteins - metabolism Ribonucleoproteins - ultrastructure RNA RNA polymerase RNA Replicase - chemistry RNA Replicase - metabolism RNA Replicase - ultrastructure RNA, Viral - chemistry RNA, Viral - metabolism RNA, Viral - ultrastructure RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism RNA-Binding Proteins - ultrastructure RNA-protein interactions transcription (genetics) Transcription, Genetic Viral Core Proteins - chemistry Viral Core Proteins - metabolism Viral Core Proteins - ultrastructure Viral genomes Viral morphology Viral Proteins - chemistry Viral Proteins - metabolism Viral Proteins - ultrastructure Virions Virology Virus Replication Viruses |
| Title | Organization of the Influenza Virus Replication Machinery |
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