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Editor, Senior Moderator
Science DOI: 10.1126/science.1227270
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Organization of the Influenza Virus Replication Machinery
Arne Moeller1,*,
Robert N. Kirchdoerfer2,*,
Clinton S. Potter1,
Bridget Carragher1,?,
Ian A. Wilson2,3,?
+ Author Affiliations
1National Resource for Automated Molecular Microscopy, Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
2Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
3The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
↵?To whom correspondence should be addressed. E-mail: bcarr@scripps.edu (B.C.); wilson@scripps.edu (I.A.W.)
↵* These authors contributed equally to this work.
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 cryo-EM. 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.
http://www.sciencemag.org/content/early/2012/11/20/science.1227270
Report
Organization of the Influenza Virus Replication Machinery
Arne Moeller1,*,
Robert N. Kirchdoerfer2,*,
Clinton S. Potter1,
Bridget Carragher1,?,
Ian A. Wilson2,3,?
+ Author Affiliations
1National Resource for Automated Molecular Microscopy, Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
2Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
3The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
↵?To whom correspondence should be addressed. E-mail: bcarr@scripps.edu (B.C.); wilson@scripps.edu (I.A.W.)
↵* These authors contributed equally to this work.
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 cryo-EM. 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.
http://www.sciencemag.org/content/early/2012/11/20/science.1227270