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Three-dimensional analysis of ribonucleoprotein complexes in influenza A virus

Author

Listed:
  • Takeshi Noda

    (International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.)

  • Yukihiko Sugita

    (Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.)

  • Kazuhiro Aoyama

    (FEI Company Japan Ltd, Application Laboratory, Kohnan, Minato-ku
    Special Research Promotion Group (Soft Biosystem Group), Graduate School of Frontier Bioscience, Osaka University, Suita)

  • Ai Hirase

    (Graduate School of life science, University of Hyogo
    Bio-multisome Research Team, RIKEN SPring-8 Center, Harima Institute
    Core Research for Evolutional Science and Technology, Japan Science and Technology Agency)

  • Eiryo Kawakami

    (Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.)

  • Atsuo Miyazawa

    (Graduate School of life science, University of Hyogo
    Bio-multisome Research Team, RIKEN SPring-8 Center, Harima Institute
    Core Research for Evolutional Science and Technology, Japan Science and Technology Agency)

  • Hiroshi Sagara

    (Medical Proteomics Laboratory, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.)

  • Yoshihiro Kawaoka

    (International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
    Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
    ERATO Infection-induced Host Responses Project
    University of Wisconsin-Madison)

Abstract

The influenza A virus genome consists of eight single-stranded negative-sense RNA (vRNA) segments. Although genome segmentation provides advantages such as genetic reassortment, which contributes to the emergence of novel strains with pandemic potential, it complicates the genome packaging of progeny virions. Here we elucidate, using electron tomography, the three-dimensional structure of ribonucleoprotein complexes (RNPs) within progeny virions. Each virion is packed with eight well-organized RNPs that possess rod-like structures of different lengths. Multiple interactions are found among the RNPs. The position of the eight RNPs is not consistent among virions, but a pattern suggests the existence of a specific mechanism for assembly of these RNPs. Analyses of budding progeny virions suggest two independent roles for the viral spike proteins: RNP association on the plasma membrane and the subsequent formation of the virion shell. Our data provide further insights into the mechanisms responsible for segmented-genome packaging into virions.

Suggested Citation

  • Takeshi Noda & Yukihiko Sugita & Kazuhiro Aoyama & Ai Hirase & Eiryo Kawakami & Atsuo Miyazawa & Hiroshi Sagara & Yoshihiro Kawaoka, 2012. "Three-dimensional analysis of ribonucleoprotein complexes in influenza A virus," Nature Communications, Nature, vol. 3(1), pages 1-6, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1647
    DOI: 10.1038/ncomms1647
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    Cited by:

    1. Timothy D Majarian & Robert F Murphy & Seema S Lakdawala, 2019. "Learning the sequence of influenza A genome assembly during viral replication using point process models and fluorescence in situ hybridization," PLOS Computational Biology, Public Library of Science, vol. 15(1), pages 1-20, January.

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