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Asymmetric cryo-EM reconstruction of phage MS2 reveals genome structure in situ

Author

Listed:
  • Roman I Koning

    (Leiden University Medical Center
    Netherlands Centre for Electron Nanoscopy, Institute of Biology Leiden, Leiden University)

  • Josue Gomez-Blanco

    (Biocomputing Unit, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC))

  • Inara Akopjana

    (Biomedical Research and Study Centre)

  • Javier Vargas

    (Biocomputing Unit, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC))

  • Andris Kazaks

    (Biomedical Research and Study Centre)

  • Kaspars Tars

    (Biomedical Research and Study Centre)

  • José María Carazo

    (Biocomputing Unit, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC))

  • Abraham J. Koster

    (Leiden University Medical Center
    Netherlands Centre for Electron Nanoscopy, Institute of Biology Leiden, Leiden University)

Abstract

In single-stranded ribonucleic acid (RNA) viruses, virus capsid assembly and genome packaging are intertwined processes. Using cryo-electron microscopy and single particle analysis we determined the asymmetric virion structure of bacteriophage MS2, which includes 178 copies of the coat protein, a single copy of the A-protein and the RNA genome. This reveals that in situ, the viral RNA genome can adopt a defined conformation. The RNA forms a branched network of stem-loops that almost all allocate near the capsid inner surface, while predominantly binding to coat protein dimers that are located in one-half of the capsid. This suggests that genomic RNA is highly involved in genome packaging and virion assembly.

Suggested Citation

  • Roman I Koning & Josue Gomez-Blanco & Inara Akopjana & Javier Vargas & Andris Kazaks & Kaspars Tars & José María Carazo & Abraham J. Koster, 2016. "Asymmetric cryo-EM reconstruction of phage MS2 reveals genome structure in situ," Nature Communications, Nature, vol. 7(1), pages 1-6, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12524
    DOI: 10.1038/ncomms12524
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    Cited by:

    1. Ran Meng & Zhongliang Xing & Jeng-Yih Chang & Zihao Yu & Jirapat Thongchol & Wen Xiao & Yuhang Wang & Karthik Chamakura & Zhiqi Zeng & Fengbin Wang & Ry Young & Lanying Zeng & Junjie Zhang, 2024. "Structural basis of Acinetobacter type IV pili targeting by an RNA virus," Nature Communications, Nature, vol. 15(1), pages 1-9, December.

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