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Double-stranded RNA virus outer shell assembly by bona fide domain-swapping

Author

Listed:
  • Zhaoyang Sun

    (Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Kamel El Omari

    (Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Xiaoyu Sun

    (University of Helsinki)

  • Serban L. Ilca

    (Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Abhay Kotecha

    (Wellcome Trust Centre for Human Genetics, University of Oxford)

  • David I. Stuart

    (Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Minna M. Poranen

    (University of Helsinki)

  • Juha T. Huiskonen

    (Wellcome Trust Centre for Human Genetics, University of Oxford
    University of Helsinki)

Abstract

Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage φ6, the assembly reaction is promoted by calcium ions but its biomechanics remain poorly understood. Here, we describe the near-atomic resolution structure of the φ6 double-shelled particle. The outer T=13 shell protein P8 consists of two alpha-helical domains joined by a linker, which allows the trimer to adopt either a closed or an open conformation. The trimers in an open conformation swap domains with each other. Our observations allow us to propose a mechanistic model for calcium concentration regulated outer shell assembly. Furthermore, the structure provides a prime exemplar of bona fide domain-swapping. This leads us to extend the theory of domain-swapping from the level of monomeric subunits and multimers to closed spherical shells, and to hypothesize a mechanism by which closed protein shells may arise in evolution.

Suggested Citation

  • Zhaoyang Sun & Kamel El Omari & Xiaoyu Sun & Serban L. Ilca & Abhay Kotecha & David I. Stuart & Minna M. Poranen & Juha T. Huiskonen, 2017. "Double-stranded RNA virus outer shell assembly by bona fide domain-swapping," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14814
    DOI: 10.1038/ncomms14814
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