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

نویسندگان

  • Zhaoyang Sun
  • Kamel El Omari
  • Xiaoyu Sun
  • Serban L Ilca
  • Abhay Kotecha
  • David I Stuart
  • Minna M Poranen
  • Juha T Huiskonen
چکیده

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.

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عنوان ژورنال:

دوره 8  شماره 

صفحات  -

تاریخ انتشار 2017