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

Zhaoyang Sun, Kamel El Omari, Xiaoyu Sun, Serban L. Ilca, Abhay Kotecha, David I. Stuart, Minna M. Poranen () and Juha T. Huiskonen ()
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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

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms14814

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