Double-stranded RNA virus outer shell assembly by bona fide domain-swapping
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 s...
| Váldodahkkit: | , , , , , , , |
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| Materiálatiipa: | Journal article |
| Giella: | English |
| Almmustuhtton: |
Springer Nature
2017
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| _version_ | 1826279079503986688 |
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| author | Sun, Z El Omari, K Sun, X Ilca, S Kotecha, A Stuart, D Poranen, M Huiskonen, J |
| author_facet | Sun, Z El Omari, K Sun, X Ilca, S Kotecha, A Stuart, D Poranen, M Huiskonen, J |
| author_sort | Sun, Z |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T23:53:28Z |
| format | Journal article |
| id | oxford-uuid:736a6d08-1a0c-4d1b-adc0-05cbd0384fc6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:53:28Z |
| publishDate | 2017 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:736a6d08-1a0c-4d1b-adc0-05cbd0384fc62022-03-26T19:56:14ZDouble-stranded RNA virus outer shell assembly by bona fide domain-swappingJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:736a6d08-1a0c-4d1b-adc0-05cbd0384fc6EnglishSymplectic Elements at OxfordSpringer Nature2017Sun, ZEl Omari, KSun, XIlca, SKotecha, AStuart, DPoranen, MHuiskonen, JCorrect 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. |
| spellingShingle | Sun, Z El Omari, K Sun, X Ilca, S Kotecha, A Stuart, D Poranen, M Huiskonen, J Double-stranded RNA virus outer shell assembly by bona fide domain-swapping |
| title | Double-stranded RNA virus outer shell assembly by bona fide domain-swapping |
| title_full | Double-stranded RNA virus outer shell assembly by bona fide domain-swapping |
| title_fullStr | Double-stranded RNA virus outer shell assembly by bona fide domain-swapping |
| title_full_unstemmed | Double-stranded RNA virus outer shell assembly by bona fide domain-swapping |
| title_short | Double-stranded RNA virus outer shell assembly by bona fide domain-swapping |
| title_sort | double stranded rna virus outer shell assembly by bona fide domain swapping |
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