ArticleNature communications2017
Double-stranded RNA virus outer shell assembly by bona fide domain-swapping.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed.
- Temperature-modulated persistent dsRNA phage infection selectively excludes superinfection and promotes generation of new viral variants.Microbiology spectrum · 2026Article
- Nonviral protein cages as tools to decipher and combat viral threats.Npj viruses · 2025Review
- Bacteriophages and their unique components provide limitless resources for exploitation.Frontiers in microbiology · 2024Article
- Bacteriophage Receptor Recognition and Nucleic Acid Transfer.Sub-cellular biochemistry · 2024Review
- Review
- Review
- Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein.Science (New York, N.Y.) · 2021Article
- Article
- Capsid Structure ofJournal of virology · 2021Article
- Review
- Genome organization and interaction with capsid protein in a multipartite RNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Multiple liquid crystalline geometries of highly compacted nucleic acid in a dsRNA virus.Nature · 2019Article
- Microbial production of lipid-protein vesicles using enveloped bacteriophage phi6.Microbial cell factories · 2019Article
- Half a Century of Research on Membrane-Containing Bacteriophages: Bringing New Concepts to Modern Virology.Viruses · 2019Review
- Structures of enveloped virions determined by cryogenic electron microscopy and tomography.Advances in virus research · 2019Article
- Article
- Article
- Mycobacterium tuberculosis CarD, an essential global transcriptional regulator forms amyloid-like fibrils.Scientific reports · 2018Article
- Image processing for cryogenic transmission electron microscopy of symmetry-mismatched complexes.Bioscience reports · 2018Article
- Shielding and activation of a viral membrane fusion protein.Nature communications · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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.
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Registered trials
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