ArticleViruses2023
Assembly and Capsid Expansion Mechanism of Bacteriophage P22 Revealed by High-Resolution Cryo-EM Structures.
Article in Viruses, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Review
- Structure of defense against restriction proteins DarA and Hdf in phage P1 reveals a new molecular mechanism during phage assembly, infection and DNA ejection.PLoS pathogens · 2026Article
- Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid.Nature communications · 2025Article
- Elucidating double stranded DNA viral scaffolding protein structures through advances in cryogenic electron microscopy data processing.Current opinion in structural biology · 2025Review
- Exploring Use of a Protein Cage System for Producing Bioactive Peptides in Escherichia coli.Microbial biotechnology · 2025Article
- Article
- Structure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.PLoS biology · 2025Article
- Cryo-EM analysis of Pseudomonas phage Pa193 structural components.Communications biology · 2024Article
- The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMRMolecules (Basel, Switzerland) · 2024Article
- Predictive modeling and cryo-EM: A synergistic approach to modeling macromolecular structure.Biophysical journal · 2024Review
- Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers.Nature communications · 2023Article
- A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.Science advances · 2023Article
- Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of many double-stranded DNA viruses, such as herpesviruses and bacteriophages, begins with the scaffolding-protein-mediated assembly of the procapsid. Subsequently, the procapsid undergoes extensive structural rearrangement and expansion to become the mature capsid. Bacteriophage P22 is an established model system used to study virus maturation. Here, we report the cryo-electron microscopy structures of procapsid, empty procapsid, empty mature capsid, and mature capsid of phage P22 at resolutions of 2.6 Å, 3.9 Å, 2.8 Å, and 3.0 Å, respectively. The structure of the procapsid allowed us to build an accurate model of the coat protein gp5 and the C-terminal region of the scaffolding protein gp8. In addition, interactions among the gp5 subunits responsible for procapsid assembly and stabilization were identified. Two C-terminal α-helices of gp8 were observed to interact with the coat protein in the procapsid. The amino acid interactions between gp5 and gp8 in the procapsid were consistent with the results of previous biochemical studies involving mutant proteins. Our structures reveal hydrogen bonds and salt bridges between the gp5 subunits in the procapsid and the conformational changes of the gp5 domains involved in the closure of the local sixfold opening and a thinner capsid shell during capsid maturation.
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