ArticleProceedings of the National Academy of Sciences of the United States of America2014
Capsid expansion mechanism of bacteriophage T7 revealed by multistate atomic models derived from cryo-EM reconstructions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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74 citing papers in PubMed, 111 citations in OpenAlex.
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- 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
- The discovery of aScience advances · 2025Article
- Cryo-EM and cryo-ET reveal the molecular architecture and host interactions of mycobacteriophage Douge.Cell reports · 2025Article
- Atomistic simulations of intact virus capsids: A computational challenge worth the scientific payoff.Current opinion in structural biology · 2025Review
- Stabilization mechanism accommodating genome length variation in evolutionarily related viral capsids.Nature communications · 2025Article
- Structure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.PLoS biology · 2025Article
- Phi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation.Science advances · 2025Article
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- Conformational changes in and translocation of small proteins: insights into the ejection mechanism of podophages.Journal of virology · 2025Article
- Cryo-Electron Microscopy in the Study of Antiviral Innate Immunity.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Single-Particle Cryo-EM to Investigate Nonenveloped Virus-Like Particles.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structure and replication of Pseudomonas aeruginosa phage JBD30.The EMBO journal · 2024Article
- Capsid structure of bacteriophage ΦKZ provides insights into assembly and stabilization of jumbo phages.Nature communications · 2024Article
- Cryo-EM structure of a Shigella podophage reveals a hybrid tail and novel decoration proteins.Structure (London, England : 1993) · 2024Article
- Cryo-EM structure of cyanophage P-SCSP1u offers insights into DNA gating and evolution of T7-like viruses.Nature communications · 2023Article
- Structure and proposed DNA delivery mechanism of a marine roseophage.Nature communications · 2023Article
14 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Many dsDNA viruses first assemble a DNA-free procapsid, using a scaffolding protein-dependent process. The procapsid, then, undergoes dramatic conformational maturation while packaging DNA. For bacteriophage T7 we report the following four single-particle cryo-EM 3D reconstructions and the derived atomic models: procapsid (4.6-Å resolution), an early-stage DNA packaging intermediate (3.5 Å), a later-stage packaging intermediate (6.6 Å), and the final infectious phage (3.6 Å). In the procapsid, the N terminus of the major capsid protein, gp10, has a six-turn helix at the inner surface of the shell, where each skewed hexamer of gp10 interacts with two scaffolding proteins. With the exit of scaffolding proteins during maturation the gp10 N-terminal helix unfolds and swings through the capsid shell to the outer surface. The refolded N-terminal region has a hairpin that forms a novel noncovalent, joint-like, intercapsomeric interaction with a pocket formed during shell expansion. These large conformational changes also result in a new noncovalent, intracapsomeric topological linking. Both interactions further stabilize the capsids by interlocking all pentameric and hexameric capsomeres in both DNA packaging intermediate and phage. Although the final phage shell has nearly identical structure to the shell of the DNA-free intermediate, surprisingly we found that the icosahedral faces of the phage are slightly (∼4 Å) contracted relative to the faces of the intermediate, despite the internal pressure from the densely packaged DNA genome. These structures provide a basis for understanding the capsid maturation process during DNA packaging that is essential for large numbers of dsDNA viruses.
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