ArticleNature communications2017
Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.
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 68 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
68 citing papers in PubMed, 99 citations in OpenAlex.
- Insights into Genome Ejection by a Therapeutic phiKMV-like Bacteriophage.Journal of molecular biology · 2026Article
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Intact architectures of myophage phi92 in extended and contracted states.PLoS pathogens · 2026Article
- A highly conserved basic motif in the wing domain of portal protein is necessary for oligomerization and incorporation in phage P22.Journal of virology · 2026Article
- Structural atlas of Pakpunavirus P7-1 reveals determinants of virion stability and genome ejection.Communications biology · 2026Article
- Genome anchoring, retention, and release by neck proteins of Staphylococcus phage 812.Communications biology · 2026Article
- Zoon0PredV: Potential Virus Species Crossover Prediction Using Convolutional Neural Networks and Viral Protein Sequence Patterns.Bioinformatics and biology insights · 2026Article
- Structural atlas ofbioRxiv : the preprint server for biology · 2025Article
- High-resolution Cryo-EM Analysis of the Therapeutic Pseudomonas Phage Pa223.Journal of molecular biology · 2025Article
- Structure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.PLoS biology · 2025Article
- Variable Assembly and Procapsid Binding of Bacteriophage P22 Terminase Subunits in Solution.Pathogens (Basel, Switzerland) · 2024Article
- DNA packaging by molecular motors: from bacteriophage to human chromosomes.Nature reviews. Genetics · 2024Review
- Integrative structural analysis of Pseudomonas phage DEV reveals a genome ejection motor.Nature communications · 2024Article
- Construction and Characterization of a High-Capacity Replication-Competent Murine Cytomegalovirus Vector for Gene Delivery.Vaccines · 2024Article
- Structural morphing in the viral portal vertex of bacteriophage lambda.Journal of virology · 2024Article
- Integrative structural analysis ofResearch square · 2024Article
- Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation.Journal of molecular biology · 2024Article
- Cryo-EM structure of a Shigella podophage reveals a hybrid tail and novel decoration proteins.Structure (London, England : 1993) · 2024Article
- Bacteriophage LDT325 enhancesFrontiers in microbiology · 2024Article
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or 'procapsid') built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrangement of the coat protein and release of scaffolding protein, resulting in dramatic procapsid lattice expansion. Here, we provide structural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric conformations: an asymmetric assembly in the procapsid (PC-portal) that is competent for high affinity binding to the large terminase packaging protein, and a symmetric ring in the mature virion (MV-portal) that has negligible affinity for the packaging motor. Modelling studies indicate the structure of PC-portal is incompatible with DNA coaxially spooled around the portal vertex, suggesting that newly packaged DNA triggers the switch from PC- to MV-conformation. Thus, we propose the signal for termination of 'Headful Packaging' is a DNA-dependent symmetrization of portal protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.