ArticleJournal of structural biology2012
Structure and size determination of bacteriophage P2 and P4 procapsids: function of size responsiveness mutations.
Article in Journal of structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 32 citations in OpenAlex.
- Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.Science advances · 2025Article
- High-yield bioproduction of virus-free virus-like P4-EKORhE multi-lysin transducing particles as an antimicrobial gene therapeutic.Frontiers in cellular and infection microbiology · 2025Article
- Architecture and Assembly of Structurally Complex Viruses.Sub-cellular biochemistry · 2024Review
- Predicting the capsid architecture of phages from metagenomic data.Computational and structural biotechnology journal · 2022Article
- High Resolution Structure of the Mature Capsid ofInternational journal of molecular sciences · 2021Article
- Bacteriophage Technology and Modern Medicine.Antibiotics (Basel, Switzerland) · 2021Review
- The Missing Tailed Phages: Prediction of Small Capsid Candidates.Microorganisms · 2020Article
- Article
- Molecular Piracy: Redirection of Bacteriophage Capsid Assembly by Mobile Genetic Elements.Viruses · 2019Review
- Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80α and SaPI1 Capsids.Viruses · 2017Article
- Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.Journal of molecular biology · 2017Article
- Convergent evolution of pathogenicity islands in helper cos phage interference.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Cryo-electron microscopy structure of lactococcal siphophage 1358 virion.Journal of virology · 2014Article
- Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly.Journal of molecular biology · 2014Article
- Subunit folds and maturation pathway of a dsRNA virus capsid.Structure (London, England : 1993) · 2013Article
- The adaptation of temperate bacteriophages to their host genomes.Molecular biology and evolution · 2013Article
- Insights into head-tailed viruses infecting extremely halophilic archaea.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Bacteriophage P4 is dependent on structural proteins supplied by a helper phage, P2, to assemble infectious virions. Bacteriophage P2 normally forms an icosahedral capsid with T=7 symmetry from the gpN capsid protein, the gpO scaffolding protein and the gpQ portal protein. In the presence of P4, however, the same structural proteins are assembled into a smaller capsid with T=4 symmetry. This size determination is effected by the P4-encoded protein Sid, which forms an external scaffold around the small P4 procapsids. Size responsiveness (sir) mutants in gpN fail to assemble small capsids even in the presence of Sid. We have produced large and small procapsids by co-expression of gpN with gpO and Sid, respectively, and applied cryo-electron microscopy and three-dimensional reconstruction methods to visualize these procapsids. gpN has an HK97-like fold and interacts with Sid in an exposed loop where the sir mutations are clustered. The T=7 lattice of P2 has dextro handedness, unlike the laevo lattices of other phages with this fold observed so far.
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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.