ArticleACS nano2015
Symmetry Controlled, Genetic Presentation of Bioactive Proteins on the P22 Virus-like Particle Using an External Decoration Protein.
Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 76 citations in OpenAlex.
- Review
- Reversible Assembly of Virus-Like Particles (VLPs) into Higher-Order Structures Controlled by Oxidation and Reduction of Linker Protein.ACS applied bio materials · 2026Article
- Templated trimerization of the phage L decoration protein on capsids.Protein science : a publication of the Protein Society · 2025Article
- Templated trimerization of the phage L decoration protein on capsids.bioRxiv : the preprint server for biology · 2024Article
- A supramolecular system mimicking the infection process of an enveloped virus through membrane fusion.Scientific reports · 2023Article
- Review
- Assembly of Protein Cages for Drug Delivery.Pharmaceutics · 2022Review
- A Designer Nanoparticle Platform for Controlled Intracellular Delivery of Bioactive Macromolecules: Inhibition of Ubiquitin-Specific Protease 7 in Breast Cancer Cells.ACS chemical biology · 2022Article
- Phage-like particle vaccines are highly immunogenic and protect against pathogenic coronavirus infection and disease.NPJ vaccines · 2022Article
- Embedding a membrane protein into an enveloped artificial viral replica.RSC chemical biology · 2022Article
- Nano-Particulate Platforms for Vaccine Delivery to Enhance Antigen-Specific CD8Methods in molecular biology (Clifton, N.J.) · 2022Article
- Controlled Modular Multivalent Presentation of the CD40 Ligand on P22 Virus-like Particles Leads to Tunable Amplification of CD40 Signaling.ACS applied bio materials · 2021Article
- Protein engineering strategies for rational immunogen design.NPJ vaccines · 2021Review
- Substrate Partitioning into Protein Macromolecular Frameworks for Enhanced Catalytic Turnover.ACS nano · 2021Article
- Recent progress in targeted delivery vectors based on biomimetic nanoparticles.Signal transduction and targeted therapy · 2021Review
- Polymer Coatings on Virus-like Particle Nanoreactors at Low Ionic Strength-Charge Reversal and Substrate Access.Biomacromolecules · 2021Article
- Multifunctional biomolecule nanostructures for cancer therapy.Nature reviews. Materials · 2021Review
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- Developing Protein-Based Nanoparticles as Versatile Delivery Systems for Cancer Therapy and Imaging.Nanomaterials (Basel, Switzerland) · 2019Review
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Viruses use spatial control of constituent proteins as a means of manipulating and evading host immune systems. Similarly, precise spatial control of proteins encapsulated or presented on designed nanoparticles has the potential to biomimetically amplify or shield biological interactions. Previously, we have shown the ability to encapsulate a wide range of guest proteins within the virus-like particle (VLP) from Salmonella typhimurium bacteriophage P22, including antigenic proteins from human pathogens such as influenza. Expanding on this robust encapsulation strategy, we have used the trimeric decoration protein (Dec) from bacteriophage L as a means of controlled exterior presentation on the mature P22 VLP, to which it binds with high affinity. Through genetic fusion to the C-terminus of the Dec protein, either the 17 kDa soluble region of murine CD40L or a minimal peptide designed from the binding region of the "self-marker" CD47 was independently presented on the P22 VLP capsid exterior. Both candidates retained function when presented as a Dec-fusion. Binding of the Dec domain to the P22 capsid was minimally changed across designed constructs, as measured by surface plasmon resonance, demonstrating the broad utility of this presentation strategy. Dec-mediated presentation offers a robust, modular means of decorating the exposed exterior of the P22 capsid in order to further orchestrate responses to internally functionalized VLPs within biological systems.
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What OpenQuestion holds
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.