ArticleBiomacromolecules2013
Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials.
Article in Biomacromolecules, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 42 citations in OpenAlex.
- Review
- A pH-Responsive Virus-Like Particle as a Protein Cage for a Targeted Delivery.Advanced healthcare materials · 2024Article
- Cell-penetrating peptides TAT and 8R functionalize P22 virus-like particles to enhance tissue distribution and retentionFrontiers in veterinary science · 2024Article
- Review
- Conformational behavior of coat protein in plants and association with coat protein-mediated resistance against TMV.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Article
- Protein cage assembly across multiple length scales.Chemical Society reviews · 2018Review
- Article
- Article
- Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22 Virus-like Particle.Bioconjugate chemistry · 2017Article
- Virus-like particles: Next-generation nanoparticles for targeted therapeutic delivery.Bioengineering & translational medicine · 2017Review
- Display of whole proteins on inner and outer surfaces of grapevine fanleaf virus-like particles.Plant biotechnology journal · 2016Article
- Engineering virus-like particles as vaccine platforms.Current opinion in virology · 2016Review
- Symmetry Controlled, Genetic Presentation of Bioactive Proteins on the P22 Virus-like Particle Using an External Decoration Protein.ACS nano · 2015Article
- Bacteriophage lambda: Early pioneer and still relevant.Virology · 2015Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Rational design of modifications to the interior and exterior surfaces of virus-like particles (VLPs) for future therapeutic and materials applications is based on structural information about the capsid. Existing cryo-electron microscopy-based models suggest that the C-terminus of the bacteriophage P22 coat protein (CP) extends toward the capsid exterior. Our biochemical analysis through genetic manipulations of the C-terminus supports the model where the CP C-terminus is exposed on the exterior of the P22 capsid. Capsids displaying a 6xHis tag appended to the CP C-terminus bind to a Ni affinity column, and the addition of positively or negatively charged coiled coil peptides to the capsid results in association of these capsids upon mixing. Additionally, a single cysteine appended to the CP C-terminus results in the formation of intercapsid disulfide bonds and can serve as a site for chemical modifications. Thus, the C-terminus is a powerful location for multivalent display of peptides that facilitate nanoscale assembly and capsid modification.
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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.