ArticlePloS one2010
Versatile virus-like particle carrier for epitope based vaccines.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 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.
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Who cites it
97 citing papers in PubMed, 200 citations in OpenAlex.
- Virus-like Particles Derived from Bacteriophage Beihai32 as a Versatile Carrier for Displaying Large Peptide Antigens.Nanomaterials (Basel, Switzerland) · 2026Article
- Protocol for high-density peptide and protein presentation on biomaterial surfaces using virus-like particles.STAR protocols · 2026Article
- Identification of efficient multi-epitope combinations against African swine fever virus based on AP205 scaffold-mediated nanodisplay technology.Journal of nanobiotechnology · 2026Article
- Application and Research Progress of Self-Assembling Protein Nanoparticles in Vaccine Development.International journal of molecular sciences · 2026Review
- Review
- Advances and future applications of immunocastration techniques: a comprehensive review.NPJ vaccines · 2026Review
- Nanoparticle-Based Antigen Delivery: Advancing Immunization Strategies against Infectious Pathogens.Biomaterials research · 2026Review
- A Plasmodium-derived nanoparticle vaccine elicits sterile protection against malaria in mice.Nature microbiology · 2026Article
- Protein nanocages: A new frontier in mucosal vaccine delivery and immune activation.Human vaccines & immunotherapeutics · 2025Review
- Article
- Virus-like Particles Formed by the Coat Protein of the Single-Stranded RNA Phage PQ465 as a Carrier for Antigen Presentation.Molecules (Basel, Switzerland) · 2025Article
- Targeted Lymph Node Immunization with Serotype-Specific Dengue VLP Vaccines Enhances Antibody Avidity and Specificity.Vaccines · 2025Article
- Colloidal Crystallization of Virus-Like Particles with Polycations.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- EngineeringVaccines · 2024Review
- Article
- Influenza A Vaccine Candidates Based on Virus-like Particles Formed by Coat Proteins of Single-Stranded RNA Phages Beihai32 and PQ465.Vaccines · 2024Article
- Preclinical Evaluation of Novel Sterically Optimized VLP-Based Vaccines against All Four DENV Serotypes.Vaccines · 2024Article
- Article
- Surface Cross-Linking by Macromolecular Tethers Enhances Virus-like Particles' Resilience to Mucosal Stress Factors.ACS nano · 2024Article
- Advances in virus-like particle-based SARS-CoV-2 vaccines.Frontiers in cellular and infection microbiology · 2024Review
37 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
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundRecombinant proteins and in particular single domains or peptides are often poorly immunogenic unless conjugated to a carrier protein. Virus-like-particles are a very efficient means to confer high immunogenicity to antigens. We report here the development of virus-like-particles (VLPs) derived from the RNA bacteriophage AP205 for epitope-based vaccines. METHODOLOGY/PRINCIPAL
findingsPeptides of angiotensin II, S.typhi outer membrane protein (D2), CXCR4 receptor, HIV1 Nef, gonadotropin releasing hormone (GnRH), Influenza A M2-protein were fused to either N- or C-terminus of AP205 coat protein. The A205-peptide fusions assembled into VLPs, and peptides displayed on the VLP were highly immunogenic in mice. GnRH fused to the C-terminus of AP205 induced a strong antibody response that inhibited GnRH function in vivo. Exposure of the M2-protein peptide at the N-terminus of AP205 resulted in a strong M2-specific antibody response upon immunization, protecting 100% of mice from a lethal influenza infection. CONCLUSIONS/SIGNIFICANCE: AP205 VLPs are therefore a very efficient and new vaccine system, suitable for complex and long epitopes, of up to at least 55 amino acid residues in length. AP205 VLPs confer a high immunogenicity to displayed epitopes, as shown by inhibition of endogenous GnRH and protective immunity against influenza infection.
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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.