ArticleScientific reports2019
Engineering a Virus-Like Particle as an Antigenic Platform for a Pfs47-Targeted Malaria Transmission-Blocking Vaccine.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 45 citations in OpenAlex.
- Application and Research Progress of Self-Assembling Protein Nanoparticles in Vaccine Development.International journal of molecular sciences · 2026Review
- Virus Biomimetic-Delivery Systems for the Production of Vaccines.Biomimetics (Basel, Switzerland) · 2026Review
- Protein nanocages: A new frontier in mucosal vaccine delivery and immune activation.Human vaccines & immunotherapeutics · 2025Review
- Article
- Development and Protective Efficacy of a Novel Nanoparticle Vaccine for Gammacoronavirus Avain Infectious Bronchitis Virus.Vaccines · 2025Article
- A bacteriophage-based virus-like particle vaccine induces cross-reactive neutralising antibodies against porcine epidemic diarrhoea viruses (PEDV).Veterinary research · 2025Article
- mRNA vaccines expressing malaria transmission-blocking antigens Pfs25 and Pfs230D1 induce a functional immune response.NPJ vaccines · 2024Article
- Development of an anti-Pfs230 monoclonal antibody as a Plasmodium falciparum gametocyte blocker.Research square · 2023Article
- Development of a Tag/Catcher-mediated capsid virus-like particle vaccine presenting the conservedInfection and immunity · 2023Article
- A nanoparticle vaccine displaying the ookinete PSOP25 antigen elicits transmission-blocking antibody response against Plasmodium berghei.Parasites & vectors · 2023Article
- A potent and durable malaria transmission-blocking vaccine designed from a single-component 60-copy Pfs230D1 nanoparticle.NPJ vaccines · 2023Article
- Malaria therapeutics: are we close enough?Parasites & vectors · 2023Review
- Review
- A modular and self-adjuvanted multivalent vaccine platform based on porcine circovirus virus-like nanoparticles.Journal of nanobiotechnology · 2022Article
- Deceiving and escaping complement - the evasive journey of the malaria parasite.Trends in parasitology · 2022Review
- Pfs47 as a Malaria Transmission-Blocking Vaccine Target.The American journal of tropical medicine and hygiene · 2022Article
- Virus-like particle vaccinology, from bench to bedside.Cellular & molecular immunology · 2022Review
- Elucidating functional epitopes within the N-terminal region of malaria transmission blocking vaccine antigen Pfs230.NPJ vaccines · 2022Article
- Heterologous Expression and Evaluation of NovelFrontiers in immunology · 2022Article
- Biological Nanoparticles in Vaccine Development.Frontiers in bioengineering and biotechnology · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We recently characterized Pfs47, a protein expressed on the surface of sexual stages and ookinetes of Plasmodium falciparum, as a malaria transmission-blocking vaccine (TBV) target. Mice immunization induced antibodies that conferred strong transmission-reducing activity (TRA) at a concentration of 200 μg/mL. Here, we sought to optimize the Pfs47 vaccine to elicit higher titers of high-affinity antibodies, capable of inducing strong TRA at a lower concentration. We report the development and evaluation of a Pfs47-based virus-like particle (VLP) vaccine generated by conjugating our 58 amino acid Pfs47 antigen to Acinetobacter phage AP205-VLP using the SpyCatcher:SpyTag adaptor system. AP205-Pfs47 complexes (VLP-P47) formed particles of ~22 nm diameter that reacted with polyclonal anti-Pfs47 antibodies, indicating that the antigen was accessible on the surface of the particle. Mice immunized with VLP-P47 followed by a boost with Pfs47 monomer induced significantly higher antibody titers, with higher binding affinity to Pfs47, than mice that received two immunizations with either VLP-P47 (VLP-P47/VLP-P47) or the Pfs47 monomer (P47/P47). Purified IgG from VLP-P47/P47 mice had strong TRA (83-98%) at concentrations as low as 5 μg/mL. These results indicate that conjugating the Pfs47 antigen to AP205-VLP significantly enhanced antigenicity and confirm the potential of Pfs47 as a TBV candidate.
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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.