ArticleNature communications2017
Molecular definition of multiple sites of antibody inhibition of malaria transmission-blocking vaccine antigen Pfs25.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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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
50 citing papers in PubMed, 70 citations in OpenAlex.
- Robust Bioconjugated Antigens Induce Immune Responses Preventing Malaria Infection and its Transmission.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- TEpiNom: A computational framework integrating population data to prioritize Plasmodium falciparum T cell epitopes.Vaccine · 2026Article
- BCRInsight: an antibody language model to decode biological signals from BCR sequences.Briefings in bioinformatics · 2026Article
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- Malaria vaccines: Current developments and immunological insights.New microbes and new infections · 2025Article
- Targeting Bottlenecks in Malaria Transmission: Antibody-Epitope Descriptions Guide the Design of Next-Generation Biomedical Interventions.Immunological reviews · 2025Review
- Protective antibodies target cryptic epitope unmasked by cleavage of malaria sporozoite protein.Science (New York, N.Y.) · 2025Article
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- Multistage protective anti-CelTOS monoclonal antibodies with cross-species sterile protection against malaria.Nature communications · 2024Article
- Diversity and selection analyses identify transmission-blocking antigens as the optimal vaccine candidates in Plasmodium falciparum.EBioMedicine · 2024Article
- Diversity and selection analyses identify transmission-blocking antigens as the optimal vaccine candidates inmedRxiv : the preprint server for health sciences · 2024Article
- Development of an anti-Pfs230 monoclonal antibody as a Plasmodium falciparum gametocyte blocker.Research square · 2023Article
- Designing an effective malaria vaccine targeting Plasmodium vivax Duffy-binding protein.Trends in parasitology · 2023Review
- A human antibody epitope map of the malaria vaccine antigen Pfs25.NPJ vaccines · 2023Article
- Targeting the Spike Receptor Binding Domain Class V Cryptic Epitope by an Antibody with Pan-Sarbecovirus Activity.Journal of virology · 2023Article
- Article
- Structural and immunological differences in Plasmodium falciparum sexual stage transmission-blocking vaccines comprised of Pfs25-EPA nanoparticles.NPJ vaccines · 2023Article
- Article
- A human antibody epitope map of Pfs230D1 derived from analysis of individuals vaccinated with a malaria transmission-blocking vaccine.Immunity · 2023Article
Corrections and comments
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Authors and funding
18 authors at 9 institutions in 3 countries.
Funding
Abstract
The Plasmodium falciparum Pfs25 protein (Pfs25) is a leading malaria transmission-blocking vaccine antigen. Pfs25 vaccination is intended to elicit antibodies that inhibit parasite development when ingested by Anopheles mosquitoes during blood meals. The Pfs25 three-dimensional structure has remained elusive, hampering a molecular understanding of its function and limiting immunogen design. We report six crystal structures of Pfs25 in complex with antibodies elicited by immunization via Pfs25 virus-like particles in human immunoglobulin loci transgenic mice. Our structural findings reveal the fine specificities associated with two distinct immunogenic sites on Pfs25. Importantly, one of these sites broadly overlaps with the epitope of the well-known 4B7 mouse antibody, which can be targeted simultaneously by antibodies that target a non-overlapping site to additively increase parasite inhibition. Our molecular characterization of inhibitory antibodies informs on the natural disposition of Pfs25 on the surface of ookinetes and provides the structural blueprints to design next-generation immunogens.
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