ArticleNature communications2023
Structure-based design of a strain transcending AMA1-RON2L malaria vaccine.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
18 citing papers in PubMed.
- Proteome-wide characterization of Plasmodium vivax antigens using a high-density peptide array.PLoS pathogens · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Erythrocyte invasion in malaria: from molecular mechanisms to rational vaccines.Nature reviews. Microbiology · 2026Review
- Malaria: past, present, and future.Signal transduction and targeted therapy · 2025Review
- Holding hands to halt malaria: stronger together through heterotypic antibody interactions.Trends in parasitology · 2025Article
- A strain-transcending anti-AMA1 human monoclonal antibody neutralizes malaria parasites independent of direct RON2L receptor blockade.Cell reports. Medicine · 2025Article
- Search continues: Exploring immunoinformatics platforms for designing an effective multiepitope malaria vaccine candidate.Biotechnologia · 2025Article
- Potent AMA1-specific human monoclonal antibody against Plasmodium vivax Pre-erythrocytic and Blood Stages.Nature communications · 2024Article
- Malaria vaccines: a new era of prevention and control.Nature reviews. Microbiology · 2024Review
- Functional and Immunologic Mapping of Domains of the Reticulocyte-Binding Protein Plasmodium vivax PvRBP2a.The Journal of infectious diseases · 2024Article
- Multistage protective anti-CelTOS monoclonal antibodies with cross-species sterile protection against malaria.Nature communications · 2024Article
- A broadly cross-reactive i-body to AMA1 potently inhibits blood and liver stages of Plasmodium parasites.Nature communications · 2024Article
- Structure-based design of a Plasmodium vivax Duffy-binding protein immunogen focuses the antibody response to functional epitopes.Protein science : a publication of the Protein Society · 2024Article
- RBD design increases the functional antibody titers elicited by SARS-CoV-2 spike vaccination.Antiviral research · 2024Article
- Vaccines and monoclonal antibodies: new tools for malaria control.Clinical microbiology reviews · 2024Review
- Structure-guided design of VAR2CSA-based immunogens and a cocktail strategy for a placental malaria vaccine.PLoS pathogens · 2024Article
- The Need for Novel Asexual Blood-Stage Malaria Vaccine Candidates forBiomolecules · 2024Review
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.
Funding
Abstract
Apical membrane antigen 1 (AMA1) is a key malaria vaccine candidate and target of neutralizing antibodies. AMA1 binds to a loop in rhoptry neck protein 2 (RON2L) to form the moving junction during parasite invasion of host cells, and this complex is conserved among apicomplexan parasites. AMA1-RON2L complex immunization achieves higher growth inhibitory activity than AMA1 alone and protects mice against Plasmodium yoelii challenge. Here, three single-component AMA1-RON2L immunogens were designed that retain the structure of the two-component AMA1-RON2L complex: one structure-based design (SBD1) and two insertion fusions. All immunogens elicited high antibody titers with potent growth inhibitory activity, yet these antibodies did not block RON2L binding to AMA1. The SBD1 immunogen induced significantly more potent strain-transcending neutralizing antibody responses against diverse strains of Plasmodium falciparum than AMA1 or AMA1-RON2L complex vaccination. This indicates that SBD1 directs neutralizing antibody responses to strain-transcending epitopes in AMA1 that are independent of RON2L binding. This work underscores the importance of neutralization mechanisms that are distinct from RON2 blockade. The stable single-component SBD1 immunogen elicits potent strain-transcending protection that may drive the development of next-generation vaccines for improved malaria and apicomplexan parasite control.
Indexed as
Identifiers
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.