ArticleProceedings of the National Academy of Sciences of the United States of America2016
Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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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Who cites it
65 citing papers in PubMed, 88 citations in OpenAlex.
- Identification and Characterization of Functional Human Monoclonal Antibodies toJournal of immunology (Baltimore, Md. : 1950) · 2019Trial
- Immunodominant B-cell epitopes for precision surveillance ofEmerging microbes & infections · 2026Article
- Machine learning framework to extract physicochemical features of B-cell epitopes recognized by a cross-reactive antibody.NPJ systems biology and applications · 2025Article
- 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
- Structure-guided design of VAR2CSA-based immunogens and a cocktail strategy for a placental malaria vaccine.PLoS pathogens · 2024Article
- Duffy antigen is expressed during erythropoiesis in Duffy-negative individuals.Cell host & microbe · 2023Article
- Human monoclonal antibodies inhibit invasion of transgenic Plasmodium knowlesi expressing Plasmodium vivax Duffy binding protein.Malaria journal · 2023Article
- Designing an effective malaria vaccine targeting Plasmodium vivax Duffy-binding protein.Trends in parasitology · 2023Review
- Genetic diversity and natural selection of Plasmodium vivax reticulocyte invasion genes in Ecuador.Malaria journal · 2023Article
- Structural basis for DARC binding in reticulocyte invasion by Plasmodium vivax.Nature communications · 2023Article
- Naturally-acquired and Vaccine-induced Human Monoclonal Antibodies tobioRxiv : the preprint server for biology · 2023Article
- Design of a stabilized non-glycosylated Pfs48/45 antigen enables a potent malaria transmission-blocking nanoparticle vaccine.NPJ vaccines · 2023Article
- A conserved epitope in VAR2CSA is targeted by a cross-reactive antibody originating fromFrontiers in cellular and infection microbiology · 2023Article
- Inhibition of a malaria host-pathogen interaction by a computationally designed inhibitor.Protein science : a publication of the Protein Society · 2023Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- GIP: an open-source computational pipeline for mapping genomic instability from protists to cancer cells.Nucleic acids research · 2022Article
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- Sequence analysis of Plasmodium vivax Duffy binding proteins reveals the presence of unique haplotypes and diversifying selection in Ethiopian isolates.Malaria journal · 2021Article
5 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
8 authors at 2 institutions in 1 country.
Funding
Abstract
Plasmodium vivax Duffy Binding Protein (PvDBP) is the most promising vaccine candidate for P. vivax malaria. The polymorphic nature of PvDBP induces strain-specific immune responses, however, and the epitopes of broadly neutralizing antibodies are unknown. These features hamper the rational design of potent DBP-based vaccines and necessitate the identification of globally conserved epitopes. Using X-ray crystallography, small-angle X-ray scattering, hydrogen-deuterium exchange mass spectrometry, and mutational mapping, we have defined epitopes for three inhibitory mAbs (mAbs 2D10, 2H2, and 2C6) and one noninhibitory mAb (3D10) that engage DBP. These studies expand the currently known inhibitory epitope repertoire by establishing protective motifs in subdomain three outside the receptor-binding and dimerization residues of DBP, and introduce globally conserved protective targets. All of the epitopes are highly conserved among DBP alleles. The identification of broadly conserved epitopes of inhibitory antibodies provides critical motifs that should be retained in the next generation of potent vaccines for P. vivax malaria.
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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.