ArticlePLoS neglected tropical diseases2015
Structural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine design.
Article in PLoS neglected tropical diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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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
34 citing papers in PubMed, 47 citations in OpenAlex.
- Identification and Characterization of Functional Human Monoclonal Antibodies toJournal of immunology (Baltimore, Md. : 1950) · 2019Trial
- A Library of Plasmodium vivax Recombinant Merozoite Proteins Reveals New Vaccine Candidates and Protein-Protein Interactions.PLoS neglected tropical diseases · 2015Trial
- Proteome-wide characterization of Plasmodium vivax antigens using a high-density peptide array.PLoS pathogens · 2026Article
- A novel micronemal protein MP38 is involved in the invasion of merozoites into erythrocytes.mBio · 2025Article
- Multistage protective anti-CelTOS monoclonal antibodies with cross-species sterile protection against malaria.Nature communications · 2024Article
- Structure-guided design of VAR2CSA-based immunogens and a cocktail strategy for a placental malaria vaccine.PLoS pathogens · 2024Article
- Genetic differentiation of Plasmodium vivax duffy binding protein in Ethiopia and comparison with other geographical isolates.Malaria journal · 2024Article
- 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
- Structural basis for DARC binding in reticulocyte invasion by Plasmodium vivax.Nature communications · 2023Article
- Computational Exploration of Licorice for Lead Compounds againstMolecules (Basel, Switzerland) · 2023Article
- Design of a stabilized non-glycosylated Pfs48/45 antigen enables a potent malaria transmission-blocking nanoparticle vaccine.NPJ vaccines · 2023Article
- Glycan masking in vaccine design: Targets, immunogens and applications.Frontiers in immunology · 2023Review
- Inhibition of a malaria host-pathogen interaction by a computationally designed inhibitor.Protein science : a publication of the Protein Society · 2023Article
- Article
- Controlled human malaria infection with a clone of Plasmodium vivax with high-quality genome assembly.JCI insight · 2021Article
- A human monoclonal antibody blocks malaria transmission and defines a highly conserved neutralizing epitope on gametes.Nature communications · 2021Article
- Progress towards the development of aExpert review of vaccines · 2021Review
- Multiplexed Microsphere-Based Flow Cytometric Assay to Assess Strain Transcending Antibodies toFrontiers in immunology · 2021Article
- Global distribution of single amino acid polymorphisms inOpen biology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The Plasmodium vivax vaccine candidate Duffy Binding Protein (DBP) is a protein necessary for P. vivax invasion of reticulocytes. The polymorphic nature of DBP induces strain-specific immune responses that pose unique challenges for vaccine development. DEKnull is a synthetic DBP based antigen that has been engineered through mutation to enhance induction of blocking inhibitory antibodies. We determined the x-ray crystal structure of DEKnull to identify if any conformational changes had occurred upon mutation. Computational and experimental analyses assessed immunogenicity differences between DBP and DEKnull epitopes. Functional binding assays with monoclonal antibodies were used to interrogate the available epitopes in DEKnull. We demonstrate that DEKnull is structurally similar to the parental Sal1 DBP. The DEKnull mutations do not cause peptide backbone shifts within the polymorphic loop, or at either the DBP dimerization interface or DARC receptor binding pockets, two important structurally conserved protective epitope motifs. All B-cell epitopes, except for the mutated DEK motif, are conserved between DEKnull and DBP. The DEKnull protein retains binding to conformationally dependent inhibitory antibodies. DEKnull is an iterative improvement of DBP as a vaccine candidate. DEKnull has reduced immunogenicity to polymorphic regions responsible for strain-specific immunity while retaining conserved protein folds necessary for induction of strain-transcending blocking inhibitory antibodies.
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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 Socratic graph.