ArticleNature microbiology2019
Structural basis for neutralization of Plasmodium vivax by naturally acquired human antibodies that target DBP.
Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 62 citations in OpenAlex.
- Proteome-wide characterization of Plasmodium vivax antigens using a high-density peptide array.PLoS pathogens · 2026Article
- How Duffy Blood Group (FY) Polymorphism and Age Modulate Vivax Malaria Risk at the Community Level: A Population-based Retrospective Cohort Study in the Amazon.The Journal of infectious diseases · 2026Article
- The PvRBP2b-TfR1 interaction is not essential for reticulocytes invasion by Plasmodium vivax isolates from Cambodia.NPJ vaccines · 2024Article
- Multistage protective anti-CelTOS monoclonal antibodies with cross-species sterile protection against malaria.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
- Evaluation of naturally acquired immune responses against novel pre-erythrocytic Plasmodium vivax proteins in a low endemic malaria population located in the Peruvian Amazon Basin.Malaria journal · 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
- Designing an effective malaria vaccine targeting Plasmodium vivax Duffy-binding protein.Trends in parasitology · 2023Review
- Development of a Plasmodium vivax biobank for functional ex vivo assays.Malaria journal · 2023Article
- Elicitation of T-cell-derived IFN-γ-dependent immunity by highly conserved Plasmodium ovale curtisi Duffy binding protein domain region II (PocDBP-RII).Parasites & vectors · 2023Article
- A human antibody epitope map of the malaria vaccine antigen Pfs25.NPJ vaccines · 2023Article
- 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
- Characterization of Duffy Binding Protein II-specific CD4Scientific reports · 2023Article
- Immunological characterization of a VIR protein family member (VIR-14) in Plasmodium vivax-infected subjects from different epidemiological regions in Africa and South America.PLoS neglected tropical diseases · 2023Article
- Design of a stabilized non-glycosylated Pfs48/45 antigen enables a potent malaria transmission-blocking nanoparticle vaccine.NPJ vaccines · 2023Article
- Inhibition of a malaria host-pathogen interaction by a computationally designed inhibitor.Protein science : a publication of the Protein Society · 2023Article
- Prospects for targeting ACKR1 in cancer and other diseases.Frontiers in immunology · 2023Review
- Current approaches to malaria vaccines.Current opinion in microbiology · 2022Review
Corrections and comments
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- Erratum issued
Authors and funding
14 authors at 7 institutions in 3 countries.
Funding
Abstract
The Plasmodium vivax Duffy-binding protein (DBP) is a prime target of the protective immune response and a promising vaccine candidate for P. vivax malaria. Naturally acquired immunity (NAI) protects against malaria in adults residing in infection-endemic regions, and the passive transfer of malarial immunity confers protection. A vaccine that replicates NAI will effectively prevent disease. Here, we report the structures of DBP region II in complex with human-derived, neutralizing monoclonal antibodies obtained from an individual in a malaria-endemic area with NAI. We identified protective epitopes using X-ray crystallography, hydrogen-deuterium exchange mass spectrometry, mutational mapping and P. vivax invasion studies. These approaches reveal that naturally acquired human antibodies neutralize P. vivax by targeting the binding site for Duffy antigen receptor for chemokines (DARC) and the dimer interface of P. vivax DBP. Antibody binding is unaffected by polymorphisms in the vicinity of epitopes, suggesting that the antibodies have evolved to engage multiple polymorphic variants of DBP. The human antibody epitopes are broadly conserved and are distinct from previously defined epitopes for broadly conserved murine monoclonal antibodies. A library of globally conserved epitopes of neutralizing human antibodies offers possibilities for rational design of strain-transcending DBP-based vaccines and therapeutics against P. vivax.
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