ArticlePLoS pathogens2014
Red blood cell invasion by Plasmodium vivax: structural basis for DBP engagement of DARC.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 109 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
- Invasion preferences suggest a possible role for Plasmodium falciparum parasites in the expansion of Duffy negativity in West and Central Africa.Molecular biology and evolution · 2026Article
- Blood group antigens and malaria susceptibility.Frontiers in cellular and infection microbiology · 2025Review
- 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
- Article
- Structure-guided design of VAR2CSA-based immunogens and a cocktail strategy for a placental malaria vaccine.PLoS pathogens · 2024Article
- Virtual Screening of Flavonoids againstCurrent computer-aided drug design · 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
- Structural Space of the Duffy Antigen/Receptor for Chemokines' Intrinsically Disordered Ectodomain 1 Explored by Temperature Replica-Exchange Molecular Dynamics Simulations.International journal of molecular sciences · 2023Article
- Immunogenicity of a Plasmodium vivax vaccine based on the duffy binding protein formulated using adjuvants compatible for use in humans.Scientific reports · 2023Article
- Vaccination withScience translational medicine · 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
- 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
- Naturally-acquired and Vaccine-induced Human Monoclonal Antibodies tobioRxiv : the preprint server for biology · 2023Article
- The chemokines CXCL8 and CXCL12: molecular and functional properties, role in disease and efforts towards pharmacological intervention.Cellular & molecular immunology · 2023Review
- Malian children infected with Plasmodium ovale and Plasmodium falciparum display very similar gene expression profiles.PLoS neglected tropical diseases · 2023Article
19 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Plasmodium parasites use specialized ligands which bind to red blood cell (RBC) receptors during invasion. Defining the mechanism of receptor recognition is essential for the design of interventions against malaria. Here, we present the structural basis for Duffy antigen (DARC) engagement by P. vivax Duffy binding protein (DBP). We used NMR to map the core region of the DARC ectodomain contacted by the receptor binding domain of DBP (DBP-RII) and solved two distinct crystal structures of DBP-RII bound to this core region of DARC. Isothermal titration calorimetry studies show these structures are part of a multi-step binding pathway, and individual point mutations of residues contacting DARC result in a complete loss of RBC binding by DBP-RII. Two DBP-RII molecules sandwich either one or two DARC ectodomains, creating distinct heterotrimeric and heterotetrameric architectures. The DARC N-terminus forms an amphipathic helix upon DBP-RII binding. The studies reveal a receptor binding pocket in DBP and critical contacts in DARC, reveal novel targets for intervention, and suggest that targeting the critical DARC binding sites will lead to potent disruption of RBC engagement as complex assembly is dependent on DARC binding. These results allow for models to examine inter-species infection barriers, Plasmodium immune evasion mechanisms, P. knowlesi receptor-ligand specificity, and mechanisms of naturally acquired P. vivax immunity. The step-wise binding model identifies a possible mechanism by which signaling pathways could be activated during invasion. It is anticipated that the structural basis of DBP host-cell engagement will enable development of rational therapeutics targeting this interaction.
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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.