ArticleScientific reports2018
Plasmodium falciparum infected erythrocytes can bind to host receptors integrins αVβ3 and αVβ6 through DBLδ1_D4 domain of PFL2665c PfEMP1 protein.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Among-population proteomic differences in Schistocephalus solidus based on excretory/secretory and total body protein predictions.Parasites & vectors · 2025Article
- Evasive mechanisms of human VSG and PfEMP1 antigens with link to Vaccine scenario: a review.Journal of parasitic diseases : official organ of the Indian Society for Parasitology · 2025Review
- A systems serology approach to identifying key antibody correlates of protection from cerebral malaria in Malawian children.BMC medicine · 2024Article
- GenotypingIndian journal of microbiology · 2024Article
- Profiling the Plasmodium falciparum Erythrocyte Membrane Protein 1-Specific Immununoglobulin G Response Among Ghanaian Children With Hemoglobin S and C.The Journal of infectious diseases · 2024Article
- PfEMP1 and var genes - Still of key importance in Plasmodium falciparum malaria pathogenesis and immunity.Advances in parasitology · 2024Review
- Are the integrin binding motifs within SARS CoV-2 spike protein and MHC class II alleles playing the key role in COVID-19?Frontiers in immunology · 2023Article
- CD36-A Host Receptor Necessary for Malaria Parasites to Establish and Maintain Infection.Microorganisms · 2022Review
- MicroRNAs: master regulators in host-parasitic protist interactions.Open biology · 2022Review
- High-Throughput BioPlex Assay for the Study of Functionally Active Plasmodium Falciparum Antigens That Are Expressed on the Surface of Infected Erythrocytes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cerebral Malaria: Current Clinical and Immunological Aspects.Frontiers in immunology · 2022Review
- Malaria Parasite Plasmodium falciparum Proteins on the Surface of Infected Erythrocytes as Targets for Novel Drug Discovery.Biochemistry. Biokhimiia · 2022Review
- Management of cell death in parasitic infections.Seminars in immunopathology · 2021Review
- Complement C1s cleaves PfEMP1 at interdomain conserved sites inhibitingProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Small Molecule Compounds Identified from Mixture-Based Library Inhibit Binding betweenInternational journal of molecular sciences · 2021Article
- Congenital Transmission of Apicomplexan Parasites: A Review.Frontiers in microbiology · 2021Review
- Optimization of in vitro trophoblast assay for real-time impedimetric sensing of trophoblast-erythrocyte interactions in Plasmodium falciparum malaria.Analytical and bioanalytical chemistry · 2020Article
- Structural insights into diverse modes of ICAM-1 binding byProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Comprehensive analysis of Fc-mediated IgM binding to the Plasmodium falciparum erythrocyte membrane protein 1 family in three parasite clones.Scientific reports · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Major complications and mortality from Plasmodium falciparum malaria are associated with cytoadhesion of parasite-infected erythrocytes (IE). The main parasite ligands for cytoadhesion are members of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) family. Interactions of different host receptor-ligand pairs may lead to various pathological outcomes, like placental or cerebral malaria. It has been shown previously that IE can bind integrin αVβ3. Using bead-immobilized PfEMP1 constructs, we have identified that the PFL2665c DBLδ1_D4 domain binds to αVβ3 and αVβ6. A parasite line expressing PFL2665c binds to surface-immobilized αVβ3 and αVβ6; both are RGD motif-binding integrins. Interactions can be inhibited by cyloRGDFV peptide, an antagonist of RGD-binding integrins. This is a first, to the best of our knowledge, implication of a specific PfEMP1 domain for binding to integrins. These host receptors have important physiological functions in endothelial and immune cells; therefore, these results will contribute to future studies and a better understanding, at the molecular level, of the physiological outcome of interactions between IE and integrin receptors on the surface of host cells.
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