ArticleThe Journal of biological chemistry2013
Molecular architecture of a complex between an adhesion protein from the malaria parasite and intracellular adhesion molecule 1.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 2 of them syntheses that pooled it.
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The trial behind it
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Who cites it
29 citing papers in PubMed, 2 syntheses or guidelines pooled it, 43 citations in OpenAlex.
- Association between K469E polymorphism of ICAM-1 gene and susceptibility of ischemic stroke: An updated meta-analysis.Molecular genetics & genomic medicine · 2019Pooled it
- Intracellular adhesion molecule-1 K469E gene polymorphism and risk of diabetic microvascular complications: a meta-analysis.PloS one · 2013Pooled it
- Mapping the expression of endothelial adhesion receptors for Plasmodium falciparum-infected erythrocytes in fatal cerebral malaria in Malawian children.Journal of neuropathology and experimental neurology · 2025Article
- An update on cerebral malaria for therapeutic intervention.Molecular biology reports · 2022Review
- Current status of experimental models for the study of malaria.Parasitology · 2022Review
- Structural basis for placental malaria mediated by Plasmodium falciparum VAR2CSA.Nature microbiology · 2021Article
- The Potential Roles of Glial Cells in the Neuropathogenesis of Cerebral Malaria.Frontiers in cellular and infection microbiology · 2021Review
- Pathophysiology and neurologic sequelae of cerebral malaria.Malaria journal · 2020Review
- Cerebral Plasmodium falciparum malaria: The role of PfEMP1 in its pathogenesis and immunity, and PfEMP1-based vaccines to prevent it.Immunological reviews · 2020Review
- Structural insights into diverse modes of ICAM-1 binding byProceedings of the National Academy of Sciences of the United States of America · 2019Article
- In silico guided reconstruction and analysis of ICAM-1-binding var genes from Plasmodium falciparum.Scientific reports · 2018Article
- Towards an anti-disease malaria vaccine.Emerging topics in life sciences · 2017Article
- Variant surface antigens of Plasmodium falciparum and their roles in severe malaria.Nature reviews. Microbiology · 2017Review
- In vitro inhibition and reversal of Plasmodium falciparum cytoadherence to endothelium by monoclonal antibodies to ICAM-1 and CD36.Malaria journal · 2017Article
- A re-assessment of gene-tag classification approaches for describingWellcome open research · 2017Article
- Plasmodium falciparum var genes expressed in children with severe malaria encode CIDRα1 domains.EMBO molecular medicine · 2016Article
- Structure of the DBL3X-DBL4ε region of the VAR2CSA placental malaria vaccine candidate: insight into DBL domain interactions.Scientific reports · 2015Article
- Mapping the Binding Site of a Cross-Reactive Plasmodium falciparum PfEMP1 Monoclonal Antibody Inhibitory of ICAM-1 Binding.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- α2-Macroglobulin Can Crosslink Multiple Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Molecules and May Facilitate Adhesion of Parasitized Erythrocytes.PLoS pathogens · 2015Article
- Investigating the function of Fc-specific binding of IgM to Plasmodium falciparum erythrocyte membrane protein 1 mediating erythrocyte rosetting.Cellular microbiology · 2015Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The adhesion of Plasmodium falciparum-infected erythrocytes to human tissues or endothelium is central to the pathology caused by the parasite during malaria. It contributes to the avoidance of parasite clearance by the spleen and to the specific pathologies of cerebral and placental malaria. The PfEMP1 family of adhesive proteins is responsible for this sequestration by mediating interactions with diverse human ligands. In addition, as the primary targets of acquired, protective immunity, the PfEMP1s are potential vaccine candidates. PfEMP1s contain large extracellular ectodomains made from CIDR (cysteine-rich interdomain regions) and DBL (Duffy-binding-like) domains and show extensive variation in sequence, size, and domain organization. Here we use biophysical methods to characterize the entire ∼300-kDa ectodomain from IT4VAR13, a protein that interacts with the host receptor, intercellular adhesion molecule-1 (ICAM-1). We show through small angle x-ray scattering that IT4VAR13 is rigid, elongated, and monomeric. We also show that it interacts with ICAM-1 through the DBLβ domain alone, forming a 1:1 complex. These studies provide a first low resolution structural view of a PfEMP1 ectodomain in complex with its ligand. They show that it combines a modular domain arrangement consisting of individual ligand binding domains, with a defined higher order architecture that exposes the ICAM-1 binding surface to allow adhesion.
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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.