ArticleScientific reports2015
Structure of the DBL3X-DBL4ε region of the VAR2CSA placental malaria vaccine candidate: insight into DBL domain interactions.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Mechanical forces control the valency of the malaria adhesin VAR2CSA by exposing cryptic glycan binding sites.PLoS computational biology · 2023Article
- Associations between prenatal malaria exposure, maternal antibodies at birth, and malaria susceptibility during the first year of life in Burkina Faso.Infection and immunity · 2023Article
- Polymorphic Molecular Signatures in Variable Regions of thePathogens (Basel, Switzerland) · 2022Article
- Cryo-EM reveals the architecture of placental malaria VAR2CSA and provides molecular insight into chondroitin sulfate binding.Nature communications · 2021Article
- Progress and Insights Toward an Effective Placental Malaria Vaccine.Frontiers in immunology · 2021Review
- Molecular architecture and domain arrangement of the placental malaria protein VAR2CSA suggests a model for carbohydrate binding.The Journal of biological chemistry · 2020Article
- VAR2CSA-Mediated Host Defense Evasion ofFrontiers in immunology · 2020Review
- Phosphorylation of the VAR2CSA extracellular region is associated with enhanced adhesive properties to the placental receptor CSA.PLoS biology · 2019Article
- Placental malaria vaccine candidate antigen VAR2CSA displays atypical domain architecture in someCommunications biology · 2019Article
- Molecular Principles of Intrauterine Growth Restriction in Plasmodium Falciparum Infection.Frontiers in endocrinology · 2019Review
- Optimization of incubation conditions of Plasmodium falciparum antibody multiplex assays to measure IgG, IgGMalaria journal · 2018Article
- Plasmodium falciparum PfEMP1 Modulates Monocyte/Macrophage Transcription Factor Activation and Cytokine and Chemokine Responses.Infection and immunity · 2018Article
- Novel Strategies for Malaria Vaccine Design.Frontiers in immunology · 2018Review
- Malaria Parasites: The Great Escape.Frontiers in immunology · 2016Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human malaria parasite, Plasmodium falciparum, is able to evade spleen-mediated clearing from blood stream by sequestering in peripheral organs. This is due to the adhesive properties conferred by the P. falciparum Erythrocyte Membrane Protein 1 (PfEMP1) family exported by the parasite to the surface of infected erythrocytes. Expression of the VAR2CSA variant of PfEMP1 leads to pregnancy-associated malaria, which occurs when infected erythrocytes massively sequester in the placenta by binding to low-sulfated Chondroitin Sulfate A (CSA) present in the intervillous spaces. VAR2CSA is a 350 kDa protein that carries six Duffy-Binding Like (DBL) domains, one Cysteine-rich Inter-Domain Regions (CIDR) and several inter-domain regions. In the present paper, we report for the first time the crystal structure at 2.9 Å of a VAR2CSA double domain, DBL3X-DBL4ε, from the FCR3 strain. DBL3X and DBL4ε share a large contact interface formed by residues that are invariant or highly conserved in VAR2CSA variants, which suggests that these two central DBL domains (DBL3X-DBL4ε) contribute significantly to the structuring of the functional VAR2CSA extracellular region. We have also examined the antigenicity of peptides corresponding to exposed loop regions of the DBL4ε structure.
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