ArticleJournal of molecular biology2009
Structural comparison of two CSPG-binding DBL domains from the VAR2CSA protein important in malaria during pregnancy.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 63 citations in OpenAlex.
- Mechanical forces control the valency of the malaria adhesin VAR2CSA by exposing cryptic glycan binding sites.PLoS computational biology · 2023Article
- A conserved epitope in VAR2CSA is targeted by a cross-reactive antibody originating fromFrontiers in cellular and infection microbiology · 2023Article
- Allelic variants of full-length VAR2CSA, the placental malaria vaccine candidate, differ in antigenicity and receptor binding affinity.Communications biology · 2021Article
- Cryo-EM reveals the architecture of placental malaria VAR2CSA and provides molecular insight into chondroitin sulfate binding.Nature communications · 2021Article
- Structural basis for placental malaria mediated by Plasmodium falciparum VAR2CSA.Nature microbiology · 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
- 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
- Role of extracellular matrix and microenvironment in regulation of tumor growth and LAR-mediated invasion in glioblastoma.PloS one · 2018Article
- Structure of the DBL3X-DBL4ε region of the VAR2CSA placental malaria vaccine candidate: insight into DBL domain interactions.Scientific reports · 2015Article
- Parity-dependent recognition of DBL1X-3X suggests an important role of the VAR2CSA high-affinity CSA-binding region in the development of the humoral response against placental malaria.Infection and immunity · 2015Article
- Structural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine design.PLoS neglected tropical diseases · 2015Article
- Article
- Malaria adhesins: structure and function.Cellular microbiology · 2014Review
- Sequence variation and structural conservation allows development of novel function and immune evasion in parasite surface protein families.Protein science : a publication of the Protein Society · 2014Review
- Rosetting Plasmodium falciparum-infected erythrocytes bind to human brain microvascular endothelial cells in vitro, demonstrating a dual adhesion phenotype mediated by distinct P. falciparum erythrocyte membrane protein 1 domains.Infection and immunity · 2014Article
- Article
- Molecular architecture of a complex between an adhesion protein from the malaria parasite and intracellular adhesion molecule 1.The Journal of biological chemistry · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Severe malaria during pregnancy is associated with accumulation of parasite-infected erythrocytes in the placenta due to interactions between VAR2CSA protein, expressed on the surface of infected-erythrocytes, and placental chondroitin sulfate proteoglycans (CSPG). VAR2CSA contains multiple CSPG-binding domains, including DBL3X and DBL6 epsilon. Previous structural studies of DBL3X suggested CSPG to bind to a positively charged patch and sulfate-binding site on the concave surface of the domain. Here we present the structure of the DBL6 epsilon domain from VAR2CSA. This domain displays the same overall architecture and secondary structure as that of DBL3X but differs in loop structures, disulfide bond positions and surface charge distribution. In particular, despite binding to CSPG, DBL6 epsilon lacks the key features of the CSPG-binding site of DBL3X. Instead DBL6 epsilon binds to CSPG through a positively charged surface on the distal side of subdomain 2 that is exposed in intact VAR2CSA on the erythrocyte surface. Finally, unlike intact VAR2CSA, both DBL3X and DBL6 epsilon bind to various carbohydrates, with greatest affinity for ligands with high sulfation and negative charge. These studies provide further insight into the structure of DBL domains and suggest a model for the role of individual domains in CSPG binding by VAR2CSA in placental malaria.
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