ArticlePloS one2011
Var2CSA minimal CSA binding region is located within the N-terminal region.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.
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Who cites it
46 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.
- Pregnancy-specific malarial immunity and risk of malaria in pregnancy and adverse birth outcomes: a systematic review.BMC medicine · 2020Pooled it
- FIKK1, a member of the FIKK kinase family, phosphorylates VAR2CSA and regulates adhesion of Plasmodium falciparum-infected erythrocytes to the placental receptor CSA.PLoS pathogens · 2026Article
- Longitudinal plasma metabolomics reveals a role for taurine in asymptomatic malaria and seasonal persistence.Nature microbiology · 2026Article
- Beyond VAR2CSA: redefining the antigenic landscape of placental malaria vaccines.Open research Africa · 2026Review
- Casein Kinases 2-dependent phosphorylation of the placental ligand VAR2CSA regulates Plasmodium falciparum-infected erythrocytes cytoadhesion.PLoS pathogens · 2025Article
- Aotus nancymaae model predicts human immune response to the placental malaria vaccine candidate VAR2CSA.Lab animal · 2023Article
- Article
- A conserved epitope in VAR2CSA is targeted by a cross-reactive antibody originating fromFrontiers in cellular and infection microbiology · 2023Article
- An Invariant Protein That Colocalizes With VAR2CSA on Plasmodium falciparum-Infected Red Cells Binds to Chondroitin Sulfate A.The Journal of infectious diseases · 2022Article
- Polymorphic Molecular Signatures in Variable Regions of thePathogens (Basel, Switzerland) · 2022Article
- The molecular mechanism of cytoadherence to placental or tumor cells through VAR2CSA from Plasmodium falciparum.Cell discovery · 2021Article
- mSphere of Influence: Structural Insights into the Molecular Mechanism Underlying Placental Malaria.mSphere · 2021Article
- 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
- Stringent Selection of KnobbyMicroorganisms · 2020Article
- VAR2CSA-Mediated Host Defense Evasion ofFrontiers in immunology · 2020Review
- VAR2CSA binding phenotype has ancient origin and arose before Plasmodium falciparum crossed to humans: implications in placental malaria vaccine design.Scientific reports · 2019Article
- Functional Antibodies against Placental Malaria Parasites Are Variant Dependent and Differ by Geographic Region.Infection and immunity · 2019Article
- Phosphorylation of the VAR2CSA extracellular region is associated with enhanced adhesive properties to the placental receptor CSA.PLoS biology · 2019Article
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Var2CSA, a key molecule linked with pregnancy-associated malaria (PAM), causes sequestration of Plasmodium falciparum infected erythrocytes (PEs) in the placenta by adhesion to chondroitin sulfate A (CSA). Var2CSA possesses a 300 kDa extracellular region composed of six Duffy-binding like (DBL) domains and a cysteine-rich interdomain region (CIDRpam) module. Although initial studies implicated several individual var2CSA DBL domains as important for adhesion of PEs to CSA, new studies revealed that these individual domains lack both the affinity and specificity displayed by the full-length extracellular region. Indeed, recent evidence suggests the presence of a single CSA-binding site formed by a higher-order domain organization rather than several independent binding sites located on the different domains. Here, we search for the minimal binding region within var2CSA that maintains high affinity and specificity for CSA binding, a characteristic feature of the full-length extracellular region. Accordingly, truncated recombinant var2CSA proteins comprising different domain combinations were expressed and their binding characteristics assessed against different sulfated glycosaminoglycans (GAGs). Our results indicate that the smallest region within var2CSA with similar binding properties to those of the full-length var2CSA is DBL1X-3X. We also demonstrate that inhibitory antibodies raised in rabbit against the full-length DBL1X-6ε target principally DBL3X and, to a lesser extent, DBL5ε. Taken together, our results indicate that efforts should focus on the DBL1X-3X region for developing vaccine and therapeutic strategies aimed at combating PAM.
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