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Article

Structural and functional insight into how the Plasmodium falciparum VAR2CSA protein mediates binding to chondroitin sulfate A in placental malaria.

The Journal of biological chemistry - 6 Jul 2012

Clausen Thomas M, Christoffersen Stig, Dahlbäck Madeleine, Langkilde Annette Eva, Jensen Kamilla E, Resende Mafalda, Agerbæk Mette Ø, Andersen Daniel, Berisha Besim, Ditlev Sisse B, Pinto Vera V, Nielsen Morten A, Theander Thor G, Larsen Sine, Salanti Ali

Abstract excerpt

Malaria is a major global health problem. Pregnant women are susceptible to infection regardless of previously acquired immunity. Placental malaria is caused by parasites capable of sequestering in the placenta. This is mediated by VAR2CSA, a parasite antigen that interacts with chondroitin sulfate A (CSA). One vaccine strategy is to block this interaction with VAR2CSA-specific antibodies. It is a priority to...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22570492
DOI: 10.1074/jbc.M112.348839
PMCID: PMC3390611

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural and functional insight into how the Plasmodium falciparum VAR2CSA protein mediates binding to chondroitin sulfate A in placental malaria.PMID 22570492Read ↗

Structural basis for placental malaria mediated by Plasmodium falciparum VAR2CSA.Semantic proximity Read ↗

Structural insight into epitopes in the pregnancy-associated malaria protein VAR2CSA.Semantic proximity Read ↗

Structural insights into global mutations in the ligand-binding domain of VAR2CSA and its implications on placental malaria vaccine.Semantic proximity Read ↗

Cryo-EM reveals the architecture of placental malaria VAR2CSA and provides molecular insight into chondroitin sulfate bindingSemantic proximity Read ↗

Allelic variants of full-length VAR2CSA, the placental malaria vaccine candidate, differ in antigenicity and receptor binding affinitySemantic proximity Read ↗

Epitope mapping and topographic analysis of VAR2CSA DBL3X involved in P. falciparum placental sequestration.Semantic proximity Read ↗

Induction of Adhesion-Inhibitory Antibodies against Placental<i>Plasmodium falciparum</i>Parasites by Using Single Domains of VAR2CSASemantic proximity Read ↗

A single member of the Plasmodium falciparum var multigene family determines cytoadhesion to the placental receptor chondroitin sulphate A.Semantic proximity Read ↗

Down-selection of the VAR2CSA DBL1-2 expressed in E. coli as a lead antigen for placental malaria vaccine developmentSemantic proximity Read ↗

Structure of the DBL3X-DBL4ε region of the VAR2CSA placental malaria vaccine candidate: insight into DBL domain interactions.Semantic proximity Read ↗

Chondroitin sulphate A (CSA)-binding of single recombinant Duffy-binding-like domains is not restricted to Plasmodium falciparum Erythrocyte Membrane Protein 1 expressed by CSA-binding parasites.Semantic proximity Read ↗

Llama immunization with full-length VAR2CSA generates cross-reactive and inhibitory single-domain antibodies against the DBL1X domainSemantic proximity Read ↗

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