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Updated: Jun 15, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
Published on: August 26, 2025
Can any lessons be learned from the ambiguous glycan binding of PfEMP1 domains?
Madeleine Dahlbäck1, Morten A Nielsen, Ali Salanti
1Centre for Medical Parasitology, Department of International Health, Immunology and Microbiology, University of Copenhagen and Department of Infectious Diseases, Copenhagen University Hospital (Rigshospitalet), CSS, Øster Farimagsgade 5A, DK-1014 Copenhagen K, Denmark. dahlback@sund.ku.dk <dahlback@sund.ku.dk>
Abstract:
Pregnancy-associated malaria (PAM) is caused by Plasmodium falciparum-infected erythrocytes (IEs) accumulating in the placenta and has dire consequences for both mother and child. The multi-domain antigen VAR2CSA confers specific adhesion of IEs to chondroitin sulphate A (CSA) in the placenta, and is the leading PAM vaccine candidate. Recent data from different laboratories show that the binding properties of individual VAR2CSA domains do not reflect the native CSA-specific adhesion of IEs, which questions the relevance of the information obtained from single domain binding assays and co-crystallization experiments. Here, we discuss the implications of these findings for VAR2CSA vaccine development and highlight the need for studying the native structure of this protein.
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