ArticleNature communications2023
The structure of a Plasmodium vivax Tryptophan Rich Antigen domain suggests a lipid binding function for a pan-Plasmodium multi-gene family.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Proteome-wide characterization of Plasmodium vivax antigens using a high-density peptide array.PLoS pathogens · 2026Article
- Plasmodium knowlesi tryptophan-rich antigen 40.1 binds human erythrocyte spectrin alpha.PLoS neglected tropical diseases · 2026Article
- A Miniaturized Assay to Evaluate Plasmodium cynomolgi and Plasmodium knowlesi as Models for Prioritizing Plasmodium vivax Vaccine Targets.The Journal of infectious diseases · 2025Article
- The essential genome ofScience (New York, N.Y.) · 2025Article
- Plasmodium vivax antigen candidate prediction improves with the addition of Plasmodium falciparum data.NPJ systems biology and applications · 2024Article
- Plasmodium vivax tryptophan-rich antigen reduces type I collagen secretion via the NF-κBp65 pathway in splenic fibroblasts.Parasites & vectors · 2024Article
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Authors and funding
11 authors at 3 institutions in 4 countries.
Funding
Abstract
Tryptophan Rich Antigens (TRAgs) are encoded by a multi-gene family found in all Plasmodium species, but are significantly expanded in P. vivax and closely related parasites. We show that multiple P. vivax TRAgs are expressed on the merozoite surface and that one, PVP01_0000100 binds red blood cells with a strong preference for reticulocytes. Using X-ray crystallography, we solved the structure of the PVP01_0000100 C-terminal tryptophan rich domain, which defines the TRAg family, revealing a three-helical bundle that is conserved across Plasmodium and has structural homology with lipid-binding BAR domains involved in membrane remodelling. Biochemical assays confirm that the PVP01_0000100 C-terminal domain has lipid binding activity with preference for sulfatide, a glycosphingolipid present in the outer leaflet of plasma membranes. Deletion of the putative orthologue in P. knowlesi, PKNH_1300500, impacts invasion in reticulocytes, suggesting a role during this essential process. Together, this work defines an emerging molecular function for the Plasmodium TRAg family.
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