8ARL

Plasmodium vivax PVP01_0000100 TRAg domain

Summary for 8ARL

• Entry DOI: 10.2210/pdb8arl/pdb
• Descriptor: Tryptophan-rich antigen (2 entities in total)
• Functional Keywords: plasmodium vivax bar domain trp-rich antigen, cell invasion
• Biological source: Plasmodium vivax (malaria parasite P. vivax)
• Total number of polymer chains: 1
• Total formula weight: 30935.82

Authors

Kundu, P.,Deane, J.E.,Rayner, J.C. (deposition date: 2022-08-17, release date: 2023-07-26, Last modification date: 2023-09-27)

Primary citation

Kundu, P.,Naskar, D.,McKie, S.J.,Dass, S.,Kanjee, U.,Introini, V.,Ferreira, M.U.,Cicuta, P.,Duraisingh, M.,Deane, J.E.,Rayner, J.C.
The structure of a Plasmodium vivax Tryptophan Rich Antigen domain suggests a lipid binding function for a pan-Plasmodium multi-gene family.
Nat Commun, 14:5703-5703, 2023

PubMed 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.

PubMed: 37709739
DOI: 10.1038/s41467-023-40885-8

Experimental method

X-RAY DIFFRACTION (1.45 Å)