2JO7

Solution structure of the adhesion protein Bd37 from Babesia divergens

Summary for 2JO7

• Entry DOI: 10.2210/pdb2jo7/pdb
• NMR Information: BMRB: 15158
• Descriptor: Glycosylphosphatidylinositol-anchored merozoite surface protein (1 entity in total)
• Functional Keywords: babesia divergens, surface antigen, gpi-anchored protein, recombinant vaccine, surface active protein
• Biological source: Babesia divergens
• Total number of polymer chains: 1
• Total formula weight: 24735.46

Authors

Auguin, D.,Yang, Y.,Lohr, F.,Arold, S.,Schetters, T.,Precigout, E.,Gorenflot, A.,Delbecq, S.,Roumestand, C. (deposition date: 2007-02-26, release date: 2007-12-11, Last modification date: 2023-12-20)

Primary citation

Delbecq, S.,Auguin, D.,Yang, Y.S.,Lohr, F.,Arold, S.,Schetters, T.,Precigout, E.,Gorenflot, A.,Roumestand, C.
The Solution Structure of the Adhesion Protein Bd37 from Babesia divergens Reveals Structural Homology with Eukaryotic Proteins Involved in Membrane Trafficking
J.Mol.Biol., 375:409-424, 2007

PubMed Abstract: Babesia divergens is the Apicomplexa agent of the bovine babesiosis in Europe: this infection leads to growth and lactation decrease, so that economical losses due to this parasite are sufficient to require the development of a vaccine. The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Delta-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Delta-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells.

PubMed: 18035372
DOI: 10.1016/j.jmb.2007.08.019

Experimental method

SOLUTION NMR