The Solution Structure of the Adhesion Protein Bd37 from Babesia divergens Reveals Structural Homology with Eukaryotic Proteins Involved in Membrane Trafficking

Stéphane Delbecq, Daniel Auguin*, Yin Shan Yang, Frank Löhr, Stefan Arold, Theo Schetters, Eric Précigout, André Gorenflot, Christian Roumestand

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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 (Δ-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 Δ-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.

Original languageEnglish (US)
Pages (from-to)409-424
Number of pages16
JournalJournal of Molecular Biology
Volume375
Issue number2
DOIs
StatePublished - Jan 11 2008

Keywords

  • GPI-anchored protein
  • apicomplexa
  • recombinant vaccine
  • surface antigen
  • vesicle traffiking

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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