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

hal-00202881, version 1

The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking.

Stéphane Delbecq ¹, Daniel Auguin ², Yin-Shan Yang ^{3, 4, 5, 6, 7, 8, 9, 10}, Frank Löhr, Stefan Arold ², Theo Schetters, Eric Précigout ¹¹, André Gorenflot ¹, Christian Roumestand ²

Journal of Molecular Biology 375, 2 (2008) 409-24

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.

1: Dynamique des interactions membranaires normales et pathologiques (DIMNP)
CNRS : UMR5235 – Université Montpellier I – Université Montpellier II - Sciences et techniques
2: Centre de biochimie structurale (CBS)
CNRS : UMR5048 – INSERM : U554 – IFR3 – Université Montpellier I – Université Montpellier II - Sciences et techniques
3: Rensselaer Polytechnic Institute (Rensselaer Polytechnic Institute)
Rensselaer Polytechnic Institute
4: Laboratoire d'études de la différenciation et de l'adhérence cellulaires (LEDAC)
CNRS : UMR5538 – Université Joseph Fourier - Grenoble I
5: Department of Electrical and Computer Engineering
Illinois Institute of Technology
6: Tokyo University of Agriculture and Technology
Tokyo University of Agriculture and Technology
7: Department of Computer Science and Engineering, University of California, San Diego (CSE-UCSD)
University of California, San Diego
8: CAD (CAD LIAMA INRIA Paris - Rocquencourt)
Centre de coopération internationale en recherche agronomique pour le développement [CIRAD] – CNRS – Institut national de la recherche agronomique (INRA) – Chinese Academy of Science (CAS) – Institute of Automation, Chinese Academy of Sciences – INRIA
9: Department of Electrical and Computer Engineering [TORONTO] (ECE)
University of Toronto
10: Galaxies, Etoiles, Physique, Instrumentation (GEPI)
CNRS : UMR8111 – INSU – Observatoire de Paris – Université Paris VII - Paris Diderot
11: Vaccination antiparasitaire (ERT1038)
Université Montpellier I

hal-00202881, version 1
http://hal.archives-ouvertes.fr/hal-00202881
oai:hal.archives-ouvertes.fr:hal-00202881
From: Annie Bosch-Savary <>
Submitted on: Tuesday, 8 January 2008 12:45:57
Updated on: Tuesday, 8 January 2008 12:45:57

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PubMed: 18035372

DOI: 10.1016/j.jmb.2007.08.019

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%% hal-00202881, version 1
%% http://hal.archives-ouvertes.fr/hal-00202881
@article{delbecq:hal-00202881,
    hal_id = {hal-00202881},
    url = {http://hal.archives-ouvertes.fr/hal-00202881},
    title = {{The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking.}},
    author = {Delbecq, St{\'e}phane and Auguin, Daniel and Yang, Yin-Shan and L{\"o}hr, Frank and Arold, Stefan and Schetters, Theo and Pr{\'e}cigout, Eric and Gorenflot, Andr{\'e} and Roumestand, Christian},
    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.}},
    language = {English},
    affiliation = {Dynamique des interactions membranaires normales et pathologiques - DIMNP , Centre de biochimie structurale - CBS , Rensselaer Polytechnic Institute - Rensselaer Polytechnic Institute , Laboratoire d'{\'e}tudes de la diff{\'e}renciation et de l'adh{\'e}rence cellulaires - LEDAC , Department of Electrical and Computer Engineering , Tokyo University of Agriculture and Technology , Department of Computer Science and Engineering, University of California, San Diego - CSE-UCSD , CAD - CAD LIAMA INRIA Paris - Rocquencourt , Department of Electrical and Computer Engineering [TORONTO] - ECE , Galaxies, Etoiles, Physique, Instrumentation - GEPI , Vaccination antiparasitaire - ERT1038},
    pages = {409-24},
    journal = {Journal of Molecular Biology},
    volume = {375},
    number = {2 },
    audience = {not specified },
    doi = {10.1016/j.jmb.2007.08.019 },
    year = {2008},
    month = Jan,
}

%F hal-00202881, version 1
%0 Journal Article
%U http://hal.archives-ouvertes.fr/hal-00202881
%2 SDV:BBM
%T The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking.
%A Delbecq, Stéphane
%A Auguin, Daniel
%A Yang, Yin-Shan
%A Löhr, Frank
%A Arold, Stefan
%A Schetters, Theo
%A Précigout, Eric
%A Gorenflot, André
%A Roumestand, Christian
%+ Dynamique des interactions membranaires normales et pathologiques - DIMNP , Centre de biochimie structurale - CBS , Rensselaer Polytechnic Institute - Rensselaer Polytechnic Institute , Laboratoire d'études de la différenciation et de l'adhérence cellulaires - LEDAC , Department of Electrical and Computer Engineering , Tokyo University of Agriculture and Technology , Department of Computer Science and Engineering, University of California, San Diego - CSE-UCSD , CAD - CAD LIAMA INRIA Paris - Rocquencourt , Department of Electrical and Computer Engineering [TORONTO] - ECE , Galaxies, Etoiles, Physique, Instrumentation - GEPI , Vaccination antiparasitaire - ERT1038
%X 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.
%G English
%R 10.1016/j.jmb.2007.08.019
%J Journal of Molecular Biology
%2 not specified
%8 2008-01-11
%2 2007-08-21
%V 375
%N 2
%P 409-24
%K Alleles; Amino Acid Sequence; Animals; Antigens, Protozoan; Babesia; Cell Membrane; Circular Dichroism; Disulfides; Epitopes; Erythrocytes; Eukaryotic Cells; Glutathione Transferase; Models, Molecular; Molecular Sequence Data; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Protozoan Proteins; Recombinant Proteins; Scattering, Small Angle; Sequence Homology, Amino Acid; Structure-Activity Relationship; X-Ray Diffraction

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