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Babesia divergens: cloning and biochemical characterization of Bd37

Published online by Cambridge University Press:  16 January 2003

S. DELBECQ ,
E. PRECIGOUT ,
A. VALLET ,
B. CARCY ,
T. P. M. SCHETTERS  and
A. GORENFLOT
S. DELBECQ
Affiliation:
Laboratoire de Biologie Cellulaire et Moléculaire, Faculté de Pharmacie, Université Montpellier I, 15 avenue C. Flahault, B.P. 14 491, 34093 Montpellier Cedex 5, France
E. PRECIGOUT
Affiliation:
Laboratoire de Biologie Cellulaire et Moléculaire, Faculté de Pharmacie, Université Montpellier I, 15 avenue C. Flahault, B.P. 14 491, 34093 Montpellier Cedex 5, France
A. VALLET
Affiliation:
Laboratoire de Biologie Cellulaire et Moléculaire, Faculté de Pharmacie, Université Montpellier I, 15 avenue C. Flahault, B.P. 14 491, 34093 Montpellier Cedex 5, France
B. CARCY
Affiliation:
Laboratoire de Biologie Cellulaire et Moléculaire, Faculté de Pharmacie, Université Montpellier I, 15 avenue C. Flahault, B.P. 14 491, 34093 Montpellier Cedex 5, France
T. P. M. SCHETTERS
Affiliation:
Department of Parasitology, Intervet International BV., Boxmeer, The Netherlands
A. GORENFLOT
Affiliation:
Laboratoire de Biologie Cellulaire et Moléculaire, Faculté de Pharmacie, Université Montpellier I, 15 avenue C. Flahault, B.P. 14 491, 34093 Montpellier Cedex 5, France
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Abstract

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The immunoprotective potential of Babesia divergens antigens released in supernatants of in vitro cultures of the parasite is generally known. Among a number of parasite molecules, a 37 kDa protein has been found in the supernatants of Babesia divergens cultures. In this report the cloning and biochemical characterization of this protein, called Bd37, are describedThe sequence data reported herein have been deposited in EMBL under Accession No. AJ422214. . In addition, the processing of the protein was studied in vitro. Results suggest that Bd37 is encoded by a single copy gene. Bd37 appears to be a merozoite-associated molecule attached to the surface by a glycosylphosphatidylinositol moiety containing a palmitate residue attached to the inositol ring. In addition, it is demonstrated that both extremities of the protein are linked by a disulphide bond. Results further indicate that a soluble, hydrophilic form of Bd37 can be released from the merozoite surface by GPI-specific phospholipase D. The potential role the Bd37 protein and the GPI anchor are discussed.

Keywords

Babesia divergensApicomplexaglycosylphosphatidylinositolmembrane-bound protein
Type
Research Article
Information
Parasitology , Volume 125 , Issue 4 , October 2002 , pp. 305 - 312
Copyright
2002 Cambridge University Press