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J. Biol. Chem., Vol. 279, Issue 19, 19607-19613, May 7, 2004

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Triatoma infestans Apyrases Belong to the 5'-Nucleotidase Family^*

Eric Faudry, Silene P. Lozzi, Jaime M. Santana, Marian D'Souza-Ault, Sylvie Kieffer¶, Carlos R. Felix||, Carlos A. O. Ricart**, Marcelo V. Sousa**, Thierry Vernet, and Antonio R. L. Teixeira

From the Chagas' Disease Multidisciplinary Research Laboratory, Department of Pathology, Faculty of Medicine, the ^||Enzymology Laboratory, and the ^**Center for Protein Research and Services, Institute of Biology, University of Brasília, Brazil 70.910-900, the ^¶Laboratoire de Chimie des Proteines, Département Réponse et Dynamique Cellulaire, CEA-Grenoble F-38054, Grenoble cedex 9, France, and the Laboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale J. P. Ebel CEACNRS/UJF, 38027 Grenoble cedex 1, France

Apyrases are nucleoside triphosphate-diphosphohydrolases (EC 3.6.1.5) present in a variety of organisms. The apyrase activity found in the saliva of hematophagous insects is correlated with the prevention of ADP-induced platelet aggregation of the host during blood sucking. Purification of apyrase activity from the saliva of the triatomine bug Triatoma infestans was achieved by affinity chromatography on oligo(dT)-cellulose and gel filtration chromatography. The isolated fraction includes five N-glycosylated polypeptides of 88, 82, 79, 68 and 67 kDa apparent molecular masses. The isolated apyrase mixture completely inhibited aggregation of human blood platelets. Labeling with the ATP substrate analogue 5'-p-fluorosulfonylbenzoyladenosine showed that the five species have ATP-binding characteristic of functional apyrases. Furthermore, tandem mass spectroscopy peptide sequencing showed that the five species share sequence similarities with the apyrase from Aedes aegypti and with 5'-nucleotidases from other species. The complete cDNA of the 79-kDa enzyme was cloned, and its sequence confirmed that it encodes for an apyrase belonging to the 5'-nucleotidase family. The gene multiplication leading to the unusual salivary apyrase diversity in T. infestans could represent an important mechanism amplifying the enzyme expression during the insect evolution to hematophagy, in addition to an escape from the host immune response, thus enhancing acquisition of a meal by this triatomine vector of Chagas' disease.

Received for publication, February 16, 2004

^* This work was supported in part by the World Bank/Financiadora de Estudos e Projetos-FINEP, the CNPq/Brazil, the Région Rhône-Alpes, and Fondation pour la Recherche Médicale/France. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AJ581749.

To whom correspondence should be addressed. Tel.: 55-61-349-4987; Fax: 55-61-273-4645; E-mail: ateixeir{at}unb.br.

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