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Originally published In Press as doi:10.1074/jbc.M203185200 on September 16, 2002

J. Biol. Chem., Vol. 277, Issue 48, 45962-45968, November 29, 2002
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trans-Sialidase from Trypanosoma cruzi Binds Host T-lymphocytes in a Lectin Manner*

Adriane R. TodeschiniDagger , Murielle F. Girard§, Jean-Michel Wieruszeski||, Marise P. Nunes§, George A. DosReis§**, Lúcia Mendonça-Previato§**Dagger Dagger , and José O. Previato§

From the Dagger  Departamento de Bioquímica, Instituto de Biologia, 20551-013 Universidade do Estado do Rio de Janeiro, Brasil, § Instituto de Biofísica Carlos Chagas Filho, Centro de Ciências da Saúde - Bloco G, Universidade Federal do Rio de Janeiro, 21 944970, Cidade Universitária, Ilha do Fundão, Rio de Janeiro, Brasil, and || Laboratoire de RMN Synthese, Structure et Fonction des Biomolecules, Institut Pasteur, 59019 Lille, France

Trypanosoma cruzi, the protozoan parasite responsible for Chagas' disease, expresses on its surface an uncommon membrane-bound sialidase, known as trans-sialidase. trans-Sialidase is the product of a multigene family encoding both active and inactive proteins. We report here that an inactive mutant of trans-sialidase physically interacts with CD4+ T cells. Using a combination of flow cytometry and immunoprecipitation techniques, we identified the sialomucin CD43 as a counterreceptor for trans-sialidase on CD4+ T cells. Using biochemical, immunological, and spectroscopic approaches, we demonstrated that the inactive trans-sialidase is a sialic acid-binding protein displaying the same specificity required by active trans-sialidase. Taken together, these results suggest that inactive members of the trans-sialidase family can physically interact with sialic acid-containing molecules on host cells and could play a role in host cell/T. cruzi interaction.

* This work was supported by grants from Conselho Nacional de Desenvolvimento Científico e Tecnológico (Programa de Apoio ao Desenvolvimento Científico e Tecnológico, Programa Núcleo de Excelência), Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro, Fundação Universitaria José Bonifácio-Universidade Federal do Rio de Janeiro, and Coordenação de Aperfeiçoamento de Pessoal de Nível Superior-Comité Français D'Évaluation De La Coopération Universitaire Avec de Brésil.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

A recipient of a post-doctoral fellowship from Bourse Lavoisier du Ministère des Affaires Etrangèrés, France.

** Howard Hughes International Research Scholars.

Dagger Dagger To whom correspondence should be addressed. Tel.: 55-21-2562-6646; Fax: 55-21-22808193; E-mail: luciamp@biof.ufrj.br.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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