Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/30569
Title: Trypanosoma cruzi heparin-binding proteins and the nature of the host cell heparan sulfate-binding domain
Authors: Rodrigues de Oliveira, Francisco Odenclo
Alves, Carlos Roberto
Calvet, Claudia Magalhaes
Toma, Leny [UNIFESP]
Boucas, Rodrigo Ippolito [UNIFESP]
Nader, Helena Bociani [UNIFESP]
Castro Cortes, Luzia Monteiro de
Krieger, Marco Aurelio
Meirelles, Maria de Nazareth S. L.
Souza Pereira, Mirian Claudia de
Fiocruz MS
Universidade Federal de São Paulo (UNIFESP)
Keywords: Trypanosoma cruzi
Cardiomyocytes
Glycosaminoglycans
Recognition process
Chromatography
Issue Date: 1-Apr-2008
Publisher: Elsevier B.V.
Citation: Microbial Pathogenesis. London: Academic Press Ltd Elsevier B.V., v. 44, n. 4, p. 329-338, 2008.
Abstract: Trypanosoma cruzi invasion is mediated by receptor-ligand recognition between the surfaces of both parasite and target cell. We have previously demonstrated the role of heparan sulfate proteoglycan in the attachment and invasion of T cruzi in cardiomyocytes. Herein, we have isolated the T cruzi heparin-binding proteins (HBP-Tc) and investigated the nature of cardiomyocyte heparan Sulfate (HS)-binding site to the parasite surface ligand. Two major heparin-binding proteins with molecular masses of 65.8 and 59 kDa were observed in total extract of amastigote and trypomastigote forms of T cruzi. Hydrophobic [S(35)]methionine labeled proteins eluted from heparin-sepharose rose affinity chromatography also revealed both proteins in trypomastigotes but only the 59 kDa is strongly recognized by biotin-conjugated glycosaminoglycans. Competition assays were performed to analyze the role of sulfated proteoglycans, including heparin, keratan Sulfate and both acetylated and highly sulfated domains of heparan sulfate, in the recognition and invasion process of T cruzi. Significant inhibitions of 84% and 35% in the percentage of infection were revealed after treatment of the parasites with heparin and the N-acetylated/ N-sulfated heparan sulfate domain, respectively, Suggesting the important role of the glycuronic acid and NS glucosamine domain of the HS chain in the recognition of the HBP-Tc during the T cruzi-cardiomyocyte interaction. (C) 2007 Elsevier B.V. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/30569
ISSN: 0882-4010
Other Identifiers: http://dx.doi.org/10.1016/j.micpath.2007.10.003
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