Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/32513
Title: Trypanosoma cruzi heparin-binding proteins and the nature of the host cell heparan sulfate-binding domain
Authors: Oliveira, Francisco Odencio Rodrigues de
Alves, Carlos Roberto
Calvet, Cláudia Magalhães
Toma, Leny
Bouças, Rodrigo Ippolito
Nader, Helena Bociani
Côrtes, Luzia Monteiro de Castro
Krieger, Marco Aurélio
Meirelles, Maria de Nazareth S. L.
Pereira, Mirian Claudia de Souza
Affilliation: Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório Ultraestrutura Celular. Rio de Janeiro, RJ. Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ. Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório Ultraestrutura Celular. Rio de Janeiro, RJ. Brasil.
Universidade Federal de São Paulo. Departamento de Bioquímica. São Paulo, SP, Brasil.
Universidade Federal de São Paulo. Departamento de Bioquímica. São Paulo, SP, Brasil.
Universidade Federal de São Paulo. Departamento de Bioquímica. São Paulo, SP, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ. Brasil.
Fundação Oswaldo Cruz. Instituto de Biologia Molecular do Paraná. Curitiba, PR, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório Ultraestrutura Celular. Rio de Janeiro, RJ. Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório Ultraestrutura Celular. Rio de Janeiro, RJ. Brasil.
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 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.
Keywords: Trypanosoma cruzi
Cardiomyocytes
Glycosaminoglycans
Recognition process
Chromatography
keywords: Trypanosoma cruzi
Cardiomiócitos
Glicosaminoglicanos
Processo de reconhecimento
Cromatografia
Issue Date: 2008
Publisher: Elsevier
Citation: OLIVEIRA JR, Francisco Odencio Rodrigues de et al. Trypanosoma cruzi heparin-binding proteins and the nature of the host cell heparan sulfate-binding domain. Microbial Pathogenesis, v. 44, p. 329-338, 2008.
DOI: 10.1016/j.micpath.2007.10.003
ISSN: 0882-4010
Copyright: restricted access
Appears in Collections:PR - ICC - Artigos de Periódicos
IOC - Artigos de Periódicos

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