Trypanosoma cruzi heparin-binding proteins present a flagellar membrane localization and serine proteinase activity

Data
2013-02-01Autor(a)
Oliveira-, F. O. R.
Alves, C. R.
Silva, F. S.
Cortes, L. M. C.
Toma, L. [UNIFESP]
Boucas, R. I. [UNIFESP]
Aguilar, T. [UNIFESP]
Nader, H. B. [UNIFESP]
Pereira, M. C. S.
Tipo
ArtigoISSN
0031-1820É parte de
ParasitologyDOI
10.1017/S0031182012001448Metadado
Mostrar registro completoResumo
Heparin-binding proteins (HBPs) play a key role in Trypanosoma cruzi-host cell interactions. HBPs recognize heparan sulfate (HS) at the host cell surface and are able to induce the cytoadherence and invasion of this parasite. Herein, we analysed the biochemical properties of the HBPs and also evaluated the expression and subcellular localization of HBPs in T. cruzi trypomastigotes. A flow cytometry analysis revealed that HBPs are highly expressed at the surface of trypomastigotes, and their peculiar localization mainly at the flagellar membrane, which is known as an important signalling domain, may enhance their binding to HS and elicit the parasite invasion. the plasmon surface resonance results demonstrated the stability of HBPs and their affinity to HS and heparin. Additionally, gelatinolytic activities of 70 kDa, 65.8 kDa and 59 kDa HBPs over a broad pH range (5.5-8.0) were revealed using a zymography assay. These proteolytic activities were sensitive to serine proteinase inhibitors, such as aprotinin and phenylmethylsulfonyl fluoride, suggesting that HBPs have the properties of trypsin-like proteinases.
Citação
Parasitology. New York: Cambridge Univ Press, v. 140, n. 2, p. 171-180, 2013.Palavras-chave
Trypanosoma cruziheparin-binding protein
plasmon surface resonance
serine proteinase
Agência(s) de Fomento
Fundacao Oswaldo Cruz (FIOCRUZ)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Programa Estrategico de Apoio a Pesquisa em Saude
Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Coleções
- EPM - Artigos [17709]