Article
Trypanosoma cruzi heparin-binding proteins present a flagellar membrane localization and serine proteinase activity
Registro en:
OLIVEIRA JR., F.O.R.; et al. Trypanosoma cruzi heparin-binding proteins present a flagellar membrane localization and serine proteinase activity. Parasitology, v.140, 171–180
0031-1820
10.1017/S0031182012001448
Autor
Oliveira Jr., F. O. R.
Alves, C. R.
Silva, F. S.
Côrtes, L. M. C.
Toma, L.
Bouças, R. I.
Aguilar, T.
Nader, H. B.
Pereira, M. C. S.
Resumen
(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.) Processo FAPESP: 07/59801-1 - Estudo do envolvimento dos proteoglicanos na interação entre células tumorais e estromais na formação do tumor coloretal e de próstata
Beneficiário: Leny Toma 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.