Trypanosoma cruzi heparin-binding proteins present a flagellar membrane localization and serine proteinase activity.
Parasitology
; 140(2): 171-80, 2013 02.
Article
en En
| MEDLINE
| ID: mdl-22975090
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Trypanosoma cruzi
/
Proteínas Protozoarias
/
Membrana Celular
/
Serina Proteasas
/
Flagelos
Idioma:
En
Revista:
Parasitology
Año:
2013
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Reino Unido