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

Published online by Cambridge University Press:  14 September 2012

F. O. R. OLIVEIRA-JR ,
C. R. ALVES ,
F. S. SILVA ,
L. M. C. CÔRTES ,
L. TOMA ,
R. I. BOUÇAS ,
T. AGUILAR ,
H. B. NADER  and
M. C. S. PEREIRA
F. O. R. OLIVEIRA-JR
Affiliation:
Laboratório de Ultra-estrutura Celular, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil
C. R. ALVES
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil
F. S. SILVA
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil
L. M. C. CÔRTES
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil
L. TOMA
Affiliation:
Departamento de Bioquímica, Universidade Federal de São Paulo, UNIFESP, SP, Brazil
R. I. BOUÇAS
Affiliation:
Departamento de Bioquímica, Universidade Federal de São Paulo, UNIFESP, SP, Brazil
T. AGUILAR
Affiliation:
Departamento de Bioquímica, Universidade Federal de São Paulo, UNIFESP, SP, Brazil
H. B. NADER
Affiliation:
Departamento de Bioquímica, Universidade Federal de São Paulo, UNIFESP, SP, Brazil
M. C. S. PEREIRA*
Affiliation:
Laboratório de Ultra-estrutura Celular, Instituto Oswaldo Cruz/FIOCRUZ, RJ, Brazil
*
*Corresponding author: Laboratório de Ultra-estrutura Celular, Instituto Oswaldo Cruz, FIOCRUZ, Av. Brasil 4365, Manguinhos, 21045-900 Rio de Janeiro, RJ, Brazil. Tel: +5521 2598 4330. Fax: +5521 2598 4330. E-mail: [email protected]
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Summary

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.

Keywords

Trypanosoma cruziheparin-binding proteinplasmon surface resonanceserine proteinase
Type
Research Article
Information
Parasitology , Volume 140 , Issue 2 , February 2013 , pp. 171 - 180
Copyright
Copyright © Cambridge University Press 2012

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