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Leishmania (Viannia) braziliensis: insights on subcellular distribution and biochemical properties of heparin-binding proteins

Published online by Cambridge University Press:  07 November 2011

LUZIA MONTEIRO DE CASTRO CÔRTES ,
MIRIAN CLAUDIA DE SOUZA PEREIRA ,
FRANCISCO ODÊNCIO RODRIGUES DE OLIVEIRA JUNIOR ,
SUZANA CORTE-REAL ,
FRANKLIN SOUZA DA SILVA ,
BERNARDO ACÁCIO SANTINI PEREIRA ,
MARIA DE FÁTIMA MADEIRA ,
MARCIA TEREZINHA BARONI DE MORAES ,
REGINALDO PEÇANHA BRAZIL  and
CARLOS ROBERTO ALVES
LUZIA MONTEIRO DE CASTRO CÔRTES
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
MIRIAN CLAUDIA DE SOUZA PEREIRA
Affiliation:
Laboratório de Ultraestrutura Celular, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
FRANCISCO ODÊNCIO RODRIGUES DE OLIVEIRA JUNIOR
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil Laboratório de Ultraestrutura Celular, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
SUZANA CORTE-REAL
Affiliation:
Laboratório de Biologia Estrutural, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
FRANKLIN SOUZA DA SILVA
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
BERNARDO ACÁCIO SANTINI PEREIRA
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
MARIA DE FÁTIMA MADEIRA
Affiliation:
Laboratório de Vigilância em Leishmanioses, IPEC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
MARCIA TEREZINHA BARONI DE MORAES
Affiliation:
Laboratório de Virologia Molecular, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
REGINALDO PEÇANHA BRAZIL
Affiliation:
Laboratório de Bioquímica e Fisiologia de Insetos, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
CARLOS ROBERTO ALVES*
Affiliation:
Laboratório de Biologia Molecular e Doenças Endêmicas, IOC – FIOCRUZ, Av. Brasil 4365, Rio de Janeiro, CEP 21040-360, Brasil
*
*Corresponding author: LABIMDOE, IOC, Fiocruz. Av. Brasil 4365, CP 926, 21040-360, Manguinhos, Rio de Janeiro, RJ, Brazil. E-mail: calves@ioc.fiocruz.br
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Summary

Leishmaniasis is a vector-borne disease and an important public health issue. Glycosaminoglycan ligands in Leishmania parasites are potential targets for new strategies to control this disease. We report the subcellular distribution of heparin-binding proteins (HBPs) in Leishmania (Viannia) braziliensis and specific biochemical characteristics of L. (V.) braziliensis HBPs. Promastigotes were fractionated, and flagella and membrane samples were applied to HiTrap Heparin affinity chromatography columns. Heparin-bound fractions from flagella and membrane samples were designated HBP Ff and HBP Mf, respectively. Fraction HBP Ff presented a higher concentration of HBPs relative to HBP Mf, and SDS-PAGE analyses showed 2 major protein bands in both fractions (65 and 55 kDa). The 65 kDa band showed gelatinolytic activity and was sensitive to inhibition by 1,10-phenanthroline. The localization of HBPs on the promastigote surfaces was confirmed using surface plasmon resonance (SPR) biosensor analysis by binding the parasites to a heparin-coated sensor chip; that was inhibited in a dose-dependent manner by pre-incubating the parasites with variable concentrations of heparin, thus indicating distinct heparin-binding capacities for the two fractions. In conclusion, protein fractions isolated from either the flagella or membranes of L. (V.) braziliensis promastigotes have characteristics of metallo-proteinases and are able to bind to glycosaminoglycans.

Keywords

Leishmania (Viannia) braziliensisglycosaminoglycansheparinheparin-binding proteinsurface plasmon resonancemetallo-proteinase
Type
Research Article
Information
Parasitology , Volume 139 , Issue 2 , February 2012 , pp. 200 - 207
Copyright
Copyright © Cambridge University Press 2011

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