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Leishmania major: detection of membrane-bound protein tyrosine phosphatase

Published online by Cambridge University Press:  05 January 2006

M. M. AGUIRRE-GARCÍA ,
A. R. ESCALONA-MONTAÑO ,
N. BAKALARA ,
A. PÉREZ-TORRES ,
L. GUTIÉRREZ-KOBEH  and
I. BECKER
M. M. AGUIRRE-GARCÍA
Affiliation:
Departamento de Medicina Experimental, Facultad de Medicina, Universidad Nacional Autónoma de México, México, D.F., México
A. R. ESCALONA-MONTAÑO
Affiliation:
Departamento de Medicina Experimental, Facultad de Medicina, Universidad Nacional Autónoma de México, México, D.F., México
N. BAKALARA
Affiliation:
Laboratoire de Genomique Fonctionelle des Trypanosomatides, UMR CNRS 5162, 146 rue Leo Saignat, 33076 Bordeaux, France
A. PÉREZ-TORRES
Affiliation:
Departamento de Biología Celular y Tisular, Facultad de Medicina, Universidad Nacional Autónoma de México, México, D.F., México
L. GUTIÉRREZ-KOBEH
Affiliation:
Departamento de Medicina Experimental, Facultad de Medicina, Universidad Nacional Autónoma de México, México, D.F., México
I. BECKER
Affiliation:
Departamento de Medicina Experimental, Facultad de Medicina, Universidad Nacional Autónoma de México, México, D.F., México
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Abstract

PTPases have been reported as a virulence factor in different pathogens. Recent studies suggest that PTPases play a role in the pathogenesis of Leishmania infections through activation of macrophage PTPases by the parasite. We report here the presence of a membrane-bound PTPase in Leishmania major promastigotes. We detected differences in the PTPases present in the procyclic and metacyclic stages of promastigotes. In metacyclic promastigotes, the PTPase activity was totally inhibited by specific PTPase and serine/threonine inhibitors, whereas in procyclic promastigotes the PTPase activity was inhibited only with PTPase inhibitors. Two antibodies against the catalytic domains of the human placental PTPase1B and a PTPase from Trypanosoma brucei cross-reacted with a 55–60 kDa molecule present in the soluble detergent-extracted fraction of a Leishmania homogenate. Metacyclic promastigotes expressed more of this molecule than parasites in the procyclic stage. Yet the specific activity of the enzyme was lower in metacyclic than in procyclic promastigotes. Ultrastructural localization of the enzyme showed that it was more membrane-associated in metacyclic promastigotes, whereas in procyclic promastigotes it was scattered throughout the cytoplasm. This is the first demonstration of a PTPase present in Leishmania major promastigotes that differs in expression, activity and ultrastructural localization between the procyclic and metacyclic stages of the parasite's life-cycle.

Keywords

Leishmania majorprocyclic and metacyclic promastigotesprotein tyrosine phosphatase
Type
Research Article
Information
Parasitology , Volume 132 , Issue 5 , May 2006 , pp. 641 - 649
Copyright
2006 Cambridge University Press

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