Parasitology Research

, Volume 107, Issue 2, pp 309–315

Leishmania mexicana promastigotes secrete a protein tyrosine phosphatase

  • Alma R. Escalona-Montaño
  • Daniel Pardavé-Alejandre
  • Rocely Cervantes-Sarabia
  • Patricia García-López
  • Manuel Gutiérrez-Quiroz
  • Laila Gutiérrez-Kobeh
  • Ingeborg Becker-Fauser
  • Maria M. Aguirre-García
Original Paper

DOI: 10.1007/s00436-010-1863-5

Cite this article as:
Escalona-Montaño, A.R., Pardavé-Alejandre, D., Cervantes-Sarabia, R. et al. Parasitol Res (2010) 107: 309. doi:10.1007/s00436-010-1863-5

Abstract

Leishmania mexicana is an intracellular protozoan parasite that infects macrophages and dendritic cells and causes a chronic cutaneous disease. Although many enzymatic activities have been reported in this parasite, the presence of kinases and phosphatases has been poorly studied. These enzymes control the phosphorylation and dephosphorylation of proteins. Specifically, protein tyrosine kinases phosphorylate tyrosine residues and protein tyrosine phosphatases (PTPases) dephosphorylate tyrosine residues. PTPase activities have been reported as pathogenic factors in various infectious microorganisms such as viruses, bacteria, and parasites. Also, it has been shown that the induction of one or more PTPase activities in macrophages represents an important pathogenicity factor in Leishmania. Recently, we reported a membrane-bound PTPase activity in promastigotes of Leishmania major. In the present work, we give evidence that promastigotes of L. mexicana are able to secrete a PTPase into the culture medium. Two antibodies: one monoclonal against the catalytic domains of the human placental PTPase 1B and a polyclonal rabbit anti-recombinant protein Petase7 from Trypanosoma brucei cross-reacted with a 50-kDa molecule. The anti-human PTPase 1B antibody depleted the enzymatic activity present in the conditioned medium. The pattern of sensitivity and resistance to specific PTPase and serine/threonine inhibitors showed that this enzyme is a protein tyrosine phosphatase.

Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Alma R. Escalona-Montaño
    • 1
  • Daniel Pardavé-Alejandre
    • 1
  • Rocely Cervantes-Sarabia
    • 1
  • Patricia García-López
    • 2
  • Manuel Gutiérrez-Quiroz
    • 3
  • Laila Gutiérrez-Kobeh
    • 1
  • Ingeborg Becker-Fauser
    • 1
  • Maria M. Aguirre-García
    • 1
  1. 1.Departamento de Medicina Experimental, Facultad de MedicinaUniversidad Nacional Autónoma de MéxicoMéxico D.F.México
  2. 2.Laboratorio de Farmacología, Subdirección de Investigación BásicaInstituto Nacional de CancerologíaMéxico D.F.México
  3. 3.Departamento de Microbiología y Parasitología, Facultad de MedicinaUniversidad Nacional Autónoma de MéxicoMéxico D.F.México