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Membrane-bound acid phosphatase (MAP) from Entamoeba histolytica has phosphotyrosine phosphatase activity and disrupts the actin cytoskeleton of host cells

Published online by Cambridge University Press:  10 March 2003

M. M. AGUIRRE-GARCÍA
Affiliation:
Experimental Pathology Department, Center for Research and Advanced Studies, IPN, Ave. IPN No. 2508, Col. San Pedro Zacatenco, México, D.F. 07360, México Present address: Experimental Medicine, School of Medicine, UNAM, México, D.F. 06726, México.
M. ANAYA-RUIZ
Affiliation:
Experimental Pathology Department, Center for Research and Advanced Studies, IPN, Ave. IPN No. 2508, Col. San Pedro Zacatenco, México, D.F. 07360, México
P. TALAMÁS-ROHANA
Affiliation:
Experimental Pathology Department, Center for Research and Advanced Studies, IPN, Ave. IPN No. 2508, Col. San Pedro Zacatenco, México, D.F. 07360, México

Abstract

Protein tyrosine phosphatases (PTPases) have been described as virulence factors in different pathogenic microorganisms. The pathogenic process by Entamoeba histolytica is a multifactorial phenomenon that occurs in 3 steps: adhesion, cytolytic and cytotoxic effect, and phagocytosis. Lytic enzymes may participate during the second part of this process. In this work, we determined that purified membrane-bound acid phosphatase (MAP) from E. histolytica trophozoites has PTPase activity. The enzyme specifically dephosphorylated O-phospho-L-tyrosine at optimum pH of 5·0, with little activity towards O-phospho-L-serine, O-phospho-L-threonine, and ATP. It was inhibited by ammonium molybdate and sodium tungstate, and trifluoperazine did not show any effect. A monoclonal antibody against the catalytic domain of the human placental PTPase 1B, cross-reacted with a 55 kDa molecule present in the solubilized fraction. The interaction of the amoebic PTPase with HeLa cells resulted in the alteration of the cell actin cytoskeleton by disruption of the actin stress fibres.

Type
Research Article
Copyright
2003 Cambridge University Press

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