title: An ecto-protein tyrosine phosphatase of Entamoeba histolytica induces cellular detachment by disruption of actin filaments in HeLa cells.
abstract: Actin cytoskeleton disruption in host cells has been demonstrated for PTPases from pathogenic microorganisms. In this work, we analysed whether the secreted acid phosphatase from Entamoeba histolytica has phosphotyrosine phosphatase activity and the possibility that this activity may participate in damaging host cells. The secreted acid phosphatase of E. histolytica, which catalyses p-nitrophenyl phosphate hydrolysis at acid pH values, was found to have phosphotyrosine phosphatase activity. The enzymatic properties of phosphotyrosine phosphatase and acid phosphatase were virtually identical and included: Km values of 10 x 10(-4) M, no requirement for divalent cations, and sensitivity to molybdate, vanadate, and tungstate. The phosphotyrosyl phosphatase activity caused significant levels of cell rounding and detachment correlating with disruption of the actin stress fibres in HeLa cells. Thus, our data suggest that secreted phosphotyrosine phosphatase could play a cytotoxic role during amoebic infection.
authors.affiliation: Experimental Pathology Department, Center for Research and Advanced Studies, Avenue IPN No 2508, Col. San Pedro Zacatenco, Mexico DF 07360, Mexico.
authors.forename: M
authors.initials: M
authors.lastname: Anaya-Ruiz
authors.forename: J L M
authors.initials: JL
authors.lastname: Pérez-Santos
authors.forename: P
authors.initials: P
authors.lastname: Talamás-Rohana
mesh_terms: D008841:Actin Cytoskeleton / Q000648:ultrastructure; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D016923:Cell Death; D004748:Entamoeba histolytica / Q000201:enzymology / Q000472:pathogenicity*; D006367:HeLa Cells / Q000469:parasitology* / Q000648:ultrastructure; D006790:Host-Parasite Interactions; D006801:Humans; D010920:Placenta / Q000201:enzymology; D011233:Precipitin Tests / Q000379:methods; D017027:Protein Tyrosine Phosphatases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D015800:Protozoan Proteins / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D015800:Protozoan Proteins; D017027:Protein Tyrosine Phosphatases