Open AccessProtein Phosphatase PP2C Identification in Entamoeba spp
Author(s) -
Abril Navarrete-Mena,
Judith PachecoYépez,
Verónica Ivonne HernándezRamírez,
Alma Reyna EscalonaMontaño,
Jenny Nancy Gómez-Sandoval,
Mario Néquiz,
Bibiana Chávez-Munguı́a,
Emiliano Tesoro-Cruz,
Patricia TalamásRohana,
María Magdalena AguirreGarcía
Publication year - 2021
Publication title -
biomed research international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 126
eISSN - 2314-6141
pISSN - 2314-6133
DOI - 10.1155/2021/5746629
Subject(s) - entamoeba histolytica , entamoeba , dispar , biology , acid phosphatase , phosphatase , microbiology and biotechnology , enzyme , biochemistry
Entamoeba histolytica is the causative agent of amoebiasis, and Entamoeba dispar is its noninvasive morphological twin. Entamoeba invadens is a reptilian parasite. In the present study, Western blot, phosphatase activity, immunofluorescence, and bioinformatic analyses were used to identify PP2C phosphatases of E. histolytica , E. dispar , and E. invadens. PP2C was identified in trophozoites of all Entamoeba species and cysts of E. invadens . Immunoblotting using a Leishmania mexicana anti-PP2C antibody recognized a 45.2 kDa PP2C in all species. In E. histolytica and E. invadens , a high molecular weight element PP2C at 75 kDa was recognized, mainly in cysts of E. invadens . Immunofluorescence demonstrated the presence of PP2C in membrane and vesicular structures in the cytosol of all species analyzed. The ~75 kDa PP2C of Entamoeba spp. shows the conserved domain characteristic of phosphatase enzymes (according to in silico analysis). Possible PP2C participation in the encystation process was discussed.
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