TY - JOUR
T1 - Protein Phosphatase PP2C Identification in Entamoeba spp
AU - Navarrete-Mena, Abril
AU - Pacheco-Yépez, Judith
AU - Hernández-Ramírez, Verónica Ivonne
AU - Escalona-Montaño, Alma Reyna
AU - Gómez-Sandoval, Jenny Nancy
AU - Néquiz-Avendaño, Mario
AU - Chávez-Munguía, Bibiana
AU - Tesoro-Cruz, Emiliano
AU - Talamás-Rohana, Patricia
AU - Aguirre-García, María Magdalena
N1 - Publisher Copyright:
© 2021 Abril Navarrete-Mena et al.
PY - 2021
Y1 - 2021
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85118412211&partnerID=8YFLogxK
U2 - 10.1155/2021/5746629
DO - 10.1155/2021/5746629
M3 - Artículo
C2 - 34697588
AN - SCOPUS:85118412211
SN - 2314-6133
VL - 2021
JO - BioMed Research International
JF - BioMed Research International
M1 - 5746629
ER -