TY - JOUR
T1 - The flavonoid (-)-epicatechin affects cytoskeleton proteins and functions in Entamoeba histolytica
AU - Bolaños, Verónica
AU - Díaz-Martínez, Alfredo
AU - Soto, Jacqueline
AU - Rodríguez, Mario A.
AU - López-Camarillo, Cesar
AU - Marchat, Laurence A.
AU - Ramírez-Moreno, Esther
N1 - Publisher Copyright:
© 2014 Elsevier B.V.
PY - 2014/12/5
Y1 - 2014/12/5
N2 - Human amoebiasis is an intestinal disease with a global distribution. Due to reports of parasite resistance or susceptibility reduction to metronidazole treatment, there is a renewed interest for the search of new molecules with antiamoebic activity. The flavonoid (-)-epicatechin that was isolated from the Mexican medicinal plant Geranium mexicanum HBK has an in vitro activity against E. histolytica trophozoites, however its molecular effects have been poorly documented. Using a proteomic approach based on two-dimensional gel electrophoresis and mass spectrometry (ESI-MS/MS) analysis, we evidenced that E. histolytica cytoskeleton proteins exhibit differential abundance in response to (-)-epicatechin treatment. Moreover, functional assays revealed modification on pathogenic mechanisms associated with cytoskeleton functionality, namely, adhesion, migration, phagocytosis and cytolysis. Consequently, these data suggested that (-)-epicatechin could affect virulence properties of this human pathogen. Biological significance: This work contributes with some advances in the action mechanisms involved in the antiamoebic effect of the flavonoid (-)-epicatechin. We found that this flavonoid has an unusual effect on trophozoites growth that is dependent of its concentration. Additionally, we reported that (-)-epicatechin affects mainly amebic cytoskeleton proteins, which results in alteration on important virulence mechanisms, like adhesion, migration, phagocytosis and cytolysis. This study provides new knowledge about a potential alternative therapy directed to the treatment of amoebiasis.This article is part of a Special Issue entitled: Proteomics, mass spectrometry and peptidomics, Cancun 2013. Guest Editors: César López-Camarillo, Victoria Pando-Robles and Bronwyn Jane Barkla.
AB - Human amoebiasis is an intestinal disease with a global distribution. Due to reports of parasite resistance or susceptibility reduction to metronidazole treatment, there is a renewed interest for the search of new molecules with antiamoebic activity. The flavonoid (-)-epicatechin that was isolated from the Mexican medicinal plant Geranium mexicanum HBK has an in vitro activity against E. histolytica trophozoites, however its molecular effects have been poorly documented. Using a proteomic approach based on two-dimensional gel electrophoresis and mass spectrometry (ESI-MS/MS) analysis, we evidenced that E. histolytica cytoskeleton proteins exhibit differential abundance in response to (-)-epicatechin treatment. Moreover, functional assays revealed modification on pathogenic mechanisms associated with cytoskeleton functionality, namely, adhesion, migration, phagocytosis and cytolysis. Consequently, these data suggested that (-)-epicatechin could affect virulence properties of this human pathogen. Biological significance: This work contributes with some advances in the action mechanisms involved in the antiamoebic effect of the flavonoid (-)-epicatechin. We found that this flavonoid has an unusual effect on trophozoites growth that is dependent of its concentration. Additionally, we reported that (-)-epicatechin affects mainly amebic cytoskeleton proteins, which results in alteration on important virulence mechanisms, like adhesion, migration, phagocytosis and cytolysis. This study provides new knowledge about a potential alternative therapy directed to the treatment of amoebiasis.This article is part of a Special Issue entitled: Proteomics, mass spectrometry and peptidomics, Cancun 2013. Guest Editors: César López-Camarillo, Victoria Pando-Robles and Bronwyn Jane Barkla.
KW - (-)-epicatechin
KW - Entamoeba histolytica
KW - Flavonoids
KW - Pathogenicity mechanisms
KW - Proteomic analysis
UR - http://www.scopus.com/inward/record.url?scp=84910089092&partnerID=8YFLogxK
U2 - 10.1016/j.jprot.2014.05.017
DO - 10.1016/j.jprot.2014.05.017
M3 - Artículo
C2 - 24887480
SN - 1874-3919
VL - 111
SP - 74
EP - 85
JO - Journal of Proteomics
JF - Journal of Proteomics
ER -