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Antiamoebic Activity of Petiveria alliacea Leaves and Their Main Component, Isoarborinol
( Lizeth M. Zavala-ocampo ),( Eva Aguirre-hernandez ),( Nury Perez-hernandez ),( Gildardo Rivera ),( Laurence A. Marchat ),( Esther Ramirez-moreno ) 한국미생물생명공학회(구 한국산업미생물학회) 2017 Journal of microbiology and biotechnology Vol.27 No.8
Petiveria alliacea L. (Phytolacaceae) is a medicinal plant with a broad range of traditional therapeutic properties, including the treatment of dysentery and intestinal infections caused by protozoan parasites. However, its effects against Entamoeba histolytica have not been reported yet. We investigated the antiamoebic activity present in the leaves of P. alliacea Antiamoebic activity was evaluated in methanolic and aqueous extracts, as well as in the hexanic, methanolic, and EtOAc fractions. The P. alliacea methanolic extract showed a better antiamoebic activity than the aqueous extract with an IC<sub>50</sub> = 0.51 mg/ml. Likewise, the hexanic fraction was the most effective fraction, showing a dose-dependent activity against E. histolytica, with an IC<sub>50</sub> = 0.68 mg/ml. Hexanic subfraction 12-19 showed the highest antiamoebic activity at 0.8 mg/ml, producing 74.3% growth inhibition without any toxicity in mammal cells. A major component in subfraction 12-19 was identified as isoarborinol, which produced 51.4% E. histolytica growth inhibition at 0.05 mg/ml without affecting mammal cells. The P. alliacea leaf extract has antiamoebic activity that can be attributed to a major metabolite known as isoarborinol.
Silencing the cleavage factor CFIm25 as a new strategy to control Entamoeba histolytica parasite
Juan David Ospina-Villa,Nancy Guillén,Ce´sar Lo´pez-Camarillo,Jacqueline Soto-Sanchez,Esther Ramirez-Moreno,Raul Garcia-Vazquez,Carlos A. Castañon-Sanchez,Abigail Betanzos,Laurence A.Marchat 한국미생물학회 2017 The journal of microbiology Vol.55 No.10
The 25 kDa subunit of the Clevage Factor Im (CFIm25) is an essential factor for messenger RNA polyadenylation in human cells. Therefore, here we investigated whether the homologous protein of Entamoeba histolytica, the protozoan responsible for human amoebiasis, might be considered as a biochemical target for parasite control. Trophozoites were cultured with bacterial double-stranded RNA molecules targeting the EhCFIm25 gene, and inhibition of mRNA and protein expression was confirmed by RT-PCR and Western blot assays, respectively. EhCFIm25 silencing was associated with a significant acceleration of cell proliferation and cell death. Moreover, trophozoites appeared as larger and multinucleated cells. These morphological changes were accompanied by a reduced mobility, and erythrophagocytosis was significantly diminished. Lastly, the knockdown of EhCFIm25 affected the poly(A) site selection in two reporter genes and revealed that EhCFIm25 stimulates the utilization of downstream poly(A) sites in E. histolytica mRNA. Overall, our data confirm that targeting the polyadenylation process represents an interesting strategy for controlling parasites, including E. histolytica. To our best knowledge, the present study is the first to have revealed the relevance of the cleavage factor CFIm25 as a biochemical target in parasites.