Scarcella S

References (3)

Title : A Single Nucleotide Polymorphism Translates into a Radical Amino Acid Substitution at the Ligand-Binding Site in Fasciola hepatica Carboxylesterase B - Miranda-Miranda_2022_Genes.(Basel)_13_
Author(s) : Miranda-Miranda E , Scarcella S , Reynaud E , Narvaez-Padilla V , Neira G , Mera YSR , Aguilar-Diaz H , Cossio-Bayugar R
Ref : Genes (Basel) , 13 : , 2022
Abstract : Fasciola hepatica anthelmintic resistance may be associated with the catalytic activity of xenobiotic metabolizing enzymes. The gene expression of one of these enzymes, identified as carboxylesterase B (CestB), was previously described as inducible in adult parasites under anthelmintic treatment and exhibited a single nucleotide polymorphism at position 643 that translates into a radical amino acid substitution at position 215 from Glutamic acid to Lysine. Alphafold 3D models of both allelic sequences exhibited a significant affinity pocket rearrangement and different ligand-docking modeling results. Further bioinformatics analysis confirmed that the radical amino acid substitution is located at the ligand affinity site of the enzyme, affecting its affinity to serine hydrolase inhibitors and preferences for ester ligands. A field genotyping survey from parasite samples obtained from two developmental stages isolated from different host species from Argentina and Mexico exhibited a 37% allele distribution for 215E and a 29% allele distribution for 215K as well as a 34% E/K heterozygous distribution. No linkage to host species or geographic origin was found in any of the allele variants.
ESTHER : Miranda-Miranda_2022_Genes.(Basel)_13_
PubMedSearch : Miranda-Miranda_2022_Genes.(Basel)_13_
PubMedID: 36292784
Gene_locus related to this paper: fashe-a0a4e0s0j7

Title : Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B - Pedroza-Gomez_2021_Pathogens_10_1454
Author(s) : Pedroza-Gomez YJ , Cossio-Bayugar R , Aguilar-Diaz H , Scarcella S , Reynaud E , Sanchez-Carbente MDR , Narvaez-Padilla V , Miranda-Miranda E
Ref : Pathogens , 10 :1454 , 2021
Abstract : Bioinformatics analysis of the complete transcriptome of Fasciola hepatica, identified a total of ten putative carboxylesterase transcripts, including a 3146 bp mRNA transcript coding a 2205 bp open reading frame that translates into a protein of 735 amino acids, resulting in a predicted protein mass of 83.5 kDa and a putative carboxylesterase B enzyme. The gene coding for this enzyme was found in two reported F. hepatica complete genomes stretching 23,230 bp, containing two exons of 1282 and 1864 bp, respectively, as well as a 20,084 bp intron between the exons. The enzymatic activity was experimentally assayed on F. hepatica protein extracts by SDS-PAGE zymograms using synthetic chromogenic substrates, confirming both the theoretical molecular weight and carboxylesterase enzymatic activity. Further bioinformatics predicted that this enzyme is an integral component of the cellular membrane that should be active as a 167 kDa homodimer complex and polyacrylamide gel electrophoresis (PAGE) zymograms experiments confirmed the analysis. Additional bioinformatics analysis showed that DNA sequences that code for this particular enzyme are highly conserved in other parasitic trematodes, although they are labeled hypothetical proteins.
ESTHER : Pedroza-Gomez_2021_Pathogens_10_1454
PubMedSearch : Pedroza-Gomez_2021_Pathogens_10_1454
PubMedID: 34832612
Gene_locus related to this paper: fashe-a0a4e0s0j7 , fashe-a0a2h1cec8 , fashe-a0a2h1cpf2 , fashe-a0a4e0s092 , fashe-a0a4e0rpg5 , fashe-a0a4e0rjz9 , fashe-a0a2h1cvt6

Title : Increase of carboxylesterase activity in Fasciola hepatica recovered from triclabendazole treated sheep - Scarcella_2012_Mol.Biochem.Parasitol_185_151
Author(s) : Scarcella S , Miranda-Miranda E , Cossio-Bayugar R , Ceballos L , Fernandez V , Solana H
Ref : Molecular & Biochemical Parasitology , 185 :151 , 2012
Abstract : In the present work we evaluate in vivo the activity of carboxylesterase of Fasciola hepatica exposed to triclabendazole We observed a statistically significant increase in enzyme activity at 24 and 48h post treatment P<0.01 and P<0.001 respectively The zymogram of cytosolic fractions identified a protein of 170kDa containing the carboxylesterase activity The densitograms of the zymograms confirmed the phenomenon of enzyme induction under the experimental conditions of the assay These results provide not only the understanding of the importance of this metabolic pathway in flukes but carboxylesterase would also be an enzyme that could participate more actively in the development of anthelmintic resistance at TCBZ.
ESTHER : Scarcella_2012_Mol.Biochem.Parasitol_185_151
PubMedSearch : Scarcella_2012_Mol.Biochem.Parasitol_185_151
PubMedID: 22814337