Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B

Bioinformatics analysis of the complete transcriptome of <i>Fasciola hepatica,</i> 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 pr...

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Autores principales:	Yaretzi J. Pedroza-Gómez, Raquel Cossio-Bayugar, Hugo Aguilar-Díaz, Silvana Scarcella, Enrique Reynaud, María del Rayo Sanchez-Carbente, Verónica Narváez-Padilla, Estefan Miranda-Miranda
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Fasciolosis bioinformatics transcriptome carboxylesterase zymogram Medicine R
Acceso en línea:	https://doaj.org/article/f3aec2c3b99347c1b3927ec80b8cd391
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spelling	oai:doaj.org-article:f3aec2c3b99347c1b3927ec80b8cd3912021-11-25T18:38:23ZTranscriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B10.3390/pathogens101114542076-0817https://doaj.org/article/f3aec2c3b99347c1b3927ec80b8cd3912021-11-01T00:00:00Zhttps://www.mdpi.com/2076-0817/10/11/1454https://doaj.org/toc/2076-0817Bioinformatics analysis of the complete transcriptome of <i>Fasciola hepatica,</i> 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 <i>F. hepatica</i> 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 <i>F. hepatica</i> 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.Yaretzi J. Pedroza-GómezRaquel Cossio-BayugarHugo Aguilar-DíazSilvana ScarcellaEnrique ReynaudMaría del Rayo Sanchez-CarbenteVerónica Narváez-PadillaEstefan Miranda-MirandaMDPI AGarticleFasciolosisbioinformaticstranscriptomecarboxylesterasezymogramMedicineRENPathogens, Vol 10, Iss 1454, p 1454 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Fasciolosis bioinformatics transcriptome carboxylesterase zymogram Medicine R
spellingShingle	Fasciolosis bioinformatics transcriptome carboxylesterase zymogram Medicine R Yaretzi J. Pedroza-Gómez Raquel Cossio-Bayugar Hugo Aguilar-Díaz Silvana Scarcella Enrique Reynaud María del Rayo Sanchez-Carbente Verónica Narváez-Padilla Estefan Miranda-Miranda Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B
description	Bioinformatics analysis of the complete transcriptome of <i>Fasciola hepatica,</i> 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 <i>F. hepatica</i> 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 <i>F. hepatica</i> 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.
format	article
author	Yaretzi J. Pedroza-Gómez Raquel Cossio-Bayugar Hugo Aguilar-Díaz Silvana Scarcella Enrique Reynaud María del Rayo Sanchez-Carbente Verónica Narváez-Padilla Estefan Miranda-Miranda
author_facet	Yaretzi J. Pedroza-Gómez Raquel Cossio-Bayugar Hugo Aguilar-Díaz Silvana Scarcella Enrique Reynaud María del Rayo Sanchez-Carbente Verónica Narváez-Padilla Estefan Miranda-Miranda
author_sort	Yaretzi J. Pedroza-Gómez
title	Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B
title_short	Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B
title_full	Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B
title_fullStr	Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B
title_full_unstemmed	Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B
title_sort	transcriptome-based identification of a functional <i>fasciola hepatica</i> carboxylesterase b
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/f3aec2c3b99347c1b3927ec80b8cd391
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Transcriptome-Based Identification of a Functional <i>Fasciola hepatica</i> Carboxylesterase B

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