Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B

Autores
Pedroza Gómez, Yaretzi J.; Cossio Bayugar, Raquel; Aguilar Díaz, Hugo; Scarcella, Silvana Andrea; Reynaud, Enrique; del Rayo Sanchez Carbente, María; Narváez Padilla, Verónica; Miranda Miranda, Estefan
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Pedroza Gómez, Yaretzi J.. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Fil: Cossio Bayugar, Raquel. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Fil: Aguilar Díaz, Hugo. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Fil: Scarcella, Silvana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Fil: Reynaud, Enrique. Universidad Nacional Autónoma de México; México
Fil: del Rayo Sanchez Carbente, María. Universidad Nacional Autónoma de México; México
Fil: Narváez Padilla, Verónica. Universidad Nacional Autónoma de México; México
Fil: Miranda Miranda, Estefan. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Materia
BIOINFORMATICS
CARBOXYLESTERASE
FASCIOLOSIS
TRANSCRIPTOME
ZYMOGRAM
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/149487
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/149487
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase BPedroza Gómez, Yaretzi J.Cossio Bayugar, RaquelAguilar Díaz, HugoScarcella, Silvana AndreaReynaud, Enriquedel Rayo Sanchez Carbente, MaríaNarváez Padilla, VerónicaMiranda Miranda, EstefanBIOINFORMATICSCARBOXYLESTERASEFASCIOLOSISTRANSCRIPTOMEZYMOGRAMhttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4Bioinformatics 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.Fil: Pedroza Gómez, Yaretzi J.. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; MéxicoFil: Cossio Bayugar, Raquel. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; MéxicoFil: Aguilar Díaz, Hugo. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; MéxicoFil: Scarcella, Silvana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; ArgentinaFil: Reynaud, Enrique. Universidad Nacional Autónoma de México; MéxicoFil: del Rayo Sanchez Carbente, María. Universidad Nacional Autónoma de México; MéxicoFil: Narváez Padilla, Verónica. Universidad Nacional Autónoma de México; MéxicoFil: Miranda Miranda, Estefan. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; MéxicoMolecular Diversity Preservation International2021-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/149487Pedroza Gómez, Yaretzi J.; Cossio Bayugar, Raquel; Aguilar Díaz, Hugo; Scarcella, Silvana Andrea; Reynaud, Enrique; et al.; Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B; Molecular Diversity Preservation International; Pathogens; 10; 11; 11-2021; 1-122076-0817CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens10111454info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/10/11/1454info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:43Zoai:ri.conicet.gov.ar:11336/149487instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:59:43.836CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
title Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
spellingShingle Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
Pedroza Gómez, Yaretzi J.
BIOINFORMATICS
CARBOXYLESTERASE
FASCIOLOSIS
TRANSCRIPTOME
ZYMOGRAM
title_short Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
title_full Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
title_fullStr Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
title_full_unstemmed Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
title_sort Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B
dc.creator.none.fl_str_mv Pedroza Gómez, Yaretzi J.
Cossio Bayugar, Raquel
Aguilar Díaz, Hugo
Scarcella, Silvana Andrea
Reynaud, Enrique
del Rayo Sanchez Carbente, María
Narváez Padilla, Verónica
Miranda Miranda, Estefan
author Pedroza Gómez, Yaretzi J.
author_facet Pedroza Gómez, Yaretzi J.
Cossio Bayugar, Raquel
Aguilar Díaz, Hugo
Scarcella, Silvana Andrea
Reynaud, Enrique
del Rayo Sanchez Carbente, María
Narváez Padilla, Verónica
Miranda Miranda, Estefan
author_role author
author2 Cossio Bayugar, Raquel
Aguilar Díaz, Hugo
Scarcella, Silvana Andrea
Reynaud, Enrique
del Rayo Sanchez Carbente, María
Narváez Padilla, Verónica
Miranda Miranda, Estefan
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BIOINFORMATICS
CARBOXYLESTERASE
FASCIOLOSIS
TRANSCRIPTOME
ZYMOGRAM
topic BIOINFORMATICS
CARBOXYLESTERASE
FASCIOLOSIS
TRANSCRIPTOME
ZYMOGRAM
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.3
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv 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.
Fil: Pedroza Gómez, Yaretzi J.. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Fil: Cossio Bayugar, Raquel. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Fil: Aguilar Díaz, Hugo. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
Fil: Scarcella, Silvana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Fil: Reynaud, Enrique. Universidad Nacional Autónoma de México; México
Fil: del Rayo Sanchez Carbente, María. Universidad Nacional Autónoma de México; México
Fil: Narváez Padilla, Verónica. Universidad Nacional Autónoma de México; México
Fil: Miranda Miranda, Estefan. Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias; México
description 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.
publishDate 2021
dc.date.none.fl_str_mv 2021-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/149487
Pedroza Gómez, Yaretzi J.; Cossio Bayugar, Raquel; Aguilar Díaz, Hugo; Scarcella, Silvana Andrea; Reynaud, Enrique; et al.; Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B; Molecular Diversity Preservation International; Pathogens; 10; 11; 11-2021; 1-12
2076-0817
CONICET Digital
CONICET
url http://hdl.handle.net/11336/149487
identifier_str_mv Pedroza Gómez, Yaretzi J.; Cossio Bayugar, Raquel; Aguilar Díaz, Hugo; Scarcella, Silvana Andrea; Reynaud, Enrique; et al.; Transcriptome-Based Identification of a Functional Fasciola hepatica Carboxylesterase B; Molecular Diversity Preservation International; Pathogens; 10; 11; 11-2021; 1-12
2076-0817
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens10111454
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/10/11/1454
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269597823139840
score 13.13397

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