Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome

Autores
Marques Da Silva, Wanderson; Bei, Jinlong; Amigo, Natalia; Valacco, Maria Pia; Amadio, Ariel Fernando; Zhang, Qi; Wu, Xiuju; Yu, Ting; Larzabal, Mariano; Chen, Zhuang; Cataldi, Ángel Adrián
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Enterohemorrhagic Escherichia coli (EHEC) O157:H7 is a human pathogen responsible fordiarrhea, hemorrhagic colitis and hemolytic uremic syndrome (HUS). To promote a comprehensiveinsight into the molecular basis of EHEC O157:H7 physiology and pathogenesis,the combined proteome of EHEC O157:H7 strains, Clade 8 and Clade 6 isolated from cattlein Argentina, and the standard EDL933 (clade 3) strain has been analyzed. From shotgunproteomic analysis a total of 2,644 non-redundant proteins of EHEC O157:H7 were identified,which correspond approximately 47% of the predicted proteome of this pathogen. Normalizedspectrum abundance factor analysis was performed to estimate the proteinabundance. According this analysis, 50 proteins were detected as the most abundant ofEHEC O157:H7 proteome. COG analysis showed that the majority of the most abundantproteins are associated with translation processes. A KEGG enrichment analysis revealedthat Glycolysis / Gluconeogenesis was the most significant pathway. On the other hand, theless abundant detected proteins are those related to DNA processes, cell respiration andprophage. Among the proteins that composed the Type III Secretion System, the mostabundant protein was EspA. Altogether, the results show a subset of important proteins thatcontribute to physiology and pathogenicity of EHEC O157:H7.
Fil: Marques Da Silva, Wanderson. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina
Fil: Bei, Jinlong. Guangdong Academy Of Agricultural Sciences; China
Fil: Amigo, Natalia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina
Fil: Valacco, Maria Pia. Universidad de Buenos Aires; Argentina
Fil: Amadio, Ariel Fernando. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Zhang, Qi. Guangdong Academy Of Agricultural Sciences; China
Fil: Wu, Xiuju. Guangdong Academy Of Agricultural Sciences; China
Fil: Yu, Ting. Guangdong Academy Of Agricultural Sciences; China
Fil: Larzabal, Mariano. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Chen, Zhuang. Guangdong Academy Of Agricultural Sciences; China
Fil: Cataldi, Ángel Adrián. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Materia
proteome
E coli
quantitative
Mass spec
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/92824

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteomeMarques Da Silva, WandersonBei, JinlongAmigo, NataliaValacco, Maria PiaAmadio, Ariel FernandoZhang, QiWu, XiujuYu, TingLarzabal, MarianoChen, ZhuangCataldi, Ángel AdriánproteomeE coliquantitativeMass spechttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Enterohemorrhagic Escherichia coli (EHEC) O157:H7 is a human pathogen responsible fordiarrhea, hemorrhagic colitis and hemolytic uremic syndrome (HUS). To promote a comprehensiveinsight into the molecular basis of EHEC O157:H7 physiology and pathogenesis,the combined proteome of EHEC O157:H7 strains, Clade 8 and Clade 6 isolated from cattlein Argentina, and the standard EDL933 (clade 3) strain has been analyzed. From shotgunproteomic analysis a total of 2,644 non-redundant proteins of EHEC O157:H7 were identified,which correspond approximately 47% of the predicted proteome of this pathogen. Normalizedspectrum abundance factor analysis was performed to estimate the proteinabundance. According this analysis, 50 proteins were detected as the most abundant ofEHEC O157:H7 proteome. COG analysis showed that the majority of the most abundantproteins are associated with translation processes. A KEGG enrichment analysis revealedthat Glycolysis / Gluconeogenesis was the most significant pathway. On the other hand, theless abundant detected proteins are those related to DNA processes, cell respiration andprophage. Among the proteins that composed the Type III Secretion System, the mostabundant protein was EspA. Altogether, the results show a subset of important proteins thatcontribute to physiology and pathogenicity of EHEC O157:H7.Fil: Marques Da Silva, Wanderson. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; ArgentinaFil: Bei, Jinlong. Guangdong Academy Of Agricultural Sciences; ChinaFil: Amigo, Natalia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; ArgentinaFil: Valacco, Maria Pia. Universidad de Buenos Aires; ArgentinaFil: Amadio, Ariel Fernando. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; ArgentinaFil: Zhang, Qi. Guangdong Academy Of Agricultural Sciences; ChinaFil: Wu, Xiuju. Guangdong Academy Of Agricultural Sciences; ChinaFil: Yu, Ting. Guangdong Academy Of Agricultural Sciences; ChinaFil: Larzabal, Mariano. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; ArgentinaFil: Chen, Zhuang. Guangdong Academy Of Agricultural Sciences; ChinaFil: Cataldi, Ángel Adrián. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; ArgentinaPublic Library of Science2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/92824Marques Da Silva, Wanderson; Bei, Jinlong; Amigo, Natalia; Valacco, Maria Pia; Amadio, Ariel Fernando; et al.; Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome; Public Library of Science; Plos One; 13; 12; 12-2018; 1-151932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://dx.plos.org/10.1371/journal.pone.0208520info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0208520info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:33:52Zoai:ri.conicet.gov.ar:11336/92824instacron: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:34982025-09-29 09:33:53.045CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
title Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
spellingShingle Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
Marques Da Silva, Wanderson
proteome
E coli
quantitative
Mass spec
title_short Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
title_full Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
title_fullStr Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
title_full_unstemmed Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
title_sort Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome
dc.creator.none.fl_str_mv Marques Da Silva, Wanderson
Bei, Jinlong
Amigo, Natalia
Valacco, Maria Pia
Amadio, Ariel Fernando
Zhang, Qi
Wu, Xiuju
Yu, Ting
Larzabal, Mariano
Chen, Zhuang
Cataldi, Ángel Adrián
author Marques Da Silva, Wanderson
author_facet Marques Da Silva, Wanderson
Bei, Jinlong
Amigo, Natalia
Valacco, Maria Pia
Amadio, Ariel Fernando
Zhang, Qi
Wu, Xiuju
Yu, Ting
Larzabal, Mariano
Chen, Zhuang
Cataldi, Ángel Adrián
author_role author
author2 Bei, Jinlong
Amigo, Natalia
Valacco, Maria Pia
Amadio, Ariel Fernando
Zhang, Qi
Wu, Xiuju
Yu, Ting
Larzabal, Mariano
Chen, Zhuang
Cataldi, Ángel Adrián
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv proteome
E coli
quantitative
Mass spec
topic proteome
E coli
quantitative
Mass spec
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Enterohemorrhagic Escherichia coli (EHEC) O157:H7 is a human pathogen responsible fordiarrhea, hemorrhagic colitis and hemolytic uremic syndrome (HUS). To promote a comprehensiveinsight into the molecular basis of EHEC O157:H7 physiology and pathogenesis,the combined proteome of EHEC O157:H7 strains, Clade 8 and Clade 6 isolated from cattlein Argentina, and the standard EDL933 (clade 3) strain has been analyzed. From shotgunproteomic analysis a total of 2,644 non-redundant proteins of EHEC O157:H7 were identified,which correspond approximately 47% of the predicted proteome of this pathogen. Normalizedspectrum abundance factor analysis was performed to estimate the proteinabundance. According this analysis, 50 proteins were detected as the most abundant ofEHEC O157:H7 proteome. COG analysis showed that the majority of the most abundantproteins are associated with translation processes. A KEGG enrichment analysis revealedthat Glycolysis / Gluconeogenesis was the most significant pathway. On the other hand, theless abundant detected proteins are those related to DNA processes, cell respiration andprophage. Among the proteins that composed the Type III Secretion System, the mostabundant protein was EspA. Altogether, the results show a subset of important proteins thatcontribute to physiology and pathogenicity of EHEC O157:H7.
Fil: Marques Da Silva, Wanderson. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina
Fil: Bei, Jinlong. Guangdong Academy Of Agricultural Sciences; China
Fil: Amigo, Natalia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina
Fil: Valacco, Maria Pia. Universidad de Buenos Aires; Argentina
Fil: Amadio, Ariel Fernando. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Zhang, Qi. Guangdong Academy Of Agricultural Sciences; China
Fil: Wu, Xiuju. Guangdong Academy Of Agricultural Sciences; China
Fil: Yu, Ting. Guangdong Academy Of Agricultural Sciences; China
Fil: Larzabal, Mariano. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
Fil: Chen, Zhuang. Guangdong Academy Of Agricultural Sciences; China
Fil: Cataldi, Ángel Adrián. Instituto Nacional de Tecnología Agropecuaria. Centro Regional Buenos Aires; Argentina
description Enterohemorrhagic Escherichia coli (EHEC) O157:H7 is a human pathogen responsible fordiarrhea, hemorrhagic colitis and hemolytic uremic syndrome (HUS). To promote a comprehensiveinsight into the molecular basis of EHEC O157:H7 physiology and pathogenesis,the combined proteome of EHEC O157:H7 strains, Clade 8 and Clade 6 isolated from cattlein Argentina, and the standard EDL933 (clade 3) strain has been analyzed. From shotgunproteomic analysis a total of 2,644 non-redundant proteins of EHEC O157:H7 were identified,which correspond approximately 47% of the predicted proteome of this pathogen. Normalizedspectrum abundance factor analysis was performed to estimate the proteinabundance. According this analysis, 50 proteins were detected as the most abundant ofEHEC O157:H7 proteome. COG analysis showed that the majority of the most abundantproteins are associated with translation processes. A KEGG enrichment analysis revealedthat Glycolysis / Gluconeogenesis was the most significant pathway. On the other hand, theless abundant detected proteins are those related to DNA processes, cell respiration andprophage. Among the proteins that composed the Type III Secretion System, the mostabundant protein was EspA. Altogether, the results show a subset of important proteins thatcontribute to physiology and pathogenicity of EHEC O157:H7.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
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/11336/92824
Marques Da Silva, Wanderson; Bei, Jinlong; Amigo, Natalia; Valacco, Maria Pia; Amadio, Ariel Fernando; et al.; Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome; Public Library of Science; Plos One; 13; 12; 12-2018; 1-15
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/92824
identifier_str_mv Marques Da Silva, Wanderson; Bei, Jinlong; Amigo, Natalia; Valacco, Maria Pia; Amadio, Ariel Fernando; et al.; Quantification of enterohemorrhagic Escherichia coli O157:H7 protein abundance by high-throughput proteome; Public Library of Science; Plos One; 13; 12; 12-2018; 1-15
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://dx.plos.org/10.1371/journal.pone.0208520
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0208520
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
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
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