Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000

According to molecular biology, genomic and proteo- mic data, the phytopathogenic gamma-proteobacte- rium Pseudomonas syringae pv. tomato DC3000 pro-duces a number of proteins that may promote infec- tion and draw nutrients from plants. Remarkably, P. syringae DC3000 strain possesses three paralogou...

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Autores: Elkhalfi, Bouchra, Serrano Delgado, Aurelio, Soukri, Abdelaziz
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/69286
Acceso en línea:https://hdl.handle.net/11441/69286
https://doi.org/10.4236/abb.2014.53026
Access Level:acceso abierto
Palabra clave:Infective State
Gene Expression
MALDI-TOF
Bacterial Speak
RNA
Secretome
GAPDH
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spelling Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000Elkhalfi, BouchraSerrano Delgado, AurelioSoukri, AbdelazizInfective StateGene ExpressionMALDI-TOFBacterial SpeakRNASecretomeGAPDHAccording to molecular biology, genomic and proteo- mic data, the phytopathogenic gamma-proteobacte- rium Pseudomonas syringae pv. tomato DC3000 pro-duces a number of proteins that may promote infec- tion and draw nutrients from plants. Remarkably, P. syringae DC3000 strain possesses three paralogous gap genes encoding glyceraldehyde-3-phosphate dehy- drogenase (GAPDH) enzymes with different predic- ted molecular sizes and metabolic functions. As GAPDH was shown to be a virulence factor in other microbial pathogens, in the current study, we analyzed the ex-pression levels of each paralogous gap gene by real- time PCR to understand the actual impact of their protein products on P. syringae virulence. We found that all of them were strongly induced during the in-fection process. Nevertheless, proteomic analysis of cul- ture supernatants revealed that only Class I GAPDH1 encoded by the gap1 gene was identified as an extra-cellular protein in infective cells. These results strongly suggest that this GAPDH should play a role in the infective process, including its well-know en-zymatic function in the glycolytic metabolic pathway.España AECID (MAEC) A1/043076/11Scientific Research PublishingBioquímica Vegetal y Biología MolecularAgencia Española de Cooperación Internacional para el Desarrollo (AECID)2014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/69286https://doi.org/10.4236/abb.2014.53026reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésAdvances in Bioscience and Biotechnology, 5, 201-208.A1/043076/11http://dx.doi.org/10.4236/abb.2014.53026info:eu-repo/semantics/openAccessoai:idus.us.es:11441/692862026-06-17T12:51:07Z
dc.title.none.fl_str_mv Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
title Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
spellingShingle Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
Elkhalfi, Bouchra
Infective State
Gene Expression
MALDI-TOF
Bacterial Speak
RNA
Secretome
GAPDH
title_short Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
title_full Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
title_fullStr Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
title_full_unstemmed Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
title_sort Identification of an extracellular infection-induced glyceraldehyde-3-phosphate dehydrogenase of the phytopathogenic proteobacterium Pseudomonas syringae pv tomato DC3000
dc.creator.none.fl_str_mv Elkhalfi, Bouchra
Serrano Delgado, Aurelio
Soukri, Abdelaziz
author Elkhalfi, Bouchra
author_facet Elkhalfi, Bouchra
Serrano Delgado, Aurelio
Soukri, Abdelaziz
author_role author
author2 Serrano Delgado, Aurelio
Soukri, Abdelaziz
author2_role author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Agencia Española de Cooperación Internacional para el Desarrollo (AECID)
dc.subject.none.fl_str_mv Infective State
Gene Expression
MALDI-TOF
Bacterial Speak
RNA
Secretome
GAPDH
topic Infective State
Gene Expression
MALDI-TOF
Bacterial Speak
RNA
Secretome
GAPDH
description According to molecular biology, genomic and proteo- mic data, the phytopathogenic gamma-proteobacte- rium Pseudomonas syringae pv. tomato DC3000 pro-duces a number of proteins that may promote infec- tion and draw nutrients from plants. Remarkably, P. syringae DC3000 strain possesses three paralogous gap genes encoding glyceraldehyde-3-phosphate dehy- drogenase (GAPDH) enzymes with different predic- ted molecular sizes and metabolic functions. As GAPDH was shown to be a virulence factor in other microbial pathogens, in the current study, we analyzed the ex-pression levels of each paralogous gap gene by real- time PCR to understand the actual impact of their protein products on P. syringae virulence. We found that all of them were strongly induced during the in-fection process. Nevertheless, proteomic analysis of cul- ture supernatants revealed that only Class I GAPDH1 encoded by the gap1 gene was identified as an extra-cellular protein in infective cells. These results strongly suggest that this GAPDH should play a role in the infective process, including its well-know en-zymatic function in the glycolytic metabolic pathway.
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/69286
https://doi.org/10.4236/abb.2014.53026
url https://hdl.handle.net/11441/69286
https://doi.org/10.4236/abb.2014.53026
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Advances in Bioscience and Biotechnology, 5, 201-208.
A1/043076/11
http://dx.doi.org/10.4236/abb.2014.53026
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Scientific Research Publishing
publisher.none.fl_str_mv Scientific Research Publishing
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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