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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Detalles Bibliográficos
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
Descripción
Sumario: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.