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Comparative proteomic analysis provides insights into the complex responses to Pseudoperonospora cubensis infection of cucumber (Cucumis sativus L.)
Cucumber (Cucumis sativus L.) is an important crop distributed in many countries. Downy mildew (DM) caused by the obligate oomycete Pseudoperonospora cubensis is especially destructive in cucumber production. So far, few studies on the changes in proteomes during the P. cubensis infection have been...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6603182/ https://www.ncbi.nlm.nih.gov/pubmed/31263111 http://dx.doi.org/10.1038/s41598-019-45111-4 |
Sumario: | Cucumber (Cucumis sativus L.) is an important crop distributed in many countries. Downy mildew (DM) caused by the obligate oomycete Pseudoperonospora cubensis is especially destructive in cucumber production. So far, few studies on the changes in proteomes during the P. cubensis infection have been performed. In the present study, the proteomes of DM-resistant variety ‘ZJ’ and DM-susceptible variety ‘SDG’ under the P. cubensis infection were investigated. In total, 6400 peptides were identified, 5629 of which were quantified. KEGG analysis showed that a number of metabolic pathways were significantly altered under P. cubensis infection, such as terpenoid backbone biosynthesis, and selenocompound metabolism in ZJ, and starch and sucrose metabolism in SDG. For terpenoid backbone synthesis, 1-deoxy-D-xylulose-5-phosphate synthase, 1-deoxy-D-xylulose 5-phosphate reductoisomerase, 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase, and geranylgeranyl pyrophosphate synthase were significantly accumulated in ZJ rather than in SDG, suggesting that pathogen-induced terpenoids accumulation might play an important role in the resistance against P. cubensis infection. Furthermore, a number of pathogenesis-related proteins, such as endochitinases, peroxidases, PR proteins and heat shock proteins were identified as DAPs, suggesting that DM resistance was controlled by a complex network. Our data allowed us to identify and screen more potential proteins related to the DM resistance. |
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