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Quantitative proteomics links metabolic pathways to specific developmental stages of the plant-pathogenic oomycete Phytophthora capsici
KTH, School of Biotechnology (BIO), Glycoscience.ORCID iD: 0000-0001-5306-2764
KTH, School of Biotechnology (BIO), Glycoscience.ORCID iD: 0000-0003-1877-4154
KTH, School of Biotechnology (BIO), Glycoscience.
2016 (English)In: Molecular plant pathology, ISSN 1464-6722, E-ISSN 1364-3703Article in journal (Refereed) Published
Abstract [en]

The oomycete Phytophthora capsici is a plant pathogen responsible for important losses to vegetable production worldwide. Its asexual reproduction plays an important role in the rapid propagation and spread of the disease in the field. A global proteomics study was conducted to compare two key asexual life stages of P. capsici, i.e. the mycelium and cysts, to identify stage-specific biochemical processes. A total of 1200 proteins was identified using qualitative and quantitative proteomics. The transcript abundance of some of the enriched proteins was also analysed by quantitative real-time polymerase chain reaction. Seventy-three proteins exhibited different levels of abundance between the mycelium and cysts. The proteins enriched in the mycelium are mainly associated with glycolysis, the tricarboxylic acid (or citric acid) cycle and the pentose phosphate pathway, providing the energy required for the biosynthesis of cellular building blocks and hyphal growth. In contrast, the proteins that are predominant in cysts are essentially involved in fatty acid degradation, suggesting that the early infection stage of the pathogen relies primarily on fatty acid degradation for energy production. The data provide a better understanding of P. capsici biology and suggest potential metabolic targets at the two different developmental stages for disease control. © 2016 BSPP AND JOHN WILEY & SONS LTD.

Place, publisher, year, edition, pages
John Wiley & Sons, 2016.
Keyword [en]
Cysts, Mass spectrometry, Mycelium, Phytophthora capsici, Plant-pathogenic oomycete, Quantitative proteomics
National Category
Biological Sciences
URN: urn:nbn:se:kth:diva-194591DOI: 10.1111/mpp.12406ScopusID: 2-s2.0-84971393355OAI: diva2:1044150

Correspondence Address: Bulone, QC 20161102

Available from: 2016-11-02 Created: 2016-10-31 Last updated: 2016-11-02Bibliographically approved

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Pang, ZhiliSrivastava, VaibhavBulone, Vincent
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