Proteomics offers insight to the mechanism behind Pisum sativum L. response to pea seed-borne mosaic virus (PSbMV)

0486069 - BFÚ 2018 RIV NL eng J - Journal Article
Černá, H. - Černý, M. - Habanová, H. - Šafářová, D. - Abushamsiya, K. - Navrátil, M. - Brzobohatý, Břetislav
Proteomics offers insight to the mechanism behind Pisum sativum L. response to pea seed-borne mosaic virus (PSbMV).
Journal of Proteomics. Roč. 153, FEB2017 (2017), s. 78-88. ISSN 1874-3919. E-ISSN 1876-7737
Institutional support: RVO:68081707
Keywords : Proteome * Pea seed-borne mosaic virus PSbMV * Potyvirus
OECD category: Biochemistry and molecular biology
Impact factor: 3.722, year: 2017

Pea seed-borne mosaic virus (PSbMV) significantly reduces yields in a broad spectra of legumes. The eukaryotic translation initiation factor has been shown to confer resistance to this pathogen, thus implying that translation and proteome dynamics play a role in resistance. This study presents the results of a proteome-wide analysis of Pisum sativum L response to PSbMV infection. LC-MS profiling of two contrasting pea cultivars, resistant (B99) and susceptible (Raman) to PSbMV infection, detected >2300 proteins, 116 of which responded to PSbMV ten and/or twenty days post-inoculation. These differentially abundant proteins are involved in number of processes that have previously been reported in the plant-pathogen response, including protein and amino acid metabolism, stress signaling, redox homeostasis, carbohydrate metabolism, and lipid metabolism. We complemented our proteome-wide analysis work with targeted analyses of free amino acids and selected small molecules, fatty acid profiling, and enzyme activity assays. Data from these additional experiments support our findings and validate the biological relevance of the observed proteome changes. We found surprising similarities in the resistant and susceptible cultivars, which implies that a seemingly unaffected plant, with no detectable levels of PSbMV, actively suppresses viral replication.
Permanent Link: http://hdl.handle.net/11104/0280956