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Title: | Disclosing proteins in the leaves of cork oak plants associated with the immune response to Phytophthora cinnamomi inoculation in the roots: A long-term proteomics approach | Authors: | Coelho, Ana Cristina Pires, Rosa Schütz, Gabriela Santa, Cátia Manadas, Bruno Pinto, Patrícia |
Issue Date: | 2021 | Publisher: | Public Library of Science | Project: | UID/Multi/00631/2013 UID/Multi/00631/2019 UIDB/00631/2020 UIDB/04326/2020 SFRH/BPD/ 84033/2012 ALG-01-0247-FEDER-037303 DL57/2016/CP1361/CT0015 POCI-01-0145-FEDER-007440 POCI-01-0145-FEDER-016428 POCI-01-0145- FEDER-029311 POCI-01-0145-FEDER-30943 PTDC/MED-NEU/27946/2017 POCI-01-0145-FEDER-402-022125 |
Serial title, monograph or event: | PLoS ONE | Volume: | 16 | Issue: | 1 | Abstract: | The pathological interaction between oak trees and Phytophthora cinnamomi has implications in the cork oak decline observed over the last decades in the Iberian Peninsula. During host colonization, the phytopathogen secretes effector molecules like elicitins to increase disease effectiveness. The objective of this study was to unravel the proteome changes associated with the cork oak immune response triggered by P. cinnamomi inoculation in a long-term assay, through SWATH-MS quantitative proteomics performed in the oak leaves. Using the Arabidopis proteome database as a reference, 424 proteins were confidently quantified in cork oak leaves, of which 80 proteins showed a p-value below 0.05 or a fold-change greater than 2 or less than 0.5 in their levels between inoculated and control samples being considered as altered. The inoculation of cork oak roots with P. cinnamomi increased the levels of proteins associated with protein-DNA complex assembly, lipid oxidation, response to endoplasmic reticulum stress, and pyridine-containing compound metabolic process in the leaves. In opposition, several proteins associated with cellular metabolic compound salvage and monosaccharide catabolic process had significantly decreased abundances. The most significant abundance variations were observed for the Ribulose 1,5-Bisphosphate Carboxylase small subunit (RBCS1A), Heat Shock protein 90-1 (Hsp90-1), Lipoxygenase 2 (LOX2) and Histone superfamily protein H3.3 (A8MRLO/At4G40030) revealing a pertinent role for these proteins in the host-pathogen interaction mechanism. This work represents the first SWATH-MS analysis performed in cork oak plants inoculated with P. cinnamomi and highlights host proteins that have a relevant action in the homeostatic states that emerge from the interaction between the oomycete and the host in the long term and in a distal organ. | URI: | https://hdl.handle.net/10316/105363 | ISSN: | 1932-6203 | DOI: | 10.1371/journal.pone.0245148 | Rights: | openAccess |
Appears in Collections: | I&D CNC - Artigos em Revistas Internacionais IIIUC - Artigos em Revistas Internacionais |
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journal.pone.0245148.pdf | 1.37 MB | Adobe PDF | View/Open |
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