Abstract
Protein phosphorylation and membrane proteins play an important role in the infection of plants by phytopathogenic fungi, given their involvement in signal transduction cascades. Botrytis cinerea is a well-studied necrotrophic fungus taken as a model organism in fungal plant pathology, given its broad host range and adverse economic impact. To elucidate relevant events during infection, several proteomics analyses have been performed in B. cinerea, but they cover only 10% of the total proteins predicted in the genome database of this fungus. To increase coverage, we analysed by LC-MS/MS the first-reported overlapped proteome in phytopathogenic fungi, the “phosphomembranome” of B. cinerea, combining the two most important signal transduction subproteomes. Of the 1112 membrane-associated phosphoproteins identified, 64 and 243 were classified as exclusively identified or overexpressed under glucose and deproteinized tomato cell wall conditions, respectively. Seven proteins were found under both conditions, but these presented a specific phosphorylation pattern, so they were considered as exclusively identified or overexpressed proteins. From bioinformatics analysis, those differences in the membrane-associated phosphoproteins composition were associated with various processes, including pyruvate metabolism, unfolded protein response, oxidative stress response, autophagy and cell death. Our results suggest these proteins play a significant role in the B. cinerea pathogenic cycle.
Highlights
Botrytis cinerea is one of the most destructive phytopathogenic fungi[1,2] since it can infect a wide range of commercial crops
The differences identified in the composition of membrane-associated phosphoproteins in each assayed condition may indicate the relative importance of the regulation of particular factors - the pyruvate metabolism, unfolded protein response (UPR), oxidative stress response, autophagy and cell death during the infection process of B. cinerea
Differences in the phosphomembranome of B. cinerea were analysed using mycelium harvested under two different pathogenicity stages: glucose (GLU) as a constitutive stage, and deproteinized tomato cell wall (TCW) as a virulence inductor, as has been previously described[11,12]
Summary
Botrytis cinerea is one of the most destructive phytopathogenic fungi[1,2] since it can infect a wide range of commercial crops. It has been established that, among the known post-translational modification (PTM) processes, phosphorylation is the main mechanism of signal transduction and modification of enzymatic activity in living organisms[14] This PTM has been reported to have an important role in infection processes of fungal plant pathogens, including B. cinerea[13,15]. For the first time, we present a combined analysis of both subproteomes ( jointly named the “phosphomembranome”), with the objectives of increasing the coverage of membrane proteins identified, and of elucidating the main components of the transduction pathways that control the infection process Towards these goals, we have analysed the phosphorylation of membranome proteins in B. cinerea under different virulence conditions, induced by plant-based elicitors, including glucose (GLU) as a constitutive stage, and deproteinized tomato cell wall (TCW) as a virulence inductor. The differences identified in the composition of membrane-associated phosphoproteins in each assayed condition may indicate the relative importance of the regulation of particular factors - the pyruvate metabolism, unfolded protein response (UPR), oxidative stress response, autophagy and cell death during the infection process of B. cinerea
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
