Differential proteome analysis of the extracts from the xylem ofCinnamomum camphorainhibitingCoriolus versicolor

Abstract

AbstractThe proteins ofCoriolus versicolortreated with the acetone extracts ofCinnamomum camphoraxylem has been investigated. The specific proteins found in the extract treatedC. versicolor, were characterized by two-dimensional (2D) gel electrophoresis (2D-GE) and identified by matrix assisted laser desorption ionization (MALDI) combined with tandem time-of-flight microscopy, i.e. TOF-MS/TOF-MS. Most of 474 proteins detected from the pure culture were common metabolic proteins. Nineteen protein spots changed significantly and 17 spots were identified successfully. The 19 proteins were assigned to 10 functional groups including ion binding, translation factor activity, nucleic acid binding and ATPase activity. These proteins are involved in signal transduction, transport and membrane trafficking. The down regulated expression of translation elongation factor 1 alpha (EF1α), α-tubulin, and tropomyosin-1 showed that protein translation elongation, growth-stimulating signal transduction, signal transduction and material transport were suppressed, which resulted in the apoptosis of the pathogen. These findings provide a better understanding of the anti-fungal mechanism ofC. camphoraand indicate the way for the development of wood preservatives based on natural extracts.