Abstract
The proteins of Coriolus versicolor treated with the acetone extracts of Cinnamomum camphora xylem has been investigated. The specific proteins found in the extract treated C. 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 of C. camphora and indicate the way for the development of wood preservatives based on natural extracts.
Acknowledgments
This research was supported by the Natural Science Foundation of China (No. 31760191) and Fujian Agriculture and Forestry University of Science and Technology Innovation Fund Project (No. CXZX2016007).
Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Research funding: None declared.
Employment or leadership: None declared.
Honorarium: None declared.
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