Proteomic analysis of phytopathogenic fungus Botrytis cinerea as a potential tool for identifying pathogenicity factors, therapeutic targets and for basic research

• Published in: Archives of microbiology Vol. 187; no. 3; pp. 207 - 215
• Main Authors: Fernández-Acero, Francisco Javier, Jorge, Inmaculada, Calvo, Enrique, Vallejo, Inmaculada, Carbú, María, Camafeita, Emilio, Garrido, Carlos, López, Juan Antonio, Jorrin, Jesús, Cantoral, Jesús Manuel
• Format: Journal Article
• Language: English
• Published: Heidelberg Berlin/Heidelberg : Springer-Verlag 01.03.2007; Berlin Springer; Springer Nature B.V
• Subjects: Analytical, structural and metabolic biochemistry; Bacteria; Biological and medical sciences; Botrytis - chemistry; Botrytis - genetics; Botrytis - pathogenicity; Botrytis cinerea; Fruits; Fundamental and applied biological sciences. Psychology; Fungal phytopathogen; Fungal Proteins - analysis; Fungal Proteins - chemistry; Fungal proteomics; Gene Expression Regulation, Fungal - genetics; Genes, Fungal - physiology; Microbiology; Miscellaneous; Mycology; Proteins; Proteome - analysis; Proteome - chemistry; virulence; Virulence Factors - isolation & purification; Fungi; Pathogenicity; Botrytis cinerea; Plant pathogen; Botrytis cinerea,Fungal phytopathogen; Virulence; Proteomics; Fungal proteomics,Virulence factor; Fungi Imperfecti; Thallophyta
• ISSN: 0302-8933; 1432-072X
• DOI: 10.1007/s00203-006-0188-3

Botrytis cinerea is a phytopathogenic fungus causing disease in a substantial number of economically important crops. In an attempt to identify putative fungal virulence factors, the two-dimensional gel electrophoresis (2-DE) protein profile from two B. cinerea strains differing in virulence and toxin production were compared. Protein extracts from fungal mycelium obtained by tissue homogenization were analyzed. The mycelial 2-DE protein profile revealed the existence of qualitative and quantitative differences between the analyzed strains. The lack of genomic data from B. cinerea required the use of peptide fragmentation data from MALDI-TOF/TOF and ESI ion trap for protein identification, resulting in the identification of 27 protein spots. A significant number of spots were identified as malate dehydrogenase (MDH) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The different expression patterns revealed by some of the identified proteins could be ascribed to differences in virulence between strains. Our results indicate that proteomic analysis are becoming an important tool to be used as a starting point for identifying new pathogenicity factors, therapeutic targets and for basic research on this plant pathogen in the postgenomic era.