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Originally published In Press as doi:10.1074/mcp.M600179-MCP200 on December 28, 2006.
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Molecular & Cellular Proteomics 6:425-438, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Crucial Role of Antioxidant Proteins and Hydrolytic Enzymes in Pathogenicity of Penicillium expansum

Analysis Based on Proteomics Approach*,S

Guozheng Qin, Shiping Tian{ddagger}, Zhulong Chan and Boqiang Li

From the Key Laboratory of Photosynthesis and Environmental Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China

Penicillium expansum, a widespread filamentous fungus, is a major causative agent of fruit decay and may lead to the production of mycotoxin that causes harmful effects on human health. In this study, we compared the cellular and extracellular proteomes of P. expansum in the absence and presence of borate, which affects the virulence of the fungal pathogen. The differentially expressed proteins were identified using ESI-Q-TOF-MS/MS. Several proteins related to stress response (glutathione S-transferase, catalase, and heat shock protein 60) and basic metabolism (glyceraldehyde-3-phosphate dehydrogenase, dihydroxy-acid dehydratase, and arginase) were identified in the cellular proteome. Catalase and glutathione S-transferase, the two antioxidant enzymes, exhibited reduced levels of expression upon exposure to borate. Because catalase and glutathione S-transferase are related to oxidative stress response, we further investigated the reactive oxygen species (ROS) levels and oxidative protein carbonylation (damaged proteins) in P. expansum. Higher amounts of ROS and carbonylated proteins were observed after borate treatment, indicating that catalase and glutathione S-transferase are important in scavenging ROS and protecting cellular proteins from oxidative damage. Additionally to find secretory proteins that contribute to the virulence, we studied the extracellular proteome of P. expansum under stress condition with reduced virulence. The expression of three protein spots were repressed in the presence of borate and identified as the same hydrolytic enzyme, polygalacturonase.

{ddagger} To whom correspondence should be addressed: Key Laboratory of Photosynthesis and Environmental Molecular Physiology, Inst. of Botany, Chinese Academy of Sciences, 20 Nanxincun, Xiangshan, Haidian District, Beijing 100093, China. Tel.: 86-10-62836559; Fax: 86-10-82594675; E-mail: tsp{at}ibcas.ac.cn


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This article has been cited by other articles:


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[Abstract] [Full Text] [PDF]


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Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.