COMPARATIVE PROTEOMICS AND GLYCOPROTEOMICS OF PROTEINS SECRETED FROM B CINEREA

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The fungus Botrytis cinerea is a widespread plant pathogen that affects many vegetables and fruits, as well as a large number of shrubs, trees, flowers, and weeds by causing grey mold or soft rot on the host tissues. B. cinerea mainly infects dicotyledons and non-graminaceous monocotyledons, and the infection not only occurs during the growth phase of crops but also during storage of the harvested products. Thus, it is responsible for significant economic losses. A great deal of research has focused on understanding the B. cinerea infection process, which in turn directs the development of effective prevention strategies. B. cinerea must breach the cell wall during the infection process and accordingly secretes a great number of enzymes that can degrade cell walls. Little is known concerning the identity of these enzymes. The majority of these cell wall degrading enzymes are glycosylated. Although the glycosylation on several recombinant proteins have been characterized, very little is known on the native enzymes, despite the importance of glycosylation on protein structure and activity. To this end, we have started to characterize the secreted proteome and glycoproteome of this fungus.