Research Projects
C. Polydnaviral cysteine-rich proteins: role in insect resistance in transgenic plants
This research is concerned with understanding the biochemical mechanisms of polydnaviral-mediated suppression of insect immune defenses and insect growth. We propose to undertake detailed structure-function and molecular studies of two cys-motif polydnaviral proteins, VHv1.1 and VHv1.4, aimed at identifying and understanding the basic molecular mechanisms of insect-parasite interactions. The goal of the research is to provide fundamental biochemical insights into insect parasitism and insect control that could be used to enhance plant resistance against insect pests. Polydnaviral cysteine-rich proteins are of interest because they are ubiquitous and interfere with insect functions, acting both as anti-immune and anti-growth agents. The goal of the proposed research is to aid in the design of synthetic mimics based on cys-motif protein structures and protein chemistry, and in the engineering of transgenic crops encoding insect resistance genes. To this end, we have defined three specific aims to determine the high-resolution 3D structures and to identify the functional determinants of polydnaviral cysteine-rich proteins mediating their functions in insect hosts following endoparasitic wasp oviposition. This research is in collaboration with Dr. Bruce A. Webb, Professor of Entomology at the University of Kentucky, and an expert in endoparasitic wasp and polydnavirus biology.
Publications
Taubner LM, McGuirl MA, Dooley DM, and Copié V, "Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein." Biochemistry vol. 45 pp.12240-52 (2006)
Jerrod Einerwold, Mahesh Jaseja, Kenneth Hapner, Bruce Webb, and Valerié Copié, "Solution structure of the carboxyl terminal cysteine rich domain of the VHv1.1 polydnaviral gene product: comparison with other cystine knot structural folds. ." Biochemistry, Vol 40, pp 14404-14412 (2001)
Lara Taubner, Michelle McGuirl, David Dooley, and Valerié Copié, "Three-dimensional structure of the apo-form of the copper(I) binding protein NosL, originating from the nos gene cluster of Achromobacter Cycloclastes. ." B. Biochemistry, Manuscript in preparation, (2006)
Personnel:
Valérie Copié
Keywords:
Biochemistry, Protein Chemistry, Structure
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