Nematodes are the world’s most destructive plant pathogen. Responsible for an estimated $100 billion dollars of crop damage annually, soil-dwelling plant parasitic nematodes target the roots of most crops and represent a significant challenge to attaining yields high enough to meet growing demand. Traditional methods of managing parasitic nematodes are either of limited efficacy, environmentally dangerous, or toxic to humans, birds, fish, and other non-target organisms. As a result, the Environmental Protection Agency has banned the use of many such agents, creating the distinct need for a next generation of nematicides. Researchers at the University of New Hampshire are investigating the use of phosphodiesterase (PDE) inhibitors as nematicides. These compounds may allow for rational nematicide design to enhance selectivity and eliminate adverse environmental effects. Our researchers have developed assays to evaluate the effects of this class of compounds on various aspects of the nematode lifecycle. UNH’s patent-pending method can be used to identify next-generation targeted nematicides to mitigate the economic, environmental, and social liabilities associated with traditional pesticides.
- Screening assays
- For determining efficacy of new PDE inhibitor-based nematicide compounds
- Greatly reduced environmental impact
- By developing new PDE inhibitor compounds selective for nematode PDEs, this method will avoid adverse effects on agrichemical and farm workers, vertebrate animals, and crops.
- Crop management
- Nematicide candidate compound screening
Intellectual Property Status
Lead Innovator - Rick Cote PH.D
Professor Cote’s research interests include the structure, function, regulation, pharmacology, and molecular evolution of the phosphodiesterase enzyme superfamily. In addition to investigating the pharmacology of nematode PDEs and applications to parasitic nematode control, he is a leading expert on the role of PDEs in the visual signaling pathway of rod and cone photoreceptor cells of the retina.
- 4 June 2012
Functional Mapping of Interacting Regions of the Photoreceptor Phosphodiesterase (PDE6) γ-Subunit with PDE6 Catalytic Dimer, Transducin, and Regulator of G-protein Signaling9–1 (RGS9–1)
- 18 April 2012
Characterization of Conformational Changes and Protein-Protein Interactions of Rod Photoreceptor Phosphodiesterase (PDE6)*
- 30 November 2009
Structural Requirements of the Photoreceptor Phosphodiesterase γ-Subunit for Inhibition of Rod PDE6 Holoenzyme and for Its Activation by Transducin*
- 8 September 2008
Direct Allosteric Regulation between the GAF Domain and Catalytic Domain of Photoreceptor Phosphodiesterase PDE6
- 3 January 2006
The Glutamic Acid-rich Protein-2 (GARP2) Is a High Affinity Rod Photoreceptor Phosphodiesterase (PDE6)-binding Protein That Modulates Its Catalytic Properties*