Submitted to: Handbook of Biologically Active Peptides
Publication Type: Book / chapter
Publication Acceptance Date: 7/1/2006
Publication Date: 1/1/2006
Citation: Masler, E.P. 2006. Free-living nematode peptides. In A. Kastin, ed. Handbook of Biologically Active Peptides. New York: Academic Press. pp. 247-253. Interpretive Summary: Plant-parasitic nematodes attack all crops of agricultural importance, causing over $10 billion in losses annually to U.S. farmers. A serious problem facing growers is the lack of acceptable nematicides. This makes the discovery of environmentally and economically sound control agents critical. An approach to discovery is identification of natural targets in nematodes that provide a biochemical basis for development of novel control agents. Since nematodes depend upon neuropeptides to control all life processes, neuropeptides are natural control targets. To expedite the identification of the most appropriate targets, this report describes a survey of neuropeptides in nematodes, demonstrating that the enormous diversity of these molecules can be exploited to identify specific molecules with useful analogs in plant-parasitic nematodes for design of control agents. This approach can greatly accelerate the discovery of environmentally responsible agents for the management of plant-parasitic nematodes, and the information will be used by researchers in the agrochemical and agricultural biotechnology industries who are developing safe, selective methods for nematode control.
Technical Abstract: Nematodes depend upon peptide messengers to regulate diverse behavioral, developmental, and metabolic events. In free-living nematodes, sequencing of the first complete animal genome facilitated detection of biologically-active peptides, including neuropeptides. This has complemented previous and ongoing efforts in biochemistry, pharmacology and physiology, revealing that nematodes possess some peptide families that are exceedingly complex. Complexity can result from large numbers of genes encoding related amino acid sequences, as in the case of the FMRFamide-like peptides, or from intricate variations of molecular architectures, as seen among members of the insulin-like peptides family. These and two other peptide families are described, along with their established and proposed functions.