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ARS Home » Southeast Area » Gainesville, Florida » Center for Medical, Agricultural and Veterinary Entomology » Chemistry Research » Research » Publications at this Location » Publication #61391
Title: PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDES: FUNCTIONS AND CHEMISTRY

Author
item Teal, Peter
item ABERNATHY, RELLA - ENTOMOLOGY, UNIV. FLA.
item Nachman, Ronald
item FANG, NIANBIA - UNIV. CALIF., BERKELEY
item Meredith, Julia
item Tumlinson Iii, James

Submitted to: Peptides
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/27/1995
Publication Date: N/A
Citation: N/A

Interpretive Summary: Female moths use chemical perfumes called pheromones to attract males for mating. These pheromones are produced only during very specific periods of the night. The production of these pheromones is regulated by chemicals called peptides that are produced in the brain. Scientists at the Insect Attractants, Behavior and Basic Biology Research Laboratory, USDA, ARS in Gainesville Florida have been studying the structures of these peptides and the ways in which these peptides act to stimulate pheromone production. Their research has been useful for determining the parts of the peptides that are necessary for inducing pheromone production and has also determined how these peptides act to stimulate pheromone production in some moth species. Studies of this type are important because the production of pheromones are critical for mating by moths. By determining how these peptides control pheromone production it may be possible to develop methods to stop the action of these peptides and inhibit production of pheromones. This could lead to the development of alternative strategies for control of pest moths.

Technical Abstract: Sex pheromones are critical for reproductive success in most species of Lepidoptera and their production is regulated by the action of pheromone biosynthesis activating neuropeptides (PBAN). These peptides, composed of 33-34 amino acids have approximately 80% sequence homology and share the C-terminal sequence FSPRL-NH[2], which has been sequence required for pheromontropic activity. This pentamer is structurally similar to the active core (FXPRL-NH[2], X=V,T or G) of the insect myotropic pyrokinins. Structure activity studies have shown that all of the pyrokinins have various degrees of pheromonotropic activity and that some have a superagonistic effect. Peptides that only have sequence homology with PBAN in the C-terminal pentapeptide region, but which are pheromonotropic, have been identified also from moths. These findings suggest that induction of pheromone biosynthesis may be regulated by more than one peptide, that PBAN may have a number of physiological functions, and that these peptides regulate induction of pheromone production in a variety of ways.