Wednesday, 29 October 2003
D0494

This presentation is part of : Display Presentations, Section B. Physiology, Biochemistry, Toxicology, and Molecular Biology

Enzyme control by the pheromone biosynthesis activating neuropeptide in sex pheromone biosynthesis in the "Z strain" of the European corn borer, Ostrinia nubilalis

Hanan Eltahlawy and Stephen P Foster. North Dakota State University, Department of Entomology, Fargo, ND

Most moth sex pheromone components are biosynthesized de novo via synthesis of saturated fatty acids, followed by specific metabolism of these acids, including desaturation, chain-shortening, reduction, acetylation or oxidation. The pheromone biosynthesis activating neuropeptide (PBAN) is known to regulate sex pheromone biosynthesis by influencing a specific enzyme step(s). However, which step PBAN influences has only been investigated in a limited number of species, and these studies have shown contrasting results. For example, PBAN is thought to influence acetyl CoA carboxylase activity in Argyrotaenia velutinana and Helicoverpa zea, fatty acid reduction in Spodoptera littoralis and Bombyx mori, the mobilization of fatty acids from triacylglycerols in Manduca sexta, and acetyl transferase activity in Sesamia nonagrioides. In order to obtain a more complex understanding of sex pheromone regulation in moths, and perhaps reconcile some of these inconsistencies, we have begun studying pheromone biosynthesis in the "Z strain" of the European corn borer. Here, we report which sex pheromone biosynthetic enzyme is most affected by PBAN in this species.

Species 1: Lepidoptera Crambidae Ostrinia nubilalis (European corn borer)
Keywords: PBAN

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