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Title: STRUCTURE ACTIVITY STUDIES WITH PHEROMONE BINDING PROTEINS OF THE GYPSY MOTH, LYMANTRIA DISPAR

Author
item HONSON, NICOLETTE - SIMON FRAZIER UNIV
item JOHNSON, MARGARET - SIMON FRAZIER UNIV
item OLIVER, JAMES
item PRESTWICH, GLENN - UNIVERSITY OF UTAH
item PLETTNER, ERIKA - SIMON FRAZIER UNIV

Submitted to: Chemical Senses
Publication Type: Abstract Only
Publication Acceptance Date: 3/1/2003
Publication Date: 7/1/2003
Citation: Honson, N., Johnson, M., Oliver, J.E., Prestwich, G.D., Plettner, E.A. 2003 Structure activity studies with pheromone binding proteins of the gypsy moth, Lymantria dispar. Chemical Senses. 28(6):491-498.

Interpretive Summary:

Technical Abstract: Pheromone olfaction in the gypsy moth, Lymantria dispar, involves accurate distinction of compounds with similar structure and polarity. The identified pheromone is (7R, 8S)-cis-2-methyl-7, 8-epoxyoctadecane, 1a, and a known antagonist is (7Z) 2-methyloctadec-7-ene, 4a. The first step in olfaction is binding of odorants by small, soluble odorant-binding proteins. The pheromone-sensing hairs contain pheromone-binding proteins (PBPs). We have studied some molecular determinants recognized by the two PBPs found in the gypsy moth, using three pheromone/PBP binding assays, one of which is new. Results indicate that I) PBPs bind analogs of the pheromone strongly with some discrimination II) PBPs experience enhancement of binding when presented with 1a or its enantiomer and 4a simultaneously or III) at high ligand:PBP ratios. We found no evidence of allostery, so the synergistic binding effects and the concentration effect may only be explained by multimerization of PBPs with each other, which leads to more than one population of binding sites. We suggest that the enhanced ligand binding at high ligand:PBP ratios may serve to sequester excess ligand and thereby attenuate very strong signals.