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Updated: Aug 16, 2026

The Identification of Sea Lamprey Pheromones Using Bioassay-Guided Fractionation
Published on: July 17, 2018
Selective and pH-dependent binding of a moth pheromone to a pheromone-binding protein
Walter S Leal1, Angela M Chen, Melissa L Erickson
1Maeda-Duffey Laboratory, Department of Entomology, University of California, Davis, CA 95616, USA. wsleal@ucdavis.edu
Abstract:
Fluorescence and circular dichroism (CD) data suggest that the major pheromone-binding protein (PBP) from the wild silkmoth, Antheraea polyphemus, ApolPBP1, undergoes a pH-dependent conformational change similar to that previously observed for the PBP from the silkworm moth, Bombyx mori, BmorPBP. All three constituents of the sex pheromone, E6,Z11-16Ac, E6,Z11-16Ald, and E4,Z9-14Ac, bound to ApolPBP1 with apparent high affinity at high pH, but reduced binding at low pH when tested individually in a "cold binding assay." In competitive assays, however, ApolPBP1 showed considerable preference for the major constituent of the sex pheromone, E6,Z11-16Ac. These data suggest that specificity of PBPs contributes at least in part to the remarkable selectivity of moth's olfactory system.
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