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Males of the gypsy moth, Lymantria dispar, are attracted by a pheromone released by females. Pheromones are detected by olfactory neurons housed in specialized sensory
hairs located on the antennae of the male moth. Once pheromone molecules enter the sensilla lymph, a highly abundant pheromone-binding
protein (PBP) transports the molecule to the sensory neuron. The PBPs are members of the insect odorant-binding protein family,
with six conserved cysteine residues. In this study, the disulfide bond connectivities of the pheromone-binding proteins PBP1
and PBP2 from the gypsy moth were found to be cysteines 19–54, 50–109, and 97–118 for PBP1, and cysteines 19–54, 50–110, and
97–119 for PBP2, as determined by cyanylation reactions and cyanogen bromide chemical cleavage. We have discovered that the
second disulfide linkage is the most easily reduced of the three, and this same linkage is missing among four cysteine-containing
insect odorant-binding proteins (OBPs). We are the first to identify the unique steric and electronic properties of this second
disulfide linkage.
Electronic Supplementary Material Supplementary material is available for this article at
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Erika PlettnerEmail: |
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