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Nature

Title:		Pheromone binding and inactivation by moth antennae
Author(s):		Vogt RG; Riddiford LM;
Address:		"Department of Zoology, University of Washington, Seattle, Washington 98195, USA"
Journal Title:		Nature
Year:		1981
Volume:		293
Issue:		5828
Page Number:		161 - 163
DOI:		10.1038/293161a0
ISSN/ISBN:		0028-0836 (Print) 0028-0836 (Linking)
Abstract:		"The antennae of male silk moths are extremely sensitive to the female sex pheromone such that a male moth can find a female up to 4.5 km away. This remarkable sensitivity is due to both the morphological and biochemical design of these antennae. Along the branches of the plumose antennae are the sensilla trichodea, each consisting of a hollow cuticular hair containing two unbranched dendrites bathed in a fluid, the receptor lymph ,3. The dendrites and receptor lymph are isolated from the haemolymph by a barrier of epidermal cells which secreted the cuticular hair. Pheromone molecules are thought to diffuse down 100 A-wide pore tubules through the cuticular wall and across the receptor lymph space to receptors located in the dendritic membrane. To prevent the accumulation of residual stimulant and hence sensory adaptation, the pheromone molecules are subsequently inactivated in an apparent two-step process of rapid 'early inactivation' followed by much slower enzymatic degradation. The biochemistry involved in this sequence of events is largely unknown. We report here the identification of three proteins which interact with the pheromone of the wild silk moth Antheraea polyphemus: a pheromone-binding protein and a pheromone-degrading esterase, both uniquely located in the pheromone-sensitive sensilla; and a second esterase common to all cuticular tissues except the sensilla"
Keywords:		Animal Structures/enzymology/*metabolism Animals Bombyx/*anatomy & histology/enzymology/*physiology Esterases/metabolism Extremities/physiology Female Insect Proteins/chemistry/isolation & purification/metabolism Male Protein Binding Sex Attractants/*meta;
Notes:		"MedlineVogt, R G Riddiford, L M eng GM0270/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. England 1981/09/10 Nature. 1981 Sep 10-16; 293(5828):161-3. doi: 10.1038/293161a0"