Sex pheromone desaturase functioning in a primitive Ostrinia moth is cryptically conserved in congeners’ genomes

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Abstract
( E )-11- and ( Z )-11-tetradecenyl acetate are the most common female sex pheromone components in Ostrinia moths. The Δ11-desaturase expressed in the pheromone gland (PG) of female moths is a key enzyme that introduces a double bond into pheromone molecules. A single Δ11-desaturase of Ostrinia nubilalis , OnubZ/E11, has been shown to produce an ∼7:3 mixture of ( E )-11- and ( Z )-11-tetradecenoate from the substrate tetradecanoate. In contrast, the sex pheromone of Ostrinia latipennis , a primitive species of Ostrinia, is ( E )-11-tetradecenol. This pheromone is unique in that it is not acetylated, and includes no Z isomer. In the present study, through the cloning and functional analysis of a PG-specific Δ11-desaturase in O. latipennis , we showed that the absence of the Z isomer in the pheromone is attributable to the strict product specificity of the Δ11-desaturase in this species, LATPG1. Phylogenetic analysis revealed that LATPG1 was not closely related to OnubZ/E11. Rather, it was closely related to retroposon-linked cryptic Δ11-desaturases ( ezi -Δ11) found in the genomes of O. nubilalis and Ostrinia furnacalis . Taken together, the results showed that an unusual Δ11-desaturase is functionally expressed in O. latipennis , although the genes encoding this enzyme appear to be cryptic in congeners.

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