Suppression of pheromone biosynthesis and mating behavior by RNA interference of pheromone gland-specific fatty acyl reductase in Maruca vitrata.
Wook Hyun ChaDae-Weon LeePublished in: Insect science (2022)
In moths, various enzymes, such as fatty acid synthases, fatty acyl desaturases, and fatty acyl reductases (FARs), are involved in pheromone biosynthesis. In particular, pheromone gland-specific FAR (pgFAR) plays an important role in converting the functional group from carboxylic to alcohol during pheromone biosynthesis. A novel pgFAR of Maruca vitrata, Mvi-pgFAR, was identified through transcriptome sequencing of its pheromone gland. To investigate the involvement of Mvi-pgFAR in pheromone biosynthesis, Mvi-pgFAR was cloned from the pheromone gland and suppressed by RNA interference (RNAi). Mvi-pgFAR harbored several conserved motifs related to NAD(P)H-binding, N-glycosylation, and adenosine / guanosine triphosphate binding. Phylogenetic analysis revealed that Mvi-pgFAR with other lepidopteran pgFARs formed an independent clade. Mvi-pgFAR was specifically expressed only in the pheromone gland. Quantitative real-time polymerase chain reaction showed that the diurnal expression levels of Mvi-pgFAR in the pheromone gland were the highest at 2 h before the scotophase. After primarily confirming Mvi-pgFAR suppression by RNAi, (E,E)-10,12-hexadecadienal (E10E12-16:Ald), a major sex pheromone component, was quantified by gas chromatography. When Mvi-pgFAR was successfully suppressed, E10E12-16:Ald production was reduced by up to half of that of the control, and the mating rate was subsequently decreased. Our results demonstrate that Mvi-pgFAR downregulation can suppress mating behavior by changing the relative sex pheromone component ratio, suggesting that Mvi-pgFAR can be used as a novel control target.