Glycerol-3-phosphate O-acyltransferase is required for PBAN-induced sex pheromone biosynthesis in Bombyx mori

Abstract

Female moths employ their own pheromone blends as a communicational medium in mating behavior. The biosynthesis and release of sex pheromone in female moths are regulated by pheromone biosynthesis activating neuropeptide (PBAN) and the corresponding action of PBAN has been well elucidated in Bombyx mori. However, very little is known about the molecular mechanism regarding the biosynthesis of sex pheromone precursor. In this study, quantitative proteomics was utilized to comprehensively elucidate the expression dynamics of pheromone glands (PGs) during development. Proteomic analysis revealed a serial of differentially expressed sex pheromone biosynthesis-associated proteins at the different time points of B. mori development. Most interestingly B. mori glycerol-3-phosphate O-acyltransferase (BmGPAT) was found to be expressed during the key periods of sex pheromone biosynthesis. RNAi knockdown of BmGPAT confirmed the important function of this protein in the biosynthesis of sex pheromone precursor, triacylglcerol (TAG), and subsequently PBAN-induced production of sex pheromone, bombykol. Behavioral analysis showed that RNAi knockdown of GPAT significantly impaired the ability of females to attract males. Our findings indicate that GPAT acts to regulate the biosynthesis of sex pheromone precursor, TAG, thus influencing PBAN-induced sex pheromone production and subsequent mating behavior.

Exploring complex pheromone biosynthetic processes in the bumblebee male labial gland by RNA sequencing

“…C). Additionally, we identified a homologue of Bombyx mori GPAT involved in pheromone biosynthesis (Du et al ., ), and 1‐acylglycerol‐3‐phosphate O‐acyltransferase (AGPAT), which was previously not considered to be involved in pheromone biosynthesis. AGPAT was more abundant in the LG and MH than in other tissues examined, indicating its possible role in MP biosynthesis (Fig.…”

“…B. In moths, a multitude of proteins involved in FA‐derived pheromone biosynthesis has been identified, including acyl‐coenzyme A‐binding protein (ACBP; Matsumoto et al ., ), fatty acid reductase (FAR; Moto et al ., ), pheromone biosynthesis activating neuropeptide receptor (PBANr; Choi et al ., ), fatty acid desaturase (Moto et al ., ), acetyl coenzyme A carboxylase (ACC; Tsfadia et al ., ), fatty acid transport protein (FATP; Ohnishi et al ., ), lipid storage droplet protein (LSD; Ohnishi et al ., ), diacylglycerol acyltransferase 2 (DGAT2; Du et al ., ), lipases (Du et al ., ; Zhang et al ., ) and glycerol‐3‐phosphate O‐acyltransferase (GPAT; Du et al ., ). Generally, the transcripts coding for these proteins are specifically and abundantly expressed in the moth pheromone gland (PG).…”

Comparative Proteomic Analysis of Chicken Primary Hepatocytes with Folic Acid Free or Supplementation Culture Mediums.

“…A total of 200 μg protein were digested following the reported methods (Du et al, 2015), and the peptide content was quantified by UV light spectral density at 280 nm. Then 80 μg peptide for each sample were used for iTRAQ labelling (Applied Biosystems).…”

“…The protein identification and iTRAQ quantification were operated using a Mascot 2.2 (Matrix Science, London, UK) and Proteome Discoverer 1.4 (Thermo Electron, San Joes, CA) as described (Wang, et al, 2013). The corresponding parameters were set as same as the description by Du et al (2015). Database search was performed against the Gallus (Uniprot) database.…”

Biotechnological potential of insect fatty acid-modifying enzymes

“…These include (i) acyltransferase involved in synthesis of FA-storing triacylglycerols [125,126]; (ii) lipases and esterases involved in hydrolytic release of FA pheromone precursors from storage triacylglycerols [127][128][129], formation of FA ethyl esters [130], or primary metabolism [131][132][133]; and (iii) cytochrome P450, involved in the oxidative decarbonylation of FAs to hydrocarbons [134]. However, for the majority of insect pheromone biosynthetic steps, the genes and enzymes involved have yet to be identified and characterized.…”