Pheromone biosynthetic pathway and chemoreception proteins in sex pheromone gland of Eogystia hippophaecolus

Hu, Ping; Wang, Dongbai; Gao, Chenglong; Lu, Peng-Fei; Tao, Jing; Luo, Youqing

doi:10.1016/j.cbd.2020.100702

Cited by 1 publication

(1 citation statement)

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“…Besides fatty aldehydes, BmAOX5 could metabolize aromatic aldehydes such as benzaldehyde, salicylaldehyde, and vanillic aldehyde. Recent studies have shown that the expression of 11 odorant-degrading enzyme genes is also found in the PG of Eogystia hippophaec by the transcriptome ( Hu et al 2020 ). Therefore, BmAOX5 may also metabolize other aldehydes in the cytoplasm for detoxification, or may participate in the degradation of aldehyde odorant compounds to locate suitable and safe spawning sites ( Choo et al 2013 , Marelja et al 2014 , Xu and Liao 2017 ).…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Aldehyde Oxidase 5 in the Pheromone Gland of the Silkworm (Lepidoptera: Bombycidae)

Zhang

Yang

Shen

et al. 2020

Journal of Insect Science

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Aldehyde oxidases (AOXs) are a subfamily of cytosolic molybdo-flavoenzymes that play critical roles in the detoxification and degradation of chemicals. Active AOXs, such as AOX1 and AOX2, have been identified and functionally analyzed in insect antennae but are rarely reported in other tissues. This is the first study to isolate and characterize the cDNA that encodes aldehyde oxidase 5 (BmAOX5) in the pheromone gland (PG) of the silkworm, Bombyx mori. The size of BmAOX5 cDNA is 3,741 nucleotides and includes an open reading frame, which encodes a protein of 1,246 amino acid residues. The theoretical molecular weight and isoelectric point of BmAOX5 are approximately 138 kDa and 5.58, respectively. BmAOX5 shares a similar primary structure with BmAOX1 and BmAOX2, containing two [2Fe-2S] redox centers, a FAD-binding domain, and a molybdenum cofactor (MoCo)-binding domain. RT–PCR revealed BmAOX5 to be particularly highly expressed in the PG (including ovipositor) of the female silkworm moth, and the expression was further confirmed by in situ hybridization, AOX activity staining, and anti-BmAOX5 western blotting. Further, BmAOX5 was shown to metabolize aromatic aldehydes, such as benzaldehyde, salicylaldehyde, and vanillic aldehyde, and fatty aldehydes, such as heptaldehyde and propionaldehyde. The maximum reaction rate ( V max ) of benzaldehyde as substrate was 21 mU and K m was 1.745 mmol/liter. These results suggested that BmAOX5 in the PG could metabolize aldehydes in the cytoplasm for detoxification or participate in the degradation of aldehyde pheromone substances and odorant compounds to identify mating partners and locate suitable spawning sites.

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