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Alcohol dehydrogenase 5 (ADH5) is a member of medium‐chain dehydrogenase/reductase family and takes part in cellular formaldehyde and S‐nitrosoglutathione metabolic network. 2‐tridecanone (2‐TD) is a toxic compound in many  Solanaceae  crops to defend against a variety of herbivory insects. In the broader context of insect development and pest control strategies, this study investigates how a new ADH5 from  Helicoverpa armigera  ( Ha ADH5) regulates the expression of  CYP6B6 , a gene involved in molting and metamorphosis, in response to 2‐TD treatment. Cloning of the  HaADH5  complementary DNA sequence revealed that its 1002 bp open reading frame encodes 334 amino acids with a predicted molecular weight of 36.5 kD.  Ha ADH5 protein was purified in the  Escherichia coli  Transetta (pET32a‐ HaADH5 ) strain using a prokaryotic expression system. The ability of  Ha ADH5 protein to interact with the 2‐TD responsive region within the promoter of  CYP6B6  was confirmed by an  in vitro  electrophoretic mobility shift assay and transcription activity validation in yeast. Finally, the expression levels of both  HaADH5  and  CYP6B6  were found to be significantly decreased in the midgut of 6th instar larvae after 48 h of treatment with 10 mg/g 2‐TD artificial diet. These results indicate that upon 2‐TD treatment of cotton bollworm,  Ha ADH5 regulates the expression of  CYP6B6  by interacting with its promoter. As  Ha ADH5 regulation of  CYP6B6  expression may contribute to the larval xenobiotic detoxification, molting and metamorphosis,  Ha ADH5 is a candidate target for controlling the growth and development of cotton bollworm.

Alcohol dehydrogenase 5 of Helicoverpa armigera interacts with the CYP6B6 promoter in response to 2‐tridecanone