| Title: | Phylogenetic and functional characterization of ten P450 genes from the CYP6AE subfamily of Helicoverpa armigera involved in xenobiotic metabolism |
| Author(s): | Shi Y; Wang H; Liu Z; Wu S; Yang Y; Feyereisen R; Heckel DG; Wu Y; |
| Address: | "College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: 2014202036@njau.edu.cn. College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: 2013202034@njau.edu.cn. College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: liuzhi@sino-agri-sal.com. College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: swwu@njau.edu.cn. College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: yhyang@njau.edu.cn. Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej, Denmark. Electronic address: rene.feyereisen@plen.ku.dk. Department of Entomology, Max Planck Institute for Chemical Ecology, Jena 07745, Germany. Electronic address: heckel@ice.mpg.de. College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: wyd@njau.edu.cn" |
| DOI: | 10.1016/j.ibmb.2017.12.006 |
| ISSN/ISBN: | 1879-0240 (Electronic) 0965-1748 (Linking) |
| Abstract: | "The cotton bollworm, Helicoverpa armigera, is a generalist herbivore widely distributed over the world and is a major lepidopteran pest on cotton. Studies, especially from Asia, show that it relies on cytochrome P450 monooxygenases with broad substrate specificities to protect itself from pesticides. The number of P450s may have expanded in the processes of coping with the wide diversity of phytochemicals that the insect encounters among its numerous host plants. In order to examine the metabolic capabilities of these P450s, we focused here on all ten P450s of the Helicoverpa armigera CYP6AE subfamily, which can be easily induced by plant toxins and pyrethroids. These P450s, along with cytochrome P450 reductase, were heterologously expressed in insect cells and compared functionally. In vitro metabolism showed that all CYP6AE subfamily members can convert esfenvalerate to 4'-hydroxyesfenvalerate efficiently except CYP6AE20. In contrast, none of the recombinant CYP6AE enzymes could metabolise gossypol under our experimental conditions. Epoxidation capabilities were observed in the CYP6AE subfamily, aldrin can be converted to dieldrin at rates up to 0.45?ª++/-?ª+0.04?ª+pmol/min/pmol P450. Seven P450s in this subfamily can metabolise imidacloprid, but with lower efficiency than Bemisia tabaci CYP6CM1vQ. CYP6AE20 had virtually no metabolic competence to these four compounds but could metabolise several model fluorogenic substrates. These results showed the broad substrate spectrum of H. armigera CYP6AE P450s and suggest a limited role of gossypol upon the evolution of H. armigera CYP6AE genes" |
| Keywords: | "Aldrin/metabolism Animals Cytochrome P450 Family 6/*genetics/metabolism Gossypol/*metabolism Inactivation, Metabolic Insect Proteins/genetics/metabolism Insecticides/*metabolism Larva/genetics/growth & development/metabolism Moths/*genetics/growth & devel;" |
| Notes: | "MedlineShi, Yu Wang, Huidong Liu, Zhi Wu, Shuwen Yang, Yihua Feyereisen, Rene Heckel, David G Wu, Yidong eng Research Support, Non-U.S. Gov't England 2017/12/21 Insect Biochem Mol Biol. 2018 Feb; 93:79-91. doi: 10.1016/j.ibmb.2017.12.006. Epub 2017 Dec 16" |
