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Online Journal of Veterinary Research©
(Including Medical and Laboratory Research)
Volume 25 (12):869-888, 2021.
Functional analysis of cytochrome P450 genes in Aedes Aegypti.
Amir Hossein Asgari Safdar1*
1Department of Animal Sciences, Faculty of Agriculture and Natural Resources, Science and Research Branch, Islamic Azad University, Tehran, IRAN.
Asgari Safdar AH., Functional analysis of cytochrome P450 genes in Aedes Aegypti, Onl J Vet Res., 25 (12):869-888, 2021. Author describes role of CYP6AA5, CYP6AL1, CYP9J32, and CYP4J16 in detoxification of permethrin, cypermethrin and deltamethrin by RNA interference (RNAi) insecticide bioassay in adults and larvae of Aedes aegypti. RNAi fed to larvae with chitosan/dsRNA nanoparticles reduced transcripts CYP6AA5 ~-39%, CYP6AL1 ~-46%, CYP9J32 ~-47%, CYP4J16A ~-44% and CYP4J16B ~-41%. This boosted larval mortality 41.2% to cypermethrin when CYP6AA5 was inhibited and 46.0% to permethrin if CYP9J32 suggesting detoxification. In adult mosquitoes, RNAi reduced CYP6AA5 78%, CYP6AL1 80% and CY4J16A transcripts 87% 96h after injection of corresponding double-stranded RNAs (dsRNAs). Expression of CYP9J32 was suppressed ~-46.5% by 24h whereas CYP4J16B ~-78.2% at 72h. Exposure of adults mosquitoes injected with CYP6AA5 dsRNA to cypermethrin for 24 h increased mortality 29.3%. Different slopes (P < 0.02) and intercept (P < 0.01) susceptibility to cypermethrin in mosquitoes injected CYP6AA5dsRNA or GFP dsRNA suggested detoxification. 3D binding revealed distances between heme iron and aromatic hydroxylation sites were 9.2 for permethrin, 9.4 cypermethrin and 7.2 Å for deltamethrin whereas for aliphatic hydroxylation sites were 5.3, 2.8 and 2.9 Å, respectively. CYP6AA5 may metabolize cypermethrin and deltamethrin by aliphatic hydroxylation with heme iron.
Keys words: Cytochrome P450, Aedes aegypti, detoxification, RNA interference, homology modeling.