Pymetrozine is hydroxylated by CYP6CM1, a cytochrome P450 conferring neonicotinoid resistance in Bemisia tabaci.

Resistance to neonicotinoid insecticides such as imidacloprid in the cotton whitefly, Bemisia tabaci, is linked to its hydroxylation by constitutively overexpressed CYP6CM1, a cytochrome P450 enzyme. Here, an investigation was conducted to establish whether CYP6CM1 functionally expressed in Sf9 cells also detoxifies pymetrozine, a selective homopteran feeding blocker known to be cross-resistant to neonicotinoids in whiteflies. Incubation of pymetrozine with functionally expressed Bemisia CYP6CM1 and subsequent LC-MS/MS analysis revealed a rapid formation of two pymetrozine metabolites by hydroxylation of its heterocyclic 1,2,4-triazine ring system. Enzyme kinetics revealed a Km value of 5.9 ± 0.3 µM and a time-dependent depletion of pymetrozine. The known cross-resistance between imidacloprid, other neonicotinoid insecticides and pymetrozine in B. tabaci is most likely conferred by the very same detoxification mechanism, i.e. a monooxygenase-based hydroxylation mechanism linked to the overexpression of CYP6CM1. These insecticide chemistries should not be alternated in whitefly resistance management strategies.