Biochemical evaluation of interactions between synergistic molecules and phase I enzymes involved in insecticide resistance in B- and Q-type Bemisia tabaci (Hemiptera: Aleyrodidae)

Pest Manag Sci. 2017 Sep;73(9):1873-1882. doi: 10.1002/ps.4553. Epub 2017 Mar 14.

Abstract

Background: Metabolic resistance is an important consideration in the whitefly Bemisia tabaci, where an esterase-based mechanism has been attributed to pyrethroid resistance and over-expression of the cytochrome P450, CYP6CM1, has been correlated to resistance to imidacloprid and other neonicotinoids.

Results: In vitro interactions between putative synergists and CYP6CM1, B and Q-type esterases were investigated, and structure-activity relationship analyses allowed the identification of chemical structures capable of acting as inhibitors of esterase and oxidase activities. Specifically, methylenedioxyphenyl (MDP) moieties with a polyether chain were preferable for optimum inhibition of B-type esterase, whilst corresponding dihydrobenzofuran structures were potent for the Q-esterase variation. Potent inhibition of CYP6CM1 resulted from structures which contained an alkynyl chain with a terminal methyl group.

Conclusions: Synergist candidates could be considered for field control of B. tabaci, especially to abrogate neonicotinoid resistance. © 2017 Society of Chemical Industry.

Keywords: Bemisia tabaci; P450s; SAR; esterase; piperonyl butoxide; synergist.

MeSH terms

  • Animals
  • Enzyme Inhibitors / pharmacology
  • Esterases / antagonists & inhibitors
  • Esterases / metabolism
  • Hemiptera / drug effects
  • Hemiptera / enzymology*
  • Hemiptera / metabolism
  • Insecticide Resistance*
  • Metabolic Detoxication, Phase I*
  • Protein Binding

Substances

  • Enzyme Inhibitors
  • Esterases