Triazophos up-regulated gene expression in the female brown planthopper, Nilaparvata lugens

J Insect Physiol. 2010 Sep;56(9):1087-94. doi: 10.1016/j.jinsphys.2010.03.004. Epub 2010 Mar 17.


The widespread use of insecticides has caused the resurgence of the brown planthopper, Nilaparvata lugens, in Asia. In this study, we investigated an organo-phosphorous insecticide, triazophos, and its ability to induce gene expression variation in female N. lugens nymphs just before emergence. By using the suppression subtractive hybridization method, a triazophos-induced cDNA library was constructed. In total, 402 differentially expressed cDNA clones were obtained. Real-time qPCR analysis confirmed that triazophos up-regulated the expression of six candidate genes at the transcript level in nymphs on day 3 of the 5th instar. These genes encode N. lugens vitellogenin, bystin, multidrug resistance protein (MRP), purine nucleoside phosphorylase (PNP), pyrroline-5-carboxylate reductase (P5CR) and carboxylesterase. Our results imply that the up-regulation of these genes may be involved in the induction of N. lugens female reproduction or resistance to insecticides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B / metabolism
  • Animals
  • Cell Adhesion Molecules / metabolism
  • DNA Primers / genetics
  • Female
  • Gene Expression Regulation / drug effects*
  • Gene Library
  • Hemiptera / drug effects
  • Hemiptera / metabolism*
  • Insecticides / toxicity*
  • Nymph / drug effects
  • Nymph / metabolism
  • Organothiophosphates / toxicity*
  • Polymerase Chain Reaction
  • Purine-Nucleoside Phosphorylase / metabolism
  • Pyrroline Carboxylate Reductases / metabolism
  • Triazoles / toxicity*
  • Vitellogenins / metabolism


  • ATP Binding Cassette Transporter, Subfamily B
  • Cell Adhesion Molecules
  • DNA Primers
  • Insecticides
  • Organothiophosphates
  • Triazoles
  • Vitellogenins
  • triazophos
  • Pyrroline Carboxylate Reductases
  • Purine-Nucleoside Phosphorylase