Molecular cloning and characterization of TRPVs in two rice pests: Nilaparvata lugens (Stål) and Nephotettix cincticeps (Uhler)

Pest Manag Sci. 2019 May;75(5):1361-1369. doi: 10.1002/ps.5254. Epub 2018 Dec 5.

Abstract

Backgroud: Insect TRPV is a subfamily of transient receptor potential (TRP) ion channels, including two genes, nanchung and inactive. It has recently been found that two commercial insecticides, pymetrozine and pyrifluquinazon, target the heteromeric TRPV ion channel complex which is specifically expressed in the chordotonal organ neurons in Drosophila. However, information on the TRPV genes in agricultural insects is still limited.

Results: In this study, we cloned and characterized two TRPV genes from Nilaparvata lugens (NlNan and NLIav) and Nephotettix cincticeps (NcNan and NcIav), two serious rice pests throughout Asia. The deduced amino acid sequences share highly identity with other insect homologues (58-85%) and have the characteristic TRPV domain architecture: five ankyrin repeats and six transmembrane domains. These TRPV transcripts were expressed in all developmental stages and expression levels in male adults were significantly higher than in female adults. Moreover, expression levels in antennae were much higher than in heads and legs.

Conclusion: NlNan, NlIav, NcNan and NcIav may have roles in male-specific behaviors, and the sequence information lays the foundation for further study on the structural and functional characterization of TRPVs in agricultural pests. © 2018 Society of Chemical Industry.

Keywords: Nephotettix cincticeps; Nilaparvata lugens; TRPV; inactive; insecticide; nanchung.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cloning, Molecular
  • Gene Expression Regulation, Developmental
  • Hemiptera / genetics*
  • Hemiptera / growth & development
  • Insect Proteins / chemistry
  • Insect Proteins / genetics*
  • Models, Molecular
  • Organ Specificity
  • Oryza*
  • Protein Conformation
  • TRPV Cation Channels / chemistry
  • TRPV Cation Channels / genetics*

Substances

  • Insect Proteins
  • TRPV Cation Channels