Comparative Proteomics of Peritrophic Matrix Provides an Insight into its Role in Cry1Ac Resistance of Cotton Bollworm Helicoverpa armigera

Toxins (Basel). 2019 Feb 2;11(2):92. doi: 10.3390/toxins11020092.

Abstract

Crystalline (Cry) proteins from Bacillus thuringiensis (Bt) are widely used in sprays and transgenic crops to control insect pests, but the evolution of insect resistance threatens their long-term use. Different resistance mechanisms have been identified, but some have not been completely elucidated. Here, the transcriptome of the midgut and proteome of the peritrophic matrix (PM) were comparatively analyzed to identify potential mechanism of resistance to Cry1Ac in laboratory-selected strain XJ10 of Helicoverpa armigera. This strain had a 146-fold resistance to Cry1Ac protoxin and 45-fold resistance to Cry1Ac activated toxin compared with XJ strain. The mRNA and protein levels for several trypsin genes were downregulated in XJ10 compared to the susceptible strain XJ. Furthermore, 215 proteins of the PM were identified, and nearly all had corresponding mRNAs in the midgut. These results provide new insights that the PM may participate in Bt resistance.

Keywords: Bt; Helicoverpa armigera; midgut; peritrophic matrix; proteome; transcriptome.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / toxicity*
  • Endotoxins / toxicity*
  • Gastrointestinal Tract / drug effects
  • Gastrointestinal Tract / metabolism
  • Hemolysin Proteins / toxicity*
  • Insect Proteins / genetics
  • Insect Proteins / metabolism
  • Insecticide Resistance*
  • Insecticides / toxicity*
  • Larva / drug effects*
  • Larva / genetics
  • Larva / metabolism
  • Moths / drug effects*
  • Moths / genetics
  • Moths / metabolism
  • Proteome / drug effects
  • Proteomics
  • Species Specificity
  • Transcriptome / drug effects
  • Trypsin / genetics
  • Trypsin / metabolism

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Insect Proteins
  • Insecticides
  • Proteome
  • insecticidal crystal protein, Bacillus Thuringiensis
  • Trypsin