Determining the involvement of two aminopeptidase Ns in the resistance of Plutella xylostella to the Bt toxin Cry1Ac: cloning and study of in vitro function

J Biochem Mol Toxicol. 2012 Feb;26(2):60-70. doi: 10.1002/jbt.20401.

Abstract

The cloning, expression in vitro, and characterization of two aminopeptidase Ns (APN5s and APN2s) isolated from the midgut of Cry1Ac-resistant (R) and susceptible (S) strains of Plutella xylostella larvae are presented in this paper. The deduced amino acid sequences of APN5s included C-terminal GPI-modification sites, the gluzincin aminopeptidase motif GATEN, and three N-glycosylated sites; those of APN2s had no GPI-modification sites, had gluzincin aminopeptidase motif GAMEN, and had four N-glycosylated sites. O-glycosylated sites were not predicted for either APN. Because APN2R and APN2S cDNAs contained the same nucleotides, only full-length cDNAs encoding APN5R and APN5S were expressed in Trichoplusia ni cells. Far-Western blotting showed that the expressed receptor APN5 bound to the Cry1Ac toxin. An enzyme-specific activity experiment also showed that APN5 genes were expressed in T. ni cells. ELISA revealed no differences in the binding of expression proteins from the resistant and susceptible strain with Cry1Ac.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / chemistry*
  • Base Sequence
  • CD13 Antigens / biosynthesis
  • CD13 Antigens / chemistry
  • CD13 Antigens / genetics*
  • Cells, Cultured
  • Cloning, Molecular
  • Endotoxins / chemistry*
  • Hemolysin Proteins / chemistry*
  • Insect Proteins / biosynthesis
  • Insect Proteins / chemistry
  • Insect Proteins / genetics*
  • Insecticide Resistance*
  • Insecticides / chemistry*
  • Kinetics
  • Larva / enzymology*
  • Molecular Sequence Data
  • Moths / enzymology*
  • Pest Control, Biological
  • Phylogeny
  • Plants, Genetically Modified
  • Protein Binding
  • Recombinant Proteins
  • Sequence Analysis, DNA

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Insect Proteins
  • Insecticides
  • Recombinant Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis
  • CD13 Antigens

Associated data

  • GENBANK/GU213036
  • GENBANK/GU213037
  • GENBANK/GU213038