Sequence variation in the cadherin gene of Ostrinia nubilalis: a tool for field monitoring

Insect Biochem Mol Biol. 2005 Feb;35(2):129-39. doi: 10.1016/j.ibmb.2004.10.008.

Abstract

Toxin-binding proteins of insect midgut epithelial cells are associated with insect resistance to Bacillus thuringiensis (Bt) Cry toxins. A 5378 nt cDNA encoding a 1717 amino acid putative midgut cadherin-like glycoprotein and candidate Cry1Ab toxin-binding protein was characterized from Ostrinia nubilalis. Intraspecific alignment of partial O. nubilalis cadherin gene sequences identified variance within proposed Cry1A toxin binding region 2 (TBR2), 1328IPLQTSILVVT[I/V] N1340, and flanking Cry1A toxin binding region 1 (TBR1), 861DIEIEIIDTNN871. DNA sequence and PCR-RFLP detected single nucleotide polymorphism between cadherin alleles, and pedigree analysis demonstrated Mendelian inheritance. A population sample from Mead, Nebraska showed allelic polymorphism. These assays may be useful for linkage mapping and field surveillance of wild populations and of O. nubilalis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Alleles
  • Amino Acid Sequence
  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / metabolism
  • Bacterial Toxins / metabolism
  • Base Sequence
  • Binding Sites / genetics
  • Cadherins / chemistry
  • Cadherins / genetics*
  • Cadherins / metabolism
  • DNA, Complementary
  • Endotoxins / metabolism
  • Genetic Variation / physiology*
  • Hemolysin Proteins
  • Insect Proteins / chemistry
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism
  • Insecticide Resistance / genetics
  • Molecular Sequence Data
  • Moths / chemistry
  • Moths / genetics*
  • Phylogeny
  • Polymorphism, Single Nucleotide
  • Protein Binding
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Bacterial Toxins
  • Cadherins
  • DNA, Complementary
  • Endotoxins
  • Hemolysin Proteins
  • Insect Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis