title: Sequence variation in the cadherin gene of Ostrinia nubilalis: a tool for field monitoring.
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.
authors.affiliation: USDA-ARS, Corn Insects and Crop Genetics Research Unit, 113 Genetics Laboratory, Iowa State University, Ames, IA 50011, USA. coates@iastate.edu
authors.forename: Brad S
authors.initials: BS
authors.lastname: Coates
authors.forename: Douglas V
authors.initials: DV
authors.lastname: Sumerford
authors.forename: Richard L
authors.initials: RL
authors.lastname: Hellmich
authors.forename: Leslie C
authors.initials: LC
authors.lastname: Lewis
mesh_terms: D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism; D001427:Bacterial Toxins / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D015820:Cadherins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary; D004731:Endotoxins / Q000378:metabolism; D014644:Genetic Variation / Q000502:physiology*; D006460:Hemolysin Proteins; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D007305:Insecticide Resistance / Q000235:genetics; D008969:Molecular Sequence Data; D009036:Moths / Q000737:chemistry / Q000235:genetics*; D010802:Phylogeny; D020641:Polymorphism, Single Nucleotide; D011485:Protein Binding; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D015820:Cadherins; D018076:DNA, Complementary; D004731:Endotoxins; D006460:Hemolysin Proteins; D019476:Insect Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis