Evolution of noctuid pheromone binding proteins: identification of PBP in the black cutworm moth, Agrotis ipsilon

Insect Biochem Mol Biol. 2002 Aug;32(8):839-46. doi: 10.1016/s0965-1748(01)00172-2.

Abstract

Male black cutworm moths (Agrotis ipsilon, Lepidoptera, Noctuoidea, Noctuidae), which are attracted by a three-component pheromone blend ((Z)-7-dodecenyl acetate, Z7-12:Ac; (Z)-9-tetradecenyl acetate, Z9-14:Ac; (Z)-11-hexadecenyl acetate, Z11-16:Ac), express diverse antennal pheromone binding proteins (PBPs). Two PBP isoforms (Aips-1 and Aips-2) that show 46% identity were cloned from antennal cDNA of male A. ipsilon. The protein Aips-1 displays a high degree of identity (70-95%) with PBPs of other noctuiids, but shows only 42-65% identity with the PBPs of more phylogenetically distant species. The other protein, Aips-2, represents a distinct group of PBP that includes proteins from Sphingidae and Yponomeutidae. These differences observed suggest that each of the two PBPs may be tuned to a specific pheromone ligand.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Evolution, Molecular
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism
  • Male
  • Molecular Sequence Data
  • Moths / genetics*
  • Moths / metabolism
  • Pheromones / metabolism
  • Phylogeny
  • Sequence Homology, Amino Acid

Substances

  • Carrier Proteins
  • DNA, Complementary
  • Insect Proteins
  • Pheromones
  • pheromone binding protein, insect