An odorant-binding protein facilitates odorant transfer from air to hydrophilic surroundings in the blowfly

Chem Senses. 2005 Sep;30(7):559-64. doi: 10.1093/chemse/bji049. Epub 2005 Aug 17.

Abstract

Chemical sense-related lipophilic ligand-binding protein (CRLBP) is an insect odorant-binding protein (OBP) found abundantly in the taste and olfactory organs of the blowfly, Phormia regina. Through computational construction, a three-dimensional molecular model of a CRLBP indicated good fitting to a fluorescent ligand, 7-hydroxycoumarin (7-HC), in its ligand-binding pocket. By showing that the fluorescence of 7-HC bound to CRLBP migrated in a native electrophoresis gel, we confirmed that CRLBP formed a stable complex with 7-HC. In an odorant-binding experiment, 7-HC vapor odor was introduced by aeration to the aquatic solution containing CRLBP and its binding to CRLBP fluorospectrometrically quantified. Because olfactory organs as well as taste organs of flies respond to vapors, we suggest that CRLBP effectively transfers odorants from the air into aquatic surroundings by forming stable complexes with airborne molecules in both chemosensory organs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Air
  • Animals
  • Binding Sites
  • Carrier Proteins / chemistry
  • Carrier Proteins / physiology
  • Diptera
  • Insect Proteins / chemistry
  • Insect Proteins / physiology
  • Models, Molecular
  • Odorants*
  • Protein Binding
  • Receptors, Odorant / chemistry*
  • Receptors, Odorant / physiology
  • Solutions
  • Umbelliferones / chemistry
  • Water

Substances

  • CRLBP protein, Phormia regina
  • Carrier Proteins
  • Insect Proteins
  • Receptors, Odorant
  • Solutions
  • Umbelliferones
  • odorant-binding protein
  • Water
  • 7-hydroxycoumarin