Chemical Senses Advance Access originally published online on August 17, 2005
Chemical Senses 2005 30(7):559-564; doi:10.1093/chemse/bji049
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An Odorant-binding Protein Facilitates Odorant Transfer from Air to Hydrophilic Surroundings in the Blowfly
1 Human Information Systems, Kanazawa Institute of Technology, 3-1 Yakkaho, Hakusan, Ishikawa 924-0834, Japan, 2 National Institute of Agrobiological Sciences, 3 Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan, 4 Suntory Institute for Bioorganic Research, Shimamoto-cho, Osaka 618-8503, Japan and 5 Graduate School of Frontier Biosciences, Osaka University, Machikaneyama, Toyonaka, Osaka 560-0043, Japan
Correspondence to be sent to: Mamiko Ozaki, Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Kyoto 606-8585, Japan. e-mail: mamiko{at}kit.ac.jp
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.
Key words: binding assay, molecular modeling, odorant-binding protein, olfactory reception, perireceptor event
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