An Odorant-binding Protein Facilitates Odorant Transfer from Air to Hydrophilic Surroundings in the Blowfly
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...
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| Veröffentlicht in: | Chemical senses 2005-09, Vol.30 (7), p.559-564 |
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| creator | Tsuchihara, Kazuko Fujikawa, Kazuyo Ishiguro, Masaji Yamada, Takuji Tada, Chiyo Ozaki, Koichi Ozaki, Mamiko |
| description | 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. |
| doi_str_mv | 10.1093/chemse/bji049 |
| format | Article |
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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.</description><identifier>ISSN: 0379-864X</identifier><identifier>EISSN: 1464-3553</identifier><identifier>DOI: 10.1093/chemse/bji049</identifier><identifier>PMID: 16107518</identifier><identifier>CODEN: CHSED8</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Air ; Animals ; binding assay ; Binding Sites ; Biochemistry. Physiology. Immunology ; Biological and medical sciences ; Calliphoridae ; Carrier Proteins - chemistry ; Carrier Proteins - physiology ; Diptera ; Fundamental and applied biological sciences. Psychology ; Insect Proteins - chemistry ; Insect Proteins - physiology ; Insecta ; Invertebrates ; Models, Molecular ; molecular modeling ; odorant-binding protein ; Odorants ; olfactory reception ; perireceptor event ; Phormia regina ; Physiology. Development ; Protein Binding ; Receptors, Odorant - chemistry ; Receptors, Odorant - physiology ; Solutions ; Umbelliferones - chemistry ; Water</subject><ispartof>Chemical senses, 2005-09, Vol.30 (7), p.559-564</ispartof><rights>2005 INIST-CNRS</rights><rights>Copyright Oxford University Press(England) Sep 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-378b733d1fed75a9a0871f0d1a9b109d913ab3f5cafba731eff87ff83f8e67113</citedby><cites>FETCH-LOGICAL-c483t-378b733d1fed75a9a0871f0d1a9b109d913ab3f5cafba731eff87ff83f8e67113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17117245$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16107518$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsuchihara, Kazuko</creatorcontrib><creatorcontrib>Fujikawa, Kazuyo</creatorcontrib><creatorcontrib>Ishiguro, Masaji</creatorcontrib><creatorcontrib>Yamada, Takuji</creatorcontrib><creatorcontrib>Tada, Chiyo</creatorcontrib><creatorcontrib>Ozaki, Koichi</creatorcontrib><creatorcontrib>Ozaki, Mamiko</creatorcontrib><title>An Odorant-binding Protein Facilitates Odorant Transfer from Air to Hydrophilic Surroundings in the Blowfly</title><title>Chemical senses</title><addtitle>Chem. Senses</addtitle><description>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.</description><subject>Air</subject><subject>Animals</subject><subject>binding assay</subject><subject>Binding Sites</subject><subject>Biochemistry. Physiology. Immunology</subject><subject>Biological and medical sciences</subject><subject>Calliphoridae</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - physiology</subject><subject>Diptera</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - physiology</subject><subject>Insecta</subject><subject>Invertebrates</subject><subject>Models, Molecular</subject><subject>molecular modeling</subject><subject>odorant-binding protein</subject><subject>Odorants</subject><subject>olfactory reception</subject><subject>perireceptor event</subject><subject>Phormia regina</subject><subject>Physiology. Development</subject><subject>Protein Binding</subject><subject>Receptors, Odorant - chemistry</subject><subject>Receptors, Odorant - physiology</subject><subject>Solutions</subject><subject>Umbelliferones - chemistry</subject><subject>Water</subject><issn>0379-864X</issn><issn>1464-3553</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0UGP1CAYBmBiNO64evRqiIl7q8tXSoHjOO5ak0nWxDXZeCGUgsNsW0Zoo_PvxZ3RSbx4AA48ecnHi9BLIG-BSHppNnZI9rLdelLJR2gBVV0VlDH6GC0I5bIQdXV3hp6ltCUEKlqKp-gMaiCcgVig--WIb7oQ9TgVrR87P37Dn2KYrB_xtTa-95OebPpj8G3ek7MRuxgGvPQRTwE3-y6G3SZjgz_PMYb5ISjhHDJtLH7Xhx-u3z9HT5zuk31xPM_Rl-ur21VTrG8-fFwt14WpBJ0KykXLKe3A2Y4zLTURHBzpQMs2j9xJoLqljhntWs0pWOcEz4s6YWsOQM_RxSF3F8P32aZJDT4Z2_d6tGFOqhasZgzofyHwisiyZBm-_gduwxzHPIQCKUtWw8OzxQGZGFKK1qld9IOOewVE_e5KHbpSh66yf3UMndvBdid9LCeDN0egk9G9y19vfDq5PCsvK3Z62KfJ_vx7r-O9qjnlTDV3X5UQqzVp3teqob8A-riuPQ</recordid><startdate>20050901</startdate><enddate>20050901</enddate><creator>Tsuchihara, Kazuko</creator><creator>Fujikawa, Kazuyo</creator><creator>Ishiguro, Masaji</creator><creator>Yamada, Takuji</creator><creator>Tada, Chiyo</creator><creator>Ozaki, Koichi</creator><creator>Ozaki, Mamiko</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20050901</creationdate><title>An Odorant-binding Protein Facilitates Odorant Transfer from Air to Hydrophilic Surroundings in the Blowfly</title><author>Tsuchihara, Kazuko ; Fujikawa, Kazuyo ; Ishiguro, Masaji ; Yamada, Takuji ; Tada, Chiyo ; Ozaki, Koichi ; Ozaki, Mamiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-378b733d1fed75a9a0871f0d1a9b109d913ab3f5cafba731eff87ff83f8e67113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Air</topic><topic>Animals</topic><topic>binding assay</topic><topic>Binding Sites</topic><topic>Biochemistry. Physiology. Immunology</topic><topic>Biological and medical sciences</topic><topic>Calliphoridae</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - physiology</topic><topic>Diptera</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - physiology</topic><topic>Insecta</topic><topic>Invertebrates</topic><topic>Models, Molecular</topic><topic>molecular modeling</topic><topic>odorant-binding protein</topic><topic>Odorants</topic><topic>olfactory reception</topic><topic>perireceptor event</topic><topic>Phormia regina</topic><topic>Physiology. Development</topic><topic>Protein Binding</topic><topic>Receptors, Odorant - chemistry</topic><topic>Receptors, Odorant - physiology</topic><topic>Solutions</topic><topic>Umbelliferones - chemistry</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsuchihara, Kazuko</creatorcontrib><creatorcontrib>Fujikawa, Kazuyo</creatorcontrib><creatorcontrib>Ishiguro, Masaji</creatorcontrib><creatorcontrib>Yamada, Takuji</creatorcontrib><creatorcontrib>Tada, Chiyo</creatorcontrib><creatorcontrib>Ozaki, Koichi</creatorcontrib><creatorcontrib>Ozaki, Mamiko</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical senses</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsuchihara, Kazuko</au><au>Fujikawa, Kazuyo</au><au>Ishiguro, Masaji</au><au>Yamada, Takuji</au><au>Tada, Chiyo</au><au>Ozaki, Koichi</au><au>Ozaki, Mamiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An Odorant-binding Protein Facilitates Odorant Transfer from Air to Hydrophilic Surroundings in the Blowfly</atitle><jtitle>Chemical senses</jtitle><addtitle>Chem. Senses</addtitle><date>2005-09-01</date><risdate>2005</risdate><volume>30</volume><issue>7</issue><spage>559</spage><epage>564</epage><pages>559-564</pages><issn>0379-864X</issn><eissn>1464-3553</eissn><coden>CHSED8</coden><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.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>16107518</pmid><doi>10.1093/chemse/bji049</doi><tpages>6</tpages></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Air Animals binding assay Binding Sites Biochemistry. Physiology. Immunology Biological and medical sciences Calliphoridae Carrier Proteins - chemistry Carrier Proteins - physiology Diptera Fundamental and applied biological sciences. Psychology Insect Proteins - chemistry Insect Proteins - physiology Insecta Invertebrates Models, Molecular molecular modeling odorant-binding protein Odorants olfactory reception perireceptor event Phormia regina Physiology. Development Protein Binding Receptors, Odorant - chemistry Receptors, Odorant - physiology Solutions Umbelliferones - chemistry Water |
| title | An Odorant-binding Protein Facilitates Odorant Transfer from Air to Hydrophilic Surroundings in the Blowfly |
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