{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T00:40:57Z","timestamp":1777509657102,"version":"3.51.4"},"update-to":[{"DOI":"10.12688\/f1000research.5879.1","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2015,1,9]],"date-time":"2015-01-09T00:00:00Z","timestamp":1420761600000}}],"reference-count":43,"publisher":"F1000 Research Ltd","license":[{"start":{"date-parts":[[2015,1,9]],"date-time":"2015-01-09T00:00:00Z","timestamp":1420761600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["f1000research.com"],"crossmark-restriction":false},"short-container-title":["F1000Res"],"abstract":"<ns4:p>\n                    Odorant-binding proteins (OBPs), also named pheromone-binding proteins when the odorant is a pheromone, are essential for insect olfaction. They solubilize odorants that reach the port of entry of the olfactory system, the pore tubules in antennae and other olfactory appendages. Then, OBPs transport these hydrophobic compounds through an aqueous sensillar lymph to receptors embedded on dendritic membranes of olfactory receptor neurons. Structures of OBPs from mosquito species have shed new light on the mechanism of transport, although there is considerable debate on how they deliver odorant to receptors. An OBP from the southern house mosquito,\n                    <ns4:italic>Culex quinquefasciatus,<\/ns4:italic>\n                    binds the hydrophobic moiety of a mosquito oviposition pheromone (MOP) on the edge of its binding cavity. Likewise, it has been demonstrated that the orthologous protein from the malaria mosquito binds the insect repellent DEET on a similar edge of its binding pocket. A high school research project was aimed at testing whether the orthologous protein from the yellow fever mosquito, AaegOBP1, binds DEET and other insect repellents, and MOP was used as a positive control. Binding assays using the fluorescence reporter N-phenyl-1-naphtylamine (NPN) were inconclusive. However, titration of NPN fluorescence emission in AaegOBP1 solution with MOP led to unexpected and intriguing results. Quenching was observed in the initial phase of titration, but addition of higher doses of MOP led to a stepwise increase in fluorescence emission coupled with a blue shift, which can be explained at least in part by formation of MOP micelles to house stray NPN molecules.\n                  <\/ns4:p>","DOI":"10.12688\/f1000research.5879.2","type":"journal-article","created":{"date-parts":[[2015,1,9]],"date-time":"2015-01-09T11:55:15Z","timestamp":1420804515000},"page":"305","update-policy":"https:\/\/doi.org\/10.12688\/f1000research.crossmark-policy","source":"Crossref","is-referenced-by-count":17,"title":["Binding of a fluorescence reporter and a ligand to an odorant-binding protein of the yellow fever mosquito, Aedes aegypti"],"prefix":"10.12688","volume":"3","author":[{"given":"Gabriel M.","family":"Leal","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Walter 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Leal","year":"2014","journal-title":"F1000Research."}],"container-title":["F1000Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/f1000research.com\/articles\/3-305\/v2\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/f1000research.com\/articles\/3-305\/v2\/pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/f1000research.com\/articles\/3-305\/v2\/iparadigms","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,12,4]],"date-time":"2018-12-04T15:00:28Z","timestamp":1543935628000},"score":1,"resource":{"primary":{"URL":"https:\/\/f1000research.com\/articles\/3-305\/v2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,1,9]]},"references-count":43,"URL":"https:\/\/doi.org\/10.12688\/f1000research.5879.2","relation":{"has-review":[{"id-type":"doi","id":"10.5256\/f1000research.6433.r7334","asserted-by":"subject"},{"id-type":"doi","id":"10.5256\/f1000research.6433.r7334","asserted-by":"object"}]},"ISSN":["2046-1402"],"issn-type":[{"value":"2046-1402","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,1,9]]},"assertion":[{"value":"Indexed","URL":"https:\/\/f1000research.com\/articles\/3-305\/v2#article-reports","order":0,"name":"referee-status","label":"Referee status","group":{"name":"current-referee-status","label":"Current Referee Status"}},{"value":"10.5256\/f1000research.6433.r7334, Kostas Iatrou, Spyros Zographos, Institute of Biosciences and Applications, National Center for Scientific Research \u201cDemokritos\u201d, Athens, Greece, 22 Jan 2015, version 2, indexed","URL":"https:\/\/f1000research.com\/articles\/3-305\/v2#referee-response-7334","order":0,"name":"referee-response-7334","label":"Referee Report","group":{"name":"article-reports","label":"Article Reports"}},{"value":"10.5256\/f1000research.6281.r7176, Paolo Pelosi, Department of Chemistry and Agricultural Biotechnology, University of Pisa, Pisa, Italy, 02 Jan 2015, version 1, 1 approved, 1 approved with reservations","URL":"https:\/\/f1000research.com\/articles\/3-305\/v1#referee-response-7176","order":1,"name":"referee-response-7176","label":"Referee Report","group":{"name":"article-reports","label":"Article Reports"}},{"value":"<b>Walter Leal<\/b>; \n<i>Posted: 02 Jan 2015<\/i>; We appreciate your time and effort to evaluate our article, and are delighted to hear that it meets your approval. We will certainly cite Sun \n<i>et al.<\/i> (2012) in the revised version of the article. The apparent formation of (E)-&szlig;-farnesene micelle, as shown in your Figure 5, skipped our attention, perhaps because this phenomenon has never been examined and explained in detail. We will certainly give the appropriate credit in the revised version. Regarding your minor concern, we have verified wavelength accuracy per vendor\u2019s instruction manual. We are, therefore, confident that the data set reported is accurate. It is worth pointing out, however, that apparent discrepancies may be explained at least in part by the proteins studied. For AaegOBP1, the NPN peaks at pH values 7 and 5 are quite different (our Figure 6), but in the presence of CquiOBP1 (Figure 5 in Leal \n<i>et al,<\/i> 2008) or AfunOBP1 (Figure 9, Xu\n<i> et al.<\/i>, 2010) the wavelength for the peaks at high and low pH are nearly the same, i.e., ca. 400 nm. All these studies were performed in our laboratory with the same instrument. Again, thank you very much for your suggestions. Sincerely, WSL &amp; GML","URL":"https:\/\/f1000research.com\/articles\/3-305\/v2#referee-comment-1156","order":2,"name":"referee-comment-1156","label":"Referee Comment","group":{"name":"article-reports","label":"Article Reports"}},{"value":"This work was supported in part from unrestricted gifts from Fuji Flavor Co. and Bedoukian Research Inc.","order":3,"name":"grant-information","label":"Grant Information"},{"value":"This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.Data associated with the article are available under the terms of the Creative Commons Zero \"No rights reserved\" data waiver (CC0 1.0 Public domain dedication).","order":0,"name":"copyright-info","label":"Copyright"}]}}