Bohbot J, Sobrio F, Lucas P, Nagnan-Le Meillour P
INRA Unité de Phytopharmacie et Médiateurs, Chimiques-Route de Saint-Cyr, Versailles, France.
Biochem Biophys Res Commun. 1998 Dec 18;253(2):489-94. doi: 10.1006/bbrc.1998.9806.
A new protocol of binding assay allowed us to functionally characterize two additional odorant-binding proteins in antennae of the moth Mamestra brassicae. These proteins have no N-terminal sequence homology with the moth pheromone-binding proteins and general odorant-binding proteins previously described. One of the two proteins designated MbraAOBP2 is between 60 and 73% similar in N-terminal to several proteins characterized in chemosensory organs of Diptera, Hymenoptera, Lepidoptera, and Phasmids, indicating that these proteins constitute a new group of odorant-binding proteins. A particularly high similarity between MbraAOBP2 and ejaculatory bulb specific protein III of Drosophila suggested that vaccenyl acetate could be a specific ligand for these proteins. As a matter of fact, MbraAOBP2 bound vaccenyl acetate in vitro, but we failed to detect any receptor cell in long and short sensilla trichodea of males. This protocol could be used as a rapid method to identify new odorant-binding proteins in chemosensory organs or tissues.
一种新的结合测定方案使我们能够在甘蓝夜蛾触角中对另外两种气味结合蛋白进行功能表征。这些蛋白与先前描述的蛾类信息素结合蛋白和一般气味结合蛋白在N端序列上没有同源性。这两种蛋白之一被命名为MbraAOBP2，其N端与双翅目、膜翅目、鳞翅目和竹节虫化学感受器官中鉴定出的几种蛋白有60%至73%的相似性，表明这些蛋白构成了一组新的气味结合蛋白。MbraAOBP2与果蝇射精球特异性蛋白III之间的相似性特别高，这表明醋酸乙烯酯可能是这些蛋白的特异性配体。事实上，MbraAOBP2在体外能结合醋酸乙烯酯，但我们未能在雄性长、短毛形感器中检测到任何受体细胞。该方案可作为一种快速方法，用于鉴定化学感受器官或组织中的新气味结合蛋白。
