State Key Laboratory for the Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
J Insect Physiol. 2012 Jun;58(6):771-81. doi: 10.1016/j.jinsphys.2012.01.011. Epub 2012 Jan 25.
Odorant-binding proteins (OBPs) are important parts of insect olfactory systems, and sensitive olfaction is vital for phytophagous insects in host foraging. Electrophysiological studies are helpful in understanding olfactory sensing in Sitobion avenae (Hemiptera: Aphididae), but the functions of odorant-binding proteins in this insect are poorly understood. In this study, we used fluorescence competition assays to measure the binding specificities of SaveOBPs. The results showed that both SaveOBP2 and SaveOBP3 were superior to SaveOBP7 in binding green leaf volatiles. It was unexpected that SaveOBP7 bound trans-β-farnesene strongly, which was known as alarm pheromone of this species. Host volatiles were recognized much more easily by SaveOBP2, and the observed binding activity of SaveOBP2 equaled for tested green leaf volatiles. Our results imply that SaveOBP7 might play a more important role in aphid alarm pheromone discrimination.
气味结合蛋白(OBPs)是昆虫嗅觉系统的重要组成部分,而对于植食性昆虫来说,敏感的嗅觉对于寻找宿主至关重要。电生理研究有助于理解燕麦缢管蚜(半翅目:蚜科)的嗅觉感知,但该昆虫的气味结合蛋白的功能仍知之甚少。在本研究中,我们使用荧光竞争测定法来测量 SaveOBPs 的结合特异性。结果表明,SaveOBP2 和 SaveOBP3 在结合绿叶挥发物方面均优于 SaveOBP7。出乎意料的是,SaveOBP7 与反式-β-法呢烯强烈结合,而反式-β-法呢烯是该物种的警报信息素。寄主挥发物更容易被 SaveOBP2 识别,并且观察到的 SaveOBP2 的结合活性与测试的绿叶挥发物相当。我们的结果表明,SaveOBP7 可能在蚜虫警报信息素识别中发挥更重要的作用。