动植物关系组知识库

Eastern honeybee Apis cerana has important ecological value for the cold flowering loquat flower pollination in early winter in East Asia. However, the low-temperature adaptive pollination mechanism has not yet been revealed. One odorant-binding protein, OBP2, had been found that could bind to some plant volatiles with strong affinity before. In this study, by using competitive fluorescence binding assay, we first measured the ligand-binding profiles of recombinant OBP2 protein with nine representative aroma chemical substances from loquat flowers. Thermodynamic results showed that three loquat volatiles, 4-Methoxybenzaldehyde, (E)-Ethyl cinnamate, and Methyl cinnamate, have the strongest binding affinity with OBP2 with the static process. And interestingly their binding affinity significantly increased at low temperature (285 K/12 degrees C) compared to high temperature (298 K/25 degrees C). In addition, site-directed mutagenesis results showed that Met55 and Lys51 may be the key amino acid sites in the electrostatic and hydrophobic interactions of OBP2 interacting with Methyl cinnamate, respectively. This study suggests that OBP2 is functionally similar and universal in binding to different flower volatiles at low temperatures. Our studies interpreted a novel olfactory mechanism of A. cerana sensing loquat floral volatiles in cold early winter, and enrich a theoretical molecular basis for the temperature-adaptive ecological mechanism of insects' pollination.