Bioactivities of synthetic salicylate-substituted carboxyl (E)-ß-Farnesene derivatives as ecofriendly agrochemicals and their binding mechanism with potential targets in aphid olfactory system.

BACKGROUND: The aphid alarm pheromone, (E)-ß-farnesene (EßF), is a natural product secreted from the aphid cornicle as a signal to warn companions of danger. Odorant binding proteins (OBPs) are the vital targets in insect signal transduction pathways. To improve bioactivity of EßF as more economic and stable aphid control agents, EßF derivatives containing an active substructure, salicylic acid moiety, were designed, synthesized, and evaluated for their bioactivities in a structure-function study under laboratory conditions. RESULTS: EßF derivatives, (E)-3,7-dimethylocta-2,6-dien-1-yl-2-hydroxy-3-methylbenzoate and (E)-3,7-dimethylocta-2,6-dien-1-yl-2-hydroxy-3-methoxybenzoate showed outstanding aphid-repellent activity at a dose of 5 µg against Acyrthosiphon pisum (repellency proportions of 67.3% and 71.2%, respectively) and Myzus persicae (repellency proportions of 80.0% and 74.4%, respectively) in laboratory. EßF and most of its derivatives bound strongly to ApisOBP9 with a higher affinity than those of the reported potential targets AphisOBP3 and ApisOBP7. The binding affinities to these three ApisOBPs were generally consistent with the in vivo aphid-repellent activity. A molecular docking study suggested that the hydrophobic effect was crucial for the interactions between the derivatives and the OBPs. CONCLUSION: New EßF derivatives containing salicylic acid moiety and their repellent activity, binding mechanism with three potential OBPs are presented. A new OBP, ApisOBP9, was characterized as a potential EßF and EßF derivatives binding protein for the first time. The hydrophobic nature of these analogues is responsible for their activity. Two analogues 3b and 3e with outstanding aphid-repellent activity could be new leads for aphid control agents.

Gene silencing of two acetylcholinesterases reveals their cholinergic and non-cholinergic functions in Rhopalosiphum padi and Sitobion avenae.

BACKGROUD: The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. RESULTS: The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae. However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2. Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae, whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. CONCLUSIONS: These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae. It also plays a non-cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1.