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




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.


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.


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. © 2014 Society of Chemical Industry