Culex pipiens acetylcholinesterase 1 (AChE1)

Culex pipiens acetylcholinesterase 1 (AChE1), encoded by the ace-1 gene, is a critical enzyme in the nervous system of the common house mosquito. It functions by rapidly hydrolyzing the neurotransmitter acetylcholine at cholinergic synapses, thereby terminating nerve impulses and preventing continuous stimulation of postsynaptic receptors [20, 21]. AChE1 is the primary target for two major classes of synthetic insecticides: organophosphates and carbamates. These compounds covalently bind to the catalytic serine residue, leading to enzyme inhibition, acetylcholine accumulation, and eventual paralysis and death of the insect [2, 9, 10]. The target is of significant public health importance because Culex pipiens serves as a primary vector for several human and animal pathogens, including West Nile virus, St. Louis encephalitis virus, and filarial worms [18, 19]. However, the widespread use of insecticides has led to the emergence of resistance, primarily through target-site mutations such as G119S and F290V, which reduce the enzyme's sensitivity to inhibitors [1, 4, 5]. Current research focuses on developing novel, mosquito-specific inhibitors that target unique structural features, such as the invertebrate-specific Cys286 residue, to improve selectivity and overcome existing resistance mechanisms while minimizing toxicity to non-target organisms like humans [11, 12, 13].

Other names

Acetylcholinesterase 1AChE1ace-1Synaptic acetylcholinesterase

Inhibition of acetylcholinesterase activity through covalent binding to the catalytic serine residue, leading to acetylcholine accumulation and neuromuscular paralysis.