Acetylcholinesterase 1 (AChE1) (AChE1)

Acetylcholinesterase 1 (AChE1) is a critical enzyme in the nervous system of the head louse (Pediculus humanus capitis), where it terminates signal transmission by rapidly hydrolyzing the neurotransmitter acetylcholine at cholinergic synapses (Source: PubMed, PMID: 22403132). In lice, this enzyme is the primary functional cholinesterase and serves as the major therapeutic target for organophosphate and carbamate pediculicides (Source: Journal of Medical Entomology). Inhibition of AChE1 leads to a toxic accumulation of acetylcholine in the synaptic cleft, causing continuous stimulation of the insect's nervous system, which results in neuromuscular paralysis and death (Source: StatPearls). This target is of significant clinical importance due to the widespread emergence of resistance, often mediated by specific point mutations in the ace1 gene, such as T82M, H331Y, and L428F, which reduce the enzyme's sensitivity to insecticides (Source: Pesticide Biochemistry and Physiology). Because human acetylcholinesterase differs structurally and metabolically from the louse enzyme, certain inhibitors like malathion can be used with a high margin of safety in humans (Source: PubChem). Understanding the molecular architecture of louse AChE1 is essential for the design of next-generation pediculicides capable of overcoming existing resistance mechanisms (Source: Parasitology Research).

Other names

AChEAcetylcholine esteraseAce1-like proteinCholinesterase

Inhibition of the acetylcholinesterase enzyme, preventing the hydrolysis of acetylcholine, leading to neuromuscular overstimulation and paralysis (Source: StatPearls).