Parascaris equorum is the only ascarid parasitic nematode in equids. In nematodes, acetylcholine receptors represent major targets for cholinergic agonist or antagonist anthelmintic drugs. Despite the large diversity of acetylcholine-receptor subunit genes present in nematodes, only a few receptor subtypes have been characterized so far. Interestingly, parasitic nematodes affecting human or animals possess two closely related genes that are essentially absent in free-living or plant parasitic species: acr-26 encodes an alpha subunit while acr-27 encodes a non-alpha subunit. Here, we cloned acr-26 and acr-27 from P. equorum. We demonstrated that the co-expression of the Peq-ACR-26 and Peq-ACR-27 subunits in Xenopus laevis oocytes resulted in a functional acetylcholine-receptor. Interestingly, affinities of Peq-26/27 AChR for pyrantel (EC50 0.32 ±0.26 μM) and morantel (EC50 0.98 ±0.26 μM) were higher than for the natural ligand ACh (EC50 34.9 ±1.1 μM). This receptor had a similar pharmacology pattern to the AChR made of ACR-26 and ACR-27 subunits from the distantly related parasite species Haemonchus contortus. Importantly, we report that the heterologous expression of Peq-acr-26 and Peq-acr-27 as transgenes in the model nematode Caenorhabditis elegans also drastically increased morantel and pyrantel sensitivity in-vivo, thus mirroring the pharmacological properties previously observed in Xenopus oocytes. Our results describe a novel class of nematode AChR representing a pharmacological target of prime interest for drug screening and relevant anthelmintic combinations.