Caenorhabditis elegans serotonin-gated chloride channel MOD-1 as a novel drug target for anthelmintic therapy
; Corradi, Jeremias
; Bouzat, Cecilia Beatriz 
Otros responsables
Fecha
2020
Editorial
Sociedad Argentina de Biofísica
Revista
Título del libro
Nombre del evento
Primeras Jornadas Virtuales de la Sociedad Argentina de Biofísica
Fecha del evento
2020-12-03
Institución organizadora
Sociedad Argentina de Biofísica
ISSN
eISSN
ISBN
978-987-27591-8-6
Idioma
Inglés
Tipo del evento
Jornada
Clasificación temática
Palabras clave
Resumen
Serotonin-gated ion channels (5-HT3) belong to the family of Cys-loop receptors, which are pentameric proteins that mediate fast synaptic transmission. In mammals, 5-HT3 are non-selective cationic channels that can be homomeric (5-HT3A) or heteromeric. Caenorhabditis elegans is a model for the study of the nervous system and for antiparasitic drug discovery. As parasitic nematodes, C. elegans contains a homomeric 5HT-gated chloride channel, MOD-1, that modulates locomotory behavior. Due to its absence in vertebrates, MOD-1 emerges as a potential antiparasitic drug target. We deciphered its pharmacological properties and searched for novel ligands by patch clamp recordings from mammalian cells heterologously expressing MOD-1. Macroscopic currents activated by 5-HT showed that MOD-1 does not rectify, desensitizes slowly, and recovers from desensitization with a time constant of 1 s. Dose-response curves revealed an EC50 for 5-HT of about 1 µM, similar to that of human 5-HT3A receptors. However, compared to their actions as partial agonists of human 5-HT3A receptors, tryptamine showed markedly increased efficacy and 2-Me-5HT showed insignificant agonist activity at MOD-1. The typical anthelmintic drugs ivermectin (IVM), levamisole, and piperazine, which are agonists of GluCl, L-AChR and GABA receptors, respectively, did not activate MOD-1. However, IVM produced a slight and piperazine a profound inhibition of 5-HT activated MOD-1 currents. The analysis revealed that piperazine is a noncompetitive antagonist of MOD-1. To gain further insights into the molecular function of the native MOD-1, we also recorded 5HT-activated chloride channels from C. elegans neurons expressing MOD-1 and compared to those heterologously expressed in mammalian cells. The elucidation of the molecular pharmacology of MOD-1 contributes to our knowledge of the function and drug selectivity of Cys-loop receptors and to its potential as a novel target for anthelmintic therapy.
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