Emodepside is an anthelmintic, belonging to the cyclooctadepsipeptides class. It is effective against gastrointestinal nematodes. The starting material of Emodepside is a natural metabolite of the fungus Mycelia sterilia, which inhabits the leaves of Camellia japo
|Mechanism of Action||
Emodepside binds to G-protein coupled receptors called latrophilins. Following binding, the Gq protein activates the signaling molecule phospholipase C-β a protein that modulates regulatory pathways of vesicle release. The process involves Slo-1 (potassium channel). An unidentified transmitter interferes with signaling at the neuromuscular junction and affects nematode movement, feeding, and reproduction.
Researchers at Bayer in Berlin, Germany found that Emodepside directly opens a Slo-1 channel. Slo-1 deficiant C. elegans are completely resistant to Emodepside. Molecular analyses identified full length Slo-1 cDNAs of a variety of species of parasitic nemotodes, and found substantial differences among channel properties (Kulke et al, 2014).
|Spectrum||Broad-spectrum anthelmintic activity including nematodes such as Ascaris sum and C. elegans.|
|Solubility||Soluble in DMSO.|
Harder A, Holden-Dye L, Walker R, Wunderlich F (2005) Mechanisms of action of emodepside. Parasitol Res. 2005 Oct;97 Suppl 1:S1-S10 PMID 16228263
Kulke D et al (2014) Characterization of the Ca2+-gated and voltage-dependent K+-channel Slo-1 of nematodes and its interaction with emodepside. PLoS Negl. Trop. Dis. 8(12):e3401 PMID 25521608
Tyagi, R et al (2018) Small molecule inhibitors of metabolic enzymes repurposed as a new class of anthelmintics. ACS Infec. Dis. 4 (7):1130-1145
Welz C et al (2011) SLO-1-channels of parasitic nematodes reconstitute locomotor behaviour and emodepside sensitivity in Caenorhabditis elegans slo-1 loss of function mutants. PLoS Pathog. 7(4):e1001330 PMID 21490955