Fasciola hepatica phosphoglyceromutase (FhPGM)

Fasciola hepatica phosphoglyceromutase (FhPGM) is a key enzyme in the glycolytic pathway of the liver fluke, a parasitic trematode that causes fascioliasis in livestock and humans (Schulman et al., 1982, PMID: 7060656). It catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a vital step for energy production within the parasite (UniProt, 2024). Unlike the cofactor-dependent phosphoglyceromutase (dPGM) found in mammals, many parasites, including F. hepatica, utilize a cofactor-independent form (iPGM) (Fraser et al., 1999). This structural difference provides a basis for selective toxicity, allowing drugs to target the parasite's metabolism without significantly affecting the host (PubMed, PMID: 10551831). The drug clorsulon is known to inhibit FhPGM, leading to a disruption of ATP synthesis and eventual death of the fluke (PubChem, CID: 68648). As resistance to frontline treatments like triclabendazole increases, FhPGM continues to be evaluated as a promising target for new anthelmintic development (NIH, 2023).

Other names

Cofactor-independent phosphoglyceromutaseiPGMPhosphoglycerate mutase2,3-bisphosphoglycerate-independent phosphoglyceromutase

Inhibition of the glycolytic pathway by blocking the conversion of 3-phosphoglycerate to 2-phosphoglycerate, leading to ATP depletion and parasite death (Schulman et al., 1982).