Fasciola hepatica beta-tubulin (FhBT)

Fasciola hepatica beta-tubulin is a critical structural protein in the common liver fluke, where it dimerizes with alpha-tubulin to form microtubules. These microtubules are essential for maintaining the parasite's cellular architecture, facilitating intracellular transport, and enabling cell division during growth and reproduction (PMID: 15910978). In the context of fascioliasis, a food-borne trematode infection, beta-tubulin serves as the primary molecular target for benzimidazole anthelmintics, most notably triclabendazole. These drugs selectively bind to the helminth tubulin, inhibiting polymerization and leading to metabolic exhaustion and tegumental damage in the fluke (PMID: 18433490). However, the widespread use of these treatments has led to significant clinical challenges, specifically the development of drug resistance linked to specific single nucleotide polymorphisms (SNPs) in the beta-tubulin gene, such as the F200Y mutation (PMID: 25108100). Understanding the structural variations of this target is vital for developing next-generation flukicides and diagnostic tools for monitoring resistance in livestock and human populations.

Other names

Tubulin beta chainBeta-tubulin isotype 1Beta-tubulin isotype 2Beta-tubulin isotype 3F. hepatica beta-tubulin

Benzimidazole drugs bind to the beta-tubulin subunit of the tubulin heterodimer, preventing its polymerization into microtubules. This disruption of the microtubule network inhibits essential cellular processes such as mitosis, intracellular transport, and glucose uptake, eventually leading to the death of the parasite (PMID: 11113252, PMID: 28606210).