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Beta-tubulin (Fasciola spp.) is a vital structural protein in liver flukes, including Fasciola hepatica and Fasciola gigantica, serving as a primary target for anthelmintic therapy (Robinson et al., 2001). It forms heterodimers with alpha-tubulin to polymerize into microtubules, which are essential for maintaining the parasite's cytoskeleton, facilitating intracellular transport, and supporting the integrity of the tegument (Patsnap, 2024). Benzimidazole drugs, most notably triclabendazole and albendazole, exert their parasiticidal effects by binding to beta-tubulin and inhibiting microtubule assembly (MDPI, 2023). Triclabendazole is uniquely effective against both immature and adult stages of the fluke, making it the cornerstone of fascioliasis treatment (ResearchGate, 2017). However, the emergence of widespread resistance, often linked to genetic variations in beta-tubulin isotypes, presents a major challenge to disease control in both livestock and humans (Cambridge Core, 2013). Research into the six known isotypes of beta-tubulin in F. hepatica continues to inform the development of novel therapeutics to overcome resistance (Acta Parasitologica, 2023). The protein's role in cell division and metabolic processes makes its disruption lethal to the parasite, while selective toxicity is achieved through higher drug affinity for fluke tubulin compared to host tubulin (Patsnap, 2024).
Inhibition of tubulin polymerization and microtubule assembly, leading to disruption of the parasite's cytoskeleton and tegument (Patsnap, 2024; MDPI, 2023).
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