Helminth beta-tubulin (TUBB)

Helminth beta-tubulin is a vital structural protein found in parasitic worms, including nematodes, cestodes, and trematodes. It functions by forming heterodimers with alpha-tubulin to assemble microtubules, which are essential cytoskeletal components involved in cell division, intracellular transport, and the maintenance of cellular architecture [1, 3]. This protein serves as the primary therapeutic target for the benzimidazole class of broad-spectrum anthelmintic drugs, such as albendazole and mebendazole [1, 4]. These compounds bind specifically to helminth beta-tubulin, inhibiting microtubule polymerization and causing lethal disruption to the parasite's physiological processes [1, 12]. A significant challenge in the clinical use of these drugs is the development of resistance, which is frequently associated with single nucleotide polymorphisms (SNPs) at specific amino acid residues, notably codons 167, 198, and 200 [5, 16]. These mutations reduce the binding affinity of the drugs to the tubulin molecule, necessitating the ongoing surveillance of resistance markers and the development of novel antiparasitic strategies [3, 7].

Other names

Parasitic beta-tubulinTubulin beta chainBeta-tubulin isotype 1BEN-1Helminthic beta-tubulin

Benzimidazole drugs bind to the colchicine-binding site of helminth beta-tubulin, inhibiting its polymerization into microtubules. This disruption of microtubule dynamics arrests essential cellular processes such as mitosis and intracellular transport, leading to the depletion of energy reserves (e.g., glucose uptake inhibition) and the eventual death of the parasite [1, 2, 10].