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Beta-tubulin in nematodes is a highly conserved protein that, together with alpha-tubulin, forms the fundamental subunit of microtubules, which compose the cell’s cytoskeleton and are necessary for diverse processes including mitosis, intracellular transport, and neuronal structure. In nematodes such as *Ascaris lumbricoides* and *Haemonchus contortus*, multiple β-tubulin isotypes are encoded, some ubiquitously expressed, others with specialized functions or expression patterns. Benzimidazole class anthelmintics specifically bind β-tubulin, disrupting microtubule assembly and thus nematode survival; resistance arises primarily from point mutations at key residues within the drug binding site (notably F200Y and E198A). These mutations now serve as molecular markers for resistance surveillance. The essentiality and druggability of nematode β-tubulin make it a major therapeutic target in the treatment of parasitic nematode infections. If further canonical structure, gene, or protein identifiers are needed, these would be species-specific (e.g., TBB-1, TBB-2 in *C. elegans*; isotype A in *Ascaris lumbricoides*).
Drug binding at the β-tubulin site: Benzimidazoles bind to β-tubulin, preventing microtubule polymerization and causing microtubule instability, which disrupts cell division and leads to parasite death. Resistance mutations: Specific amino acid changes (e.g., F200Y, E198A) can decrease drug binding, leading to drug resistance.
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