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Beta-tubulin is a fundamental structural protein that polymerizes with alpha-tubulin to form microtubules, which are essential for various cellular processes including mitosis, intracellular transport, and maintenance of cell shape (UniProt, P16245). In parasites such as helminths and protozoa, beta-tubulin serves as a critical therapeutic target for anthelmintic drugs like benzimidazoles (e.g., albendazole and mebendazole) (PubMed, PMID: 3255811). These drugs selectively bind to the parasite's beta-tubulin, inhibiting the polymerization of microtubules and leading to the disruption of glucose uptake and eventual death of the organism (StatPearls, NBK553087). The selectivity of these agents is primarily due to the higher affinity for the parasite isoform compared to the mammalian host's beta-tubulin (PubMed, PMID: 15530334). However, the clinical utility of these drugs is increasingly threatened by the development of resistance, often linked to specific point mutations in the beta-tubulin gene, such as the F200Y substitution (PubMed, PMID: 24508212).
Inhibition of microtubule polymerization by binding to the beta-tubulin subunit, which prevents the addition of tubulin dimers to growing microtubules, leading to the loss of cytoplasmic microtubules and disruption of essential cellular functions such as mitosis and nutrient transport (PubMed, PMID: 3255811).
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