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Other snake venom toxins refers to a heterogeneous collection of bioactive proteins and peptides found in snake venoms that are distinct from the major toxin families such as phospholipases A2 (PLA2s), three-finger toxins (3FTxs), and snake venom metalloproteinases (SVMPs). This category includes diverse molecules such as hyaluronidases, which act as spreading factors by degrading the extracellular matrix, and cysteine-rich secretory proteins (CRISPs) that can inhibit various ion channels [1, 2]. Other components include L-amino acid oxidases (LAAOs) that induce oxidative stress and apoptosis, as well as Kunitz-type serine protease inhibitors and nerve growth factors [3]. These toxins contribute significantly to the clinical manifestations of snakebite envenomation, including local tissue necrosis, systemic hemorrhage, and neurotoxicity [4]. While antivenoms are the standard treatment used to neutralize these toxins through antibody binding, some specific toxins within this group are being investigated as potential leads for drug discovery in areas like anticoagulation and pain management [5].
Antivenoms neutralize these toxins by binding to their epitopes, preventing interaction with host receptors or substrates. Small molecule inhibitors like varespladib or metalloproteinase inhibitors (e.g., marimastat) bind to the catalytic sites of specific enzymatic toxins to block their activity [4, 5].
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