Alpha-neurotoxin (Bungarus caeruleus) (α-NTX)

Common Krait long-chain three-finger alpha-neurotoxins are a class of potent neurotoxic proteins found in the venom of the snake Bungarus caeruleus [PubMed: 30219148]. These toxins belong to the three-finger toxin (3FTx) superfamily, characterized by a structural motif of three beta-stranded loops extending from a central core [UniProt: Family: Three-finger toxin family]. Their primary biological function is to act as high-affinity antagonists of the nicotinic acetylcholine receptors (nAChRs) located at the postsynaptic membrane of the neuromuscular junction [PubMed: 15649515]. By binding to these receptors, the toxins prevent the neurotransmitter acetylcholine from initiating muscle contraction, leading to progressive flaccid paralysis [WHO: Snakebite envenoming]. In clinical cases of envenomation, this paralysis often results in fatal respiratory failure if not treated promptly with appropriate antivenom [PubMed: 25463111]. These toxins are the primary targets for neutralization by polyvalent and monovalent antivenoms, which contain antibodies that bind and sequester the toxins [StatPearls: Snake Toxicity]. Additionally, they are widely used in pharmacological research as molecular probes to study the structure and function of acetylcholine receptors [PubMed: 11744018].

Other names

Long-chain three-finger alpha-neurotoxinCommon Krait alpha-neurotoxinPostsynaptic neurotoxin3FTxBungarotoxin

Neutralization of the toxin by antibody binding, which prevents the toxin from interacting with nicotinic acetylcholine receptors at the neuromuscular junction.