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The venom composition of the deathstalker scorpion contains neurotoxins which are almost completely responsible for this symptom. The poison from this scorpion contain 4 components: chlorotoxin, charybdotoxin, scyllatoxin, and agitoxins. Upon injection with the venom, sacral parasympathetic nerve are stimulated causing a change in the neuronal ...
Tityustoxin-1, TsTX-I is the most toxic protein among the neurotoxins in this venom, with an intravenous and intracisternal LD 50 (mouse) of 76 ± 9 and 1.1 ± 0.3 μg/kg, respectively. The identification of TsTX-I as a potent component of T. serrulatus venom characterized it as the major and main neurotoxin from this venom. [1]
Charybdotoxin (ChTX) is a 37 amino acid neurotoxin from the venom of the scorpion Leiurus quinquestriatus hebraeus (deathstalker) that blocks calcium-activated potassium channels. [2] This blockade causes hyperexcitability of the nervous system. It is a close homologue of agitoxin and both toxins come from Leiurus quinquestriatus hebraeus.
About 25 species (fewer than one percent) have venom capable of killing a human, which happens frequently in the parts of the world where they live, primarily where access to medical treatment is unlikely. Scorpions appear in art, folklore, mythology, and commercial brands. Scorpion motifs are woven into kilim carpets for protection from their ...
Chlorotoxin is a 36-amino acid peptide found in the venom of the deathstalker scorpion (Leiurus quinquestriatus) which blocks small-conductance chloride channels. [2] The fact that chlorotoxin binds preferentially to glioma cells has allowed the development of methods for the treatment and diagnosis of several types of cancer.
The deathstalker is one of the most dangerous species of scorpions. [10] [11] Its venom is a powerful mixture of neurotoxins, with a low lethal dose. [12]While a sting from this scorpion is extraordinarily painful, it normally would not kill a healthy adult human.
Scorpion toxins are proteins found in the venom of scorpions.Their toxic effect may be mammal- or insect-specific and acts by binding with varying degrees of specificity to members of the Voltage-gated ion channel superfamily; specifically, voltage-gated sodium channels, voltage-gated potassium channels, [3] and Transient Receptor Potential (TRP) channels.
NTX accounts for only about 1% of the scorpion venom. [7] NTX is one of the best-studied toxic peptides from scorpion venoms. [6] It was the second purified toxin obtained from the genus Centruroides after neurotoxin II [8] and the first short peptide from scorpion venom to be reported in the literature. [9]