Abstract
It was recently discovered that Ssm Spooky Toxin (SsTx) with 53 residues serves as a key killer factor in red-headed centipede’s venom arsenal, due to its potent blockage of the widely expressed KCNQ channels to simultaneously and efficiently disrupt cardiovascular, respiratory, muscular, and nervous systems, suggesting that SsTx is a basic compound for centipedes’ defense and predation. Here, we show that SsTx also inhibits KV1.3 channel, which would amplify the broad-spectrum disruptive effect of blocking KV7 channels. Interestingly, residue R12 in SsTx extends into the selectivity filter to block KV7.4, however, residue K11 in SsTx replaces this ploy when toxin binds on KV1.3. Both SsTx and its mutant SsTx_R12A inhibit cytokines production in T cells without affecting the level of KV1.3 expression. The results further suggest that SsTx is a key molecule for defense and predation in the centipedes’ venoms and it evolves efficient strategy to disturb multiple physiological targets.
Highlights
With over 3000 species, centipedes, arthropods of the class Chilopoda are widely distributed in both tropical and subtropical regions
SsTxThrough used different side chains of to toxin targetmutants, KV1.3, which allowed usSsTx to modify them towards diseases the construction we found that used different side targeting
SsTxAsconsists of in53ouramino acids refolded by twoprey intracellular bonds
Summary
With over 3000 species, centipedes, arthropods of the class Chilopoda are widely distributed in both tropical and subtropical regions. Their first pair of legs have been modified into strong mandibles and venomous fangs called forcipules that play a critical role in defense and predation [1]. We have identified and characterized several peptide toxins from centipede venom and established they act on ion channels that are associated with pain and inflammation [3,4,5,6,7]. A centipede toxin (RhTx) causes intense local pain by targeting the heat activation machinery of nociceptor TRPV1
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