Scorpion Stings Repel Its Predator (Video by LAI Ren's Team)
Venom is evolved to arm many otherwise defenseless animals with a lethal weapon, and is secreted by animals such as snakes, centipedes, scorpions and spiders.
Scorpion stings are well known to be extremely painful, however, why scorpion stings produce an insufferable pain remains unknown worldwide due to the lack of understanding of molecular base.
A recent study conducted by LAI Ren and his colleagues at Kunming Institute of Zoology of Chinese Academy of Sciences, UC Davis in USA and Zhejiang University revealed this molecular mechanism, and the results were published in Science Advances.
Like tasting red chili pepper, scorpion toxin BmP01, a 29-amino acid peptide, can activate capsaicin receptor (TRPV1) and induce burning pain. However, BmP01-induced TRPV1 activation is highly acid related and acts as a “one-two” punch mechanism.
Similar to most venoms, scorpion venom is weakly acidic (pH 6.5). Under acidic conditions, the E601 sites of TRPV1 are found to be first occupied by protons, which makes TRPV1 ready to open.
Subsequently, occupying E649 by BmP01 can easily produce strong channel activation and an insufferable pain. On the contrary, BmP01 is not a potent activator at neutral pH because it occupies only the E649 site.
Researchers suggested the functional and evolutionary importance of the venom acidity in scorpion toxin-induced pain. These data also offered some clues for clinical treatment of scorpion stings.
Scorpions’ Defense Mechanism (Image by LAI Ren’s Team)
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