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Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel.

Hakim MA, Jiang W, Luo L, Li B, Yang S, Song Y, Lai R - Toxins (Basel) (2015)

Bottom Line: Furthermore, OPEN ACCESS Toxins 2015, 7 3672 BmP01 evoked currents on TRPV1-expressed HEK293T cells, but not on HEK293T cells without TRPV1.These results suggest that (1) BmP01 is one of the pain-inducing agents in scorpion venoms; and (2) BmP01 induces pain by acting on TRPV1.To our knowledge, this is the first report about a scorpion toxin that produces pain by targeting TRPV1.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China. hakeem.geb.ru@gmail.com.

ABSTRACT
The intense pain induced by scorpion sting is a frequent clinical manifestation. To date, there is no established protocol with significant efficacy to alleviate the pain induced by scorpion envenomation. One of the important reasons is that, little information on pain-inducing compound from scorpion venoms is available. Here, a pain-inducing peptide (BmP01) has been identified and characterized from the venoms of scorpion (Mesobuthus martensii). In an animal model, intraplantar injection of BmP01 in mouse hind paw showed significant acute pain in wild type (WT) mice but not in TRPV1 knock-out (TRPV1 KO) mice during 30 min recording. BmP01 evoked currents in WT dorsal root ganglion (DRG) neurons but had no effect on DRG neurons of TRPV1 KO mice. Furthermore, OPEN ACCESS Toxins 2015, 7 3672 BmP01 evoked currents on TRPV1-expressed HEK293T cells, but not on HEK293T cells without TRPV1. These results suggest that (1) BmP01 is one of the pain-inducing agents in scorpion venoms; and (2) BmP01 induces pain by acting on TRPV1. To our knowledge, this is the first report about a scorpion toxin that produces pain by targeting TRPV1. Identification of a pain-inducing compound may facilitate treating pain induced by scorpion envenomation.

No MeSH data available.


Related in: MedlinePlus

The sequence and structure of BmP01. (A) Sequence of cDNA encoding BmP01, the signal peptide (underlined) is of 28 amino acids in length, and the mature peptide consists of 29 amino acids, designated with white text on a blue background; (B) The 3D-structure of BmP01 is provided from Protein Data Bank (Protein Data Bank code 1WM7); (C) Alignment of purified BmP01 with three previously reported peptides from scorpion. They contain the same number of amino acids and disulfide bonds.
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toxins-07-03671-f002: The sequence and structure of BmP01. (A) Sequence of cDNA encoding BmP01, the signal peptide (underlined) is of 28 amino acids in length, and the mature peptide consists of 29 amino acids, designated with white text on a blue background; (B) The 3D-structure of BmP01 is provided from Protein Data Bank (Protein Data Bank code 1WM7); (C) Alignment of purified BmP01 with three previously reported peptides from scorpion. They contain the same number of amino acids and disulfide bonds.

Mentions: The partial N-terminal sequence, determined by automatic Edman degradation, ATCEDCPEHCATQNARAK was used for designing degenerate primers (Table 1) in order to clone the signal and mature peptide sequence from cDNA library. By cloning the gene from venom-gland cDNA library, the complete transcript of BmP01 was identified, revealing that the toxin is translated as a larger precursor of 57 amino acids in length and the mature peptide is yielded during post-translational modification by cleaving off a signal peptide consisting 28 amino acids (Figure 2A). In Figure 2A, the full cDNA and amino acid sequence of this peptide suggest that the peptide we purified is BmP01, which is confirmed by NCBI protein blast. BmP01, an ICK motif toxin with alpha helix and beta sheet, contains three di-sulfide bridges (Figure 2B). The alignment of the mature peptide sequence of BmP01 showed some homologues from other scorpion venoms (Figure 2C).


Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel.

Hakim MA, Jiang W, Luo L, Li B, Yang S, Song Y, Lai R - Toxins (Basel) (2015)

The sequence and structure of BmP01. (A) Sequence of cDNA encoding BmP01, the signal peptide (underlined) is of 28 amino acids in length, and the mature peptide consists of 29 amino acids, designated with white text on a blue background; (B) The 3D-structure of BmP01 is provided from Protein Data Bank (Protein Data Bank code 1WM7); (C) Alignment of purified BmP01 with three previously reported peptides from scorpion. They contain the same number of amino acids and disulfide bonds.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4591660&req=5

toxins-07-03671-f002: The sequence and structure of BmP01. (A) Sequence of cDNA encoding BmP01, the signal peptide (underlined) is of 28 amino acids in length, and the mature peptide consists of 29 amino acids, designated with white text on a blue background; (B) The 3D-structure of BmP01 is provided from Protein Data Bank (Protein Data Bank code 1WM7); (C) Alignment of purified BmP01 with three previously reported peptides from scorpion. They contain the same number of amino acids and disulfide bonds.
Mentions: The partial N-terminal sequence, determined by automatic Edman degradation, ATCEDCPEHCATQNARAK was used for designing degenerate primers (Table 1) in order to clone the signal and mature peptide sequence from cDNA library. By cloning the gene from venom-gland cDNA library, the complete transcript of BmP01 was identified, revealing that the toxin is translated as a larger precursor of 57 amino acids in length and the mature peptide is yielded during post-translational modification by cleaving off a signal peptide consisting 28 amino acids (Figure 2A). In Figure 2A, the full cDNA and amino acid sequence of this peptide suggest that the peptide we purified is BmP01, which is confirmed by NCBI protein blast. BmP01, an ICK motif toxin with alpha helix and beta sheet, contains three di-sulfide bridges (Figure 2B). The alignment of the mature peptide sequence of BmP01 showed some homologues from other scorpion venoms (Figure 2C).

Bottom Line: Furthermore, OPEN ACCESS Toxins 2015, 7 3672 BmP01 evoked currents on TRPV1-expressed HEK293T cells, but not on HEK293T cells without TRPV1.These results suggest that (1) BmP01 is one of the pain-inducing agents in scorpion venoms; and (2) BmP01 induces pain by acting on TRPV1.To our knowledge, this is the first report about a scorpion toxin that produces pain by targeting TRPV1.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China. hakeem.geb.ru@gmail.com.

ABSTRACT
The intense pain induced by scorpion sting is a frequent clinical manifestation. To date, there is no established protocol with significant efficacy to alleviate the pain induced by scorpion envenomation. One of the important reasons is that, little information on pain-inducing compound from scorpion venoms is available. Here, a pain-inducing peptide (BmP01) has been identified and characterized from the venoms of scorpion (Mesobuthus martensii). In an animal model, intraplantar injection of BmP01 in mouse hind paw showed significant acute pain in wild type (WT) mice but not in TRPV1 knock-out (TRPV1 KO) mice during 30 min recording. BmP01 evoked currents in WT dorsal root ganglion (DRG) neurons but had no effect on DRG neurons of TRPV1 KO mice. Furthermore, OPEN ACCESS Toxins 2015, 7 3672 BmP01 evoked currents on TRPV1-expressed HEK293T cells, but not on HEK293T cells without TRPV1. These results suggest that (1) BmP01 is one of the pain-inducing agents in scorpion venoms; and (2) BmP01 induces pain by acting on TRPV1. To our knowledge, this is the first report about a scorpion toxin that produces pain by targeting TRPV1. Identification of a pain-inducing compound may facilitate treating pain induced by scorpion envenomation.

No MeSH data available.


Related in: MedlinePlus