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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

Purification of BmP01 from venom of the scorpion Mesobuthus martensii. (A) Venom of scorpion was fractionated using Sephadex G-50 gel filtration; (B) The peak eluting at 1000–1403 min (indicated by an arrow) was further fractionated on a C18 RP-HPLC column. Ten fractions obtained were screened for pain behavioral study in mice. F1 fraction eluting at 38 min (indicated by an arrow) showed the pain inducing activity (inserted panel, n = 10); (C) F1 was fully purified on an analytical C18 RP-HPLC column with a retention gradient of ~35% acetonitrile; (D) Molecular weight of the purified peptide was determined to be 3178.6 Da by MALDI-TOF analysis.
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toxins-07-03671-f001: Purification of BmP01 from venom of the scorpion Mesobuthus martensii. (A) Venom of scorpion was fractionated using Sephadex G-50 gel filtration; (B) The peak eluting at 1000–1403 min (indicated by an arrow) was further fractionated on a C18 RP-HPLC column. Ten fractions obtained were screened for pain behavioral study in mice. F1 fraction eluting at 38 min (indicated by an arrow) showed the pain inducing activity (inserted panel, n = 10); (C) F1 was fully purified on an analytical C18 RP-HPLC column with a retention gradient of ~35% acetonitrile; (D) Molecular weight of the purified peptide was determined to be 3178.6 Da by MALDI-TOF analysis.

Mentions: In order to explore pain-producing peptides from scorpion venom, we initially isolated and applied the crude venom to Sephadex G-50 (Pharmacia Fine Chemicals, Uppsala, Sweden) column for purification. The crude venom was separated into several fractions by monitoring under ultraviolet at 280 nm (Figure 1A). Among these protein fractions, the fraction containing two peaks marked by arrow was then applied to the C18 RP-HPLC (Waters, Milford, CT, USA) column for further purification (RP-HPLC; Gemini C18 column, 5 μm particle size, 110 Å pore size, 250 × 4.6 mm). After separation of the fraction, ten fraction components (F1–F10) obtained were screened to investigate the pain behavior by observing paw licking duration in mouse model (Figure 1B). F1, the component (pointed by blue down arrow) having desired pain-producing activity was finally purified using analytical RP-HPLC on a C18 column with a retention gradient of ~35% acetonitrile (Figure 1C). The molecular weight of the purified peptide was 3178.6 Da, determined by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (Bruker Daltonik GmbH, Leipzig, Germany) (Figure 1D).


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)

Purification of BmP01 from venom of the scorpion Mesobuthus martensii. (A) Venom of scorpion was fractionated using Sephadex G-50 gel filtration; (B) The peak eluting at 1000–1403 min (indicated by an arrow) was further fractionated on a C18 RP-HPLC column. Ten fractions obtained were screened for pain behavioral study in mice. F1 fraction eluting at 38 min (indicated by an arrow) showed the pain inducing activity (inserted panel, n = 10); (C) F1 was fully purified on an analytical C18 RP-HPLC column with a retention gradient of ~35% acetonitrile; (D) Molecular weight of the purified peptide was determined to be 3178.6 Da by MALDI-TOF analysis.
© Copyright Policy
Related In: Results  -  Collection

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

toxins-07-03671-f001: Purification of BmP01 from venom of the scorpion Mesobuthus martensii. (A) Venom of scorpion was fractionated using Sephadex G-50 gel filtration; (B) The peak eluting at 1000–1403 min (indicated by an arrow) was further fractionated on a C18 RP-HPLC column. Ten fractions obtained were screened for pain behavioral study in mice. F1 fraction eluting at 38 min (indicated by an arrow) showed the pain inducing activity (inserted panel, n = 10); (C) F1 was fully purified on an analytical C18 RP-HPLC column with a retention gradient of ~35% acetonitrile; (D) Molecular weight of the purified peptide was determined to be 3178.6 Da by MALDI-TOF analysis.
Mentions: In order to explore pain-producing peptides from scorpion venom, we initially isolated and applied the crude venom to Sephadex G-50 (Pharmacia Fine Chemicals, Uppsala, Sweden) column for purification. The crude venom was separated into several fractions by monitoring under ultraviolet at 280 nm (Figure 1A). Among these protein fractions, the fraction containing two peaks marked by arrow was then applied to the C18 RP-HPLC (Waters, Milford, CT, USA) column for further purification (RP-HPLC; Gemini C18 column, 5 μm particle size, 110 Å pore size, 250 × 4.6 mm). After separation of the fraction, ten fraction components (F1–F10) obtained were screened to investigate the pain behavior by observing paw licking duration in mouse model (Figure 1B). F1, the component (pointed by blue down arrow) having desired pain-producing activity was finally purified using analytical RP-HPLC on a C18 column with a retention gradient of ~35% acetonitrile (Figure 1C). The molecular weight of the purified peptide was 3178.6 Da, determined by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (Bruker Daltonik GmbH, Leipzig, Germany) (Figure 1D).

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