Purification and characterization of a novel short-chain insecticidal toxin with two disulfide bridges from the venom of the scorpion Liocheles australasiae

Matsushita, Nobuto; Miyashita, Masahiro; Sakai, Atsushi; Nakagawa, Yoshiaki; Miyagawa, Hisashi

doi:10.1016/j.toxicon.2007.06.014

Cited by 32 publications

(15 citation statements)

References 28 publications

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“…These short-chain toxins are composed of 30 to 40 amino acid residues and are mainly cross-linked by two or four disulfide bridges that are mostly active on K + or Cl -and Ca 2+ channels (7)(8)(9). In such groups we can find a short toxin with four disulfide bonds called chlorotoxin, a chloride-channel blocking toxin extracted from the scorpion Leiurus quinquestriatus (10)(11)(12).…”

Section: Introductionmentioning

confidence: 99%

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Comparison of two purified toxic fractions from Mesobuthus eupeus scorpion venom

Shirmardi¹,

Shamsaei²,

Ghanei³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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Abstract:Iranian scorpions belong mainly to the Buthidae and Scorpionidae families, distributed into 16 genera and 25 species. In Iran, similar to other parts of the world, there are a few known species of scorpions responsible for severe envenoming; amongst which Mesobuthus eupeus is the most common. Its venom contains several toxin fractions that may affect the ion channel. In the present study purification, labeling and biological evaluation of M. eupeus venom are described. For separation, soluble venom was loaded on a chromatography column packed with Sephadex G-50 gel. Subsequently, the fractions were collected according to UV absorption at a wavelength of 280 nm. Toxic fraction (F3) was loaded on an anionic ion exchanger resin and then on a cationic resin. Finally, toxic subfractions F3.1.6 and F3.1.9 were labeled with 99m Tc and injected into normal mice to distinguish excretion pathway. The venom toxic fraction was successfully obtained in its purified form. Radiolabeling of toxic fractions was performed at high specific activity with radiochemical purity of more than 97 and 95% respectively for F3.1.6 and F3.1.9. Biodistribution studies in normal mice with two toxic fractions usually show rapid clearance of the compounds from blood and tissue except for kidneys. Since tissue distribution studies are very important for clinical purpose, the present findings suggest that 99m Tc labeling of venom is a useful tool for in vivo studies and comprises an excellent approach to monitoring the process of biodistribution and kinetics of toxins.

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Section: Introductionmentioning

confidence: 99%

“…The main focus has been placed on the Buthidae family because some species within this family possess particularly potent venoms that are harmful to humans (1)(2)(3)(4)(5)(6)8). Knowing the biodistribution of their venom is helpful for development of potent antivenoms for clinical use.…”

Section: Introductionmentioning

confidence: 99%

Comparison of two purified toxic fractions from Mesobuthus eupeus scorpion venom

Shirmardi¹,

Shamsaei²,

Ghanei³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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show abstract

“…14) In the present study, another toxic fraction VIII, was further separated by RP-HPLC (Fig. 1A), and the resulting five fractions, A-E, were examined for their toxicity toward insects by injecting into crickets (A. domestica, 50 AE 5 mg body weight).…”

mentioning

confidence: 99%

Purification and cDNA Cloning of LaIT2, a Novel Insecticidal Toxin from Venom of the ScorpionLiocheles australasiae

Matsushita¹,

Miyashita²,

Ichiki³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…e scorpion toxin LaIT1 was used as a model peptides, which contains several Lys residues. 12) A er reduction and alkylation of cysteine residues, LaIT1 were digested with endoproteinase Lys-C, and resultant peptides were subjected to the modi cation. As shown in Table 2, conversion rates were satisfactory for all peptides (78-93%).…”

Section: Resultsmentioning

confidence: 99%

A Facile Method for Preferential Modification of the N-Terminal Amino Group of Peptides Using Triazine-Based Coupling Reagents

et al. 2017

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Purification and characterization of a novel short-chain insecticidal toxin with two disulfide bridges from the venom of the scorpion Liocheles australasiae

Cited by 32 publications

References 28 publications

Comparison of two purified toxic fractions from Mesobuthus eupeus scorpion venom

Comparison of two purified toxic fractions from Mesobuthus eupeus scorpion venom

Purification and cDNA Cloning of LaIT2, a Novel Insecticidal Toxin from Venom of the ScorpionLiocheles australasiae

A Facile Method for Preferential Modification of the N-Terminal Amino Group of Peptides Using Triazine-Based Coupling Reagents

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