Three structurally related, highly potent, peptides from the venom of Parabuthus transvaalicus possess divergent biological activity

Bora Inceoglu, Jozsef Lango, Isaac N Pessah, Bruce D. Hammock

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The venom of South African scorpion Parabuthus transvaalicus contains a novel group of peptide toxins. These peptides resemble the long chain neurotoxins (LCN) of 60-70 residues with four disulfide bridges; however they are 58 residues long and have only three disulfide bridges constituting a new family of peptide toxins. Here we report the isolation and characterization of three new members of this mammal specific group of toxins. Dortoxin is a lethal peptide, bestoxin causes writhing in mice and altitoxin is a highly depressant peptide. Binding ability of these peptides to rat brain synaptosomes is tested. While the crude venom of P. transvaalicus enhances the binding of [ 3H] BTX to rat brain synaptosomes none of these individual toxins had a positive effect on binding. Although the primary structures of these toxins are very similar to birtoxin, their 3D models indicate significant differences. Dortoxin, bestoxin and altitoxin cumulatively constitute at least 20% of the peptide contained in the venom of P. transvaalicus and contribute very significantly to the toxicity of the venom of this medically important scorpion species. Therefore the amino acid sequences presented here can be used to make more specific and effective antivenins. Possible approaches to a systematic nomenclature of toxins are suggested.

Original languageEnglish (US)
Pages (from-to)727-733
Number of pages7
JournalToxicon
Volume45
Issue number6
DOIs
StatePublished - May 2005

Fingerprint

Venoms
Bioactivity
Peptides
Scorpions
Synaptosomes
Disulfides
Rats
Brain
Antivenins
Mammals
Neurotoxins
Terminology
Toxicity
Amino Acid Sequence
Amino Acids

Keywords

  • Birtoxin
  • Ikitoxin
  • Na channel
  • Nomenclature
  • Scorpion
  • Toxin

ASJC Scopus subject areas

  • Toxicology

Cite this

Three structurally related, highly potent, peptides from the venom of Parabuthus transvaalicus possess divergent biological activity. / Inceoglu, Bora; Lango, Jozsef; Pessah, Isaac N; Hammock, Bruce D.

In: Toxicon, Vol. 45, No. 6, 05.2005, p. 727-733.

Research output: Contribution to journalArticle

@article{15d41a6ce2634d80998a616ea5dfe7d6,
title = "Three structurally related, highly potent, peptides from the venom of Parabuthus transvaalicus possess divergent biological activity",
abstract = "The venom of South African scorpion Parabuthus transvaalicus contains a novel group of peptide toxins. These peptides resemble the long chain neurotoxins (LCN) of 60-70 residues with four disulfide bridges; however they are 58 residues long and have only three disulfide bridges constituting a new family of peptide toxins. Here we report the isolation and characterization of three new members of this mammal specific group of toxins. Dortoxin is a lethal peptide, bestoxin causes writhing in mice and altitoxin is a highly depressant peptide. Binding ability of these peptides to rat brain synaptosomes is tested. While the crude venom of P. transvaalicus enhances the binding of [ 3H] BTX to rat brain synaptosomes none of these individual toxins had a positive effect on binding. Although the primary structures of these toxins are very similar to birtoxin, their 3D models indicate significant differences. Dortoxin, bestoxin and altitoxin cumulatively constitute at least 20{\%} of the peptide contained in the venom of P. transvaalicus and contribute very significantly to the toxicity of the venom of this medically important scorpion species. Therefore the amino acid sequences presented here can be used to make more specific and effective antivenins. Possible approaches to a systematic nomenclature of toxins are suggested.",
keywords = "Birtoxin, Ikitoxin, Na channel, Nomenclature, Scorpion, Toxin",
author = "Bora Inceoglu and Jozsef Lango and Pessah, {Isaac N} and Hammock, {Bruce D.}",
year = "2005",
month = "5",
doi = "10.1016/j.toxicon.2005.01.020",
language = "English (US)",
volume = "45",
pages = "727--733",
journal = "Toxicon",
issn = "0041-0101",
publisher = "Elsevier Limited",
number = "6",

}

TY - JOUR

T1 - Three structurally related, highly potent, peptides from the venom of Parabuthus transvaalicus possess divergent biological activity

AU - Inceoglu, Bora

AU - Lango, Jozsef

AU - Pessah, Isaac N

AU - Hammock, Bruce D.

PY - 2005/5

Y1 - 2005/5

N2 - The venom of South African scorpion Parabuthus transvaalicus contains a novel group of peptide toxins. These peptides resemble the long chain neurotoxins (LCN) of 60-70 residues with four disulfide bridges; however they are 58 residues long and have only three disulfide bridges constituting a new family of peptide toxins. Here we report the isolation and characterization of three new members of this mammal specific group of toxins. Dortoxin is a lethal peptide, bestoxin causes writhing in mice and altitoxin is a highly depressant peptide. Binding ability of these peptides to rat brain synaptosomes is tested. While the crude venom of P. transvaalicus enhances the binding of [ 3H] BTX to rat brain synaptosomes none of these individual toxins had a positive effect on binding. Although the primary structures of these toxins are very similar to birtoxin, their 3D models indicate significant differences. Dortoxin, bestoxin and altitoxin cumulatively constitute at least 20% of the peptide contained in the venom of P. transvaalicus and contribute very significantly to the toxicity of the venom of this medically important scorpion species. Therefore the amino acid sequences presented here can be used to make more specific and effective antivenins. Possible approaches to a systematic nomenclature of toxins are suggested.

AB - The venom of South African scorpion Parabuthus transvaalicus contains a novel group of peptide toxins. These peptides resemble the long chain neurotoxins (LCN) of 60-70 residues with four disulfide bridges; however they are 58 residues long and have only three disulfide bridges constituting a new family of peptide toxins. Here we report the isolation and characterization of three new members of this mammal specific group of toxins. Dortoxin is a lethal peptide, bestoxin causes writhing in mice and altitoxin is a highly depressant peptide. Binding ability of these peptides to rat brain synaptosomes is tested. While the crude venom of P. transvaalicus enhances the binding of [ 3H] BTX to rat brain synaptosomes none of these individual toxins had a positive effect on binding. Although the primary structures of these toxins are very similar to birtoxin, their 3D models indicate significant differences. Dortoxin, bestoxin and altitoxin cumulatively constitute at least 20% of the peptide contained in the venom of P. transvaalicus and contribute very significantly to the toxicity of the venom of this medically important scorpion species. Therefore the amino acid sequences presented here can be used to make more specific and effective antivenins. Possible approaches to a systematic nomenclature of toxins are suggested.

KW - Birtoxin

KW - Ikitoxin

KW - Na channel

KW - Nomenclature

KW - Scorpion

KW - Toxin

UR - http://www.scopus.com/inward/record.url?scp=15944429389&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=15944429389&partnerID=8YFLogxK

U2 - 10.1016/j.toxicon.2005.01.020

DO - 10.1016/j.toxicon.2005.01.020

M3 - Article

C2 - 15804521

AN - SCOPUS:15944429389

VL - 45

SP - 727

EP - 733

JO - Toxicon

JF - Toxicon

SN - 0041-0101

IS - 6

ER -