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

Department of Chemistry, University of California, Davis, Davis, California, United States
Toxicon (Impact Factor: 2.49). 06/2005; 45(6):727-33. DOI: 10.1016/j.toxicon.2005.01.020
Source: PubMed


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 [(3)H] 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.

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    • "A subfamily of NaScTx, represented by Birtoxin, is especially interesting in this aspect. All the members in this subfamily contain only three disulfides with a slightly smaller size (about 58 residues) relative to the NaScTxs with four disulfides [15] [16] [17] [18]. They share 40–60% sequence identity to b-toxins but display more diverse pharmacological activity. "
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