Isolation and characterization of a novel lepidopteran-selective toxin from the venom of South Indian red scorpion, Mesobuthus tamulus
| Autor: | R, Wudayagiri, B, Inceoglu, R, Herrmann, M, Derbel, P V, Choudary, B D, Hammock |
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| Jazyk: | angličtina |
| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Insecticides fungi Molecular Sequence Data lcsh:Animal biochemistry Scorpion Venoms Chromatography Ion Exchange Lepidoptera lcsh:Biochemistry Mice Animals Biological Assay lcsh:QD415-436 Amino Acid Sequence Sequence Alignment lcsh:QP501-801 Chromatography High Pressure Liquid Research Article |
| Zdroj: | BMC Biochemistry, Vol 2, Iss 1, p 16 (2001) BMC Biochemistry |
| ISSN: | 1471-2091 |
| Popis: | Background Scorpion venom contains insect and mammal selective toxins. We investigated the venom of the South Indian red scorpion, Mesobuthus tamulus for the purpose of identifying potent insecticidal peptide toxins. Results A lepidopteran-selective toxin (Buthus tamulus insect toxin; ButaIT) has been isolated from this venom. The primary structure analysis reveals that it is a single polypeptide composed of 37 amino acids cross-linked by four disulfide bridges with high sequence homology to other short toxins such as Peptide I, neurotoxin P2, Lqh-8/6, chlorotoxin, insectotoxin I5A, insect toxin 15 and insectotoxin I1. Three dimensional modeling using Swiss automated protein modeling server reveals that this toxin contains a short α-helix and three antiparallel β-strands, similar to other short scorpion toxins. This toxin is selectively active on Heliothis virescens causing flaccid paralysis but was non-toxic to blowfly larvae and mice. Conclusion This is the first report of a Heliothine selective peptide toxin. Identification of diverse insect selective toxins offer advantages in employing these peptides selectively for pest control. |
| Databáze: | OpenAIRE |
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