1. Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily.
- Author
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ElFessi-Magouri R, Peigneur S, Khamessi O, Srairi-Abid N, ElAyeb M, Mille BG, Cuypers E, Tytgat J, and Kharrat R
- Subjects
- Animals, Disulfides chemistry, Male, Mice, Inbred C57BL, Molecular Weight, Oocytes drug effects, Oocytes metabolism, Patch-Clamp Techniques, Peptides genetics, Peptides isolation & purification, Potassium Channels, Voltage-Gated antagonists & inhibitors, Potassium Channels, Voltage-Gated metabolism, Scorpions chemistry, Sequence Homology, Amino Acid, Toxicity Tests methods, Xenopus laevis, Peptides chemistry, Peptides pharmacology, Scorpion Venoms chemistry
- Abstract
Kbot55 is a 39 amino acid peptide isolated from the venom of the Tunisian scorpion Buthus occitanus tunetanus. This peptide is cross-linked by 3 disulfide bridges and has a molecular mass of 4128.65Da. Kbot55 is very low represented in the venom and thus represents a challenge for biochemical characterization. In this study, Kbot55 has been subjected to a screening on ion channels expressed in Xenopus laevis oocytes. It was found that Kbot55 targets voltage-gated potassium channels with high affinity. Kbot55 shows very low amino acid identity with other scorpion potassium toxins and therefore was considered a bona fide novel type of scorpion toxin. Sequence alignment analysis indicated that Kbot55 is the first representative of the new α-Ktx31 subfamily and therefore was classified as α-Ktx31.1., (Copyright © 2015 Elsevier Inc. All rights reserved.)
- Published
- 2016
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