Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily

  • Rym ElFessi-Magouri
  • , Steve Peigneur
  • , Oussema Khamessi
  • , Najet Srairi-Abid
  • , Mohamed ElAyeb
  • , Bea Garcia Mille
  • , Eva Cuypers
  • , Jan Tytgat
  • , Riadh Kharrat*
  • *Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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.

Original languageEnglish
Pages (from-to)4-8
Number of pages5
JournalPeptides
Volume80
DOIs
Publication statusPublished - Jun 2016
Externally publishedYes

Keywords

  • Animals
  • Disulfides/chemistry
  • Male
  • Mice, Inbred C57BL
  • Molecular Weight
  • Oocytes/drug effects
  • Patch-Clamp Techniques
  • Peptides/chemistry
  • Potassium Channels, Voltage-Gated/antagonists & inhibitors
  • Scorpion Venoms/chemistry
  • Scorpions/chemistry
  • Sequence Homology, Amino Acid
  • Toxicity Tests/methods
  • Xenopus laevis

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