Novel potassium channel blocker venom peptides from Mesobuthus gibbosus (Scorpiones: Buthidae)


Diego-Garcia E., Peigneur S., Debaveye S., Gheldof E., Tytgat J., ÇALIŞKAN F.

TOXICON, cilt.61, ss.72-82, 2013 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 61
  • Basım Tarihi: 2013
  • Doi Numarası: 10.1016/j.toxicon.2012.10.010
  • Dergi Adı: TOXICON
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.72-82
  • Eskişehir Osmangazi Üniversitesi Adresli: Evet

Özet

In the present study, we report for the first time, the molecular, biochemical and electrophysiological characterization of the components present in the soluble venom from Mesobuthus gibbosus (Brulle, 1832). According to the epidemiological and clinical situation of scorpion envenomation cases M. gibbosus scorpion is one of the most important health-threatening species of Turkey. Despite the medical importance reported for M. gibbosus, there is no additional information on toxin peptides and venom components to clarify the toxic effect of the M. gibbosus sting. Biochemical characterization of the venom was performed using different protocols and techniques following a bioassay-guided strategy (HPLC, mass spectrometry and Edman degradation sequencing). Venom fractions were tested in electrophysiological assays on a panel of six K+ channels (K(v)1.1-1.6) by using the two-electrode voltage clamp technique. Three new alpha-KTx peptides were found and called MegKTx1, MegKTx2 and MegKTx3 (M. gibbosus, K+ channel toxin number 1-3). A cDNA library from the telson was constructed and specific screening of transcripts was performed. Biochemical and molecular characterization of MegKTx peptides and transcripts shows a relation with toxins of three different alpha-KTx subfamilies (alpha-KTx3.x, alpha-KTx9.x and alpha-KTx16.x). (C) 2012 Elsevier Ltd. All rights reserved.