OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum

Elisabeth F. Schwartz, Adam Bartok, Carlos Alberto Schwartz, Ferenc Papp, Froylan Gómez-Lagunas, G. Panyi, Lourival D. Possani

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Opisthacanthus cayaporum belongs to the Liochelidae family, and the scorpions from this genus occur in southern Africa, Central America and South America and, therefore, can be considered a true Gondwana heritage. In this communication, the isolation, primary structure characterization, and K +-channel blocking activity of new peptide from this scorpion venom are reported. OcyKTx2 is a 34 amino acid long peptide with four disulfide bridges and molecular mass of 3807 Da. Electrophysiological assays conducted with pure OcyKTx2 showed that this toxin reversibly blocks Shaker B K +-channels with a Kd of 82 nM, and presents an even better affinity toward hKv1.3, blocking it with a Kd of ∼18 nM. OcyKTx2 shares high sequence identity with peptides belonging to subfamily 6 of α-KTxs that clustered very closely in the phylogenetic tree included here. Sequence comparison, chain length and number of disulfide bridges analysis classify OcyKTx2 into subfamily 6 of the α-KTx scorpion toxins (systematic name, α-KTx6.17).

Original languageEnglish
Pages (from-to)40-46
Number of pages7
JournalPeptides
Volume46
DOIs
Publication statusPublished - 2013

Fingerprint

Scorpion Venoms
Scorpions
Disulfides
Peptides
Southern Africa
Central America
South America
Molecular mass
Chain length
Names
Assays
Amino Acids
Communication

Keywords

  • HKv1.3
  • Lymphocyte Opisthacanthus cayaporum
  • OcyKTx2
  • Scorpion toxin
  • Shaker B K-channel

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Schwartz, E. F., Bartok, A., Schwartz, C. A., Papp, F., Gómez-Lagunas, F., Panyi, G., & Possani, L. D. (2013). OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum. Peptides, 46, 40-46. https://doi.org/10.1016/j.peptides.2013.04.021

OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum. / Schwartz, Elisabeth F.; Bartok, Adam; Schwartz, Carlos Alberto; Papp, Ferenc; Gómez-Lagunas, Froylan; Panyi, G.; Possani, Lourival D.

In: Peptides, Vol. 46, 2013, p. 40-46.

Research output: Contribution to journalArticle

Schwartz, EF, Bartok, A, Schwartz, CA, Papp, F, Gómez-Lagunas, F, Panyi, G & Possani, LD 2013, 'OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum', Peptides, vol. 46, pp. 40-46. https://doi.org/10.1016/j.peptides.2013.04.021
Schwartz, Elisabeth F. ; Bartok, Adam ; Schwartz, Carlos Alberto ; Papp, Ferenc ; Gómez-Lagunas, Froylan ; Panyi, G. ; Possani, Lourival D. / OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum. In: Peptides. 2013 ; Vol. 46. pp. 40-46.
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AB - Opisthacanthus cayaporum belongs to the Liochelidae family, and the scorpions from this genus occur in southern Africa, Central America and South America and, therefore, can be considered a true Gondwana heritage. In this communication, the isolation, primary structure characterization, and K +-channel blocking activity of new peptide from this scorpion venom are reported. OcyKTx2 is a 34 amino acid long peptide with four disulfide bridges and molecular mass of 3807 Da. Electrophysiological assays conducted with pure OcyKTx2 showed that this toxin reversibly blocks Shaker B K +-channels with a Kd of 82 nM, and presents an even better affinity toward hKv1.3, blocking it with a Kd of ∼18 nM. OcyKTx2 shares high sequence identity with peptides belonging to subfamily 6 of α-KTxs that clustered very closely in the phylogenetic tree included here. Sequence comparison, chain length and number of disulfide bridges analysis classify OcyKTx2 into subfamily 6 of the α-KTx scorpion toxins (systematic name, α-KTx6.17).

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