Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K+-channels with distinctly different affinities

Cesar V F Batista, Froylan Gómez-Lagunas, Ricardo C. Rodríguez De La Vega, Péter Hajdu, G. Panyi, R. Gáspár, Lourival D. Possani

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Two novel toxic peptides (Tc30 and Tc32) were isolated and characterized from the venom of the Brazilian scorpion Tityus cambridgei. The first have 37 and the second 35 amino acid residues, with molecular masses of 3871.8 and 3521.5, respectively. Both contain three disulfide bridges but share only 27% identity. They are relatively potent inhibitors of K+-currents in human T lymphocytes with Kd values of 10 nM for Tc32 and 16 nM for Tc30, but they are less potent or quite poor blockers of Shaker B K +-channels, with respective Kd values of 74 nM and 4.7 μM. Tc30 has a lysine in position 27 and a tyrosine at position 36 identical to those of charybdotoxin. These two positions conform the dyad considered essential for activity. On the contrary, Tc32 has a serine in the position equivalent to lysine 27 of charybdotoxin and does not contain any aromatic amino acid. Due to its unique primary sequence and to its distinctive preference for K+-channels of T lymphocytes, it was classified as the first example of a new subfamily of K+-channel-specific peptides (α-KTx18.1). Tc30 is a member of the Tityus toxin II-9 subfamily and was given the number α-KTx4.4.

Original languageEnglish
Pages (from-to)123-131
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1601
Issue number2
DOIs
Publication statusPublished - Dec 16 2002

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Charybdotoxin
Scorpions
T-cells
Lysine
Scorpion Venoms
T-Lymphocytes
Aromatic Amino Acids
Peptides
Poisons
Molecular mass
Disulfides
Serine
Tyrosine
Amino Acids

Keywords

  • K-channel
  • Kv1.3
  • Nomenclature
  • Scorpion toxin
  • Shaker B
  • T lymphocyte

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics

Cite this

Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K+-channels with distinctly different affinities. / Batista, Cesar V F; Gómez-Lagunas, Froylan; Rodríguez De La Vega, Ricardo C.; Hajdu, Péter; Panyi, G.; Gáspár, R.; Possani, Lourival D.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1601, No. 2, 16.12.2002, p. 123-131.

Research output: Contribution to journalArticle

Batista, Cesar V F ; Gómez-Lagunas, Froylan ; Rodríguez De La Vega, Ricardo C. ; Hajdu, Péter ; Panyi, G. ; Gáspár, R. ; Possani, Lourival D. / Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K+-channels with distinctly different affinities. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2002 ; Vol. 1601, No. 2. pp. 123-131.
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AU - Rodríguez De La Vega, Ricardo C.

AU - Hajdu, Péter

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AU - Possani, Lourival D.

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AB - Two novel toxic peptides (Tc30 and Tc32) were isolated and characterized from the venom of the Brazilian scorpion Tityus cambridgei. The first have 37 and the second 35 amino acid residues, with molecular masses of 3871.8 and 3521.5, respectively. Both contain three disulfide bridges but share only 27% identity. They are relatively potent inhibitors of K+-currents in human T lymphocytes with Kd values of 10 nM for Tc32 and 16 nM for Tc30, but they are less potent or quite poor blockers of Shaker B K +-channels, with respective Kd values of 74 nM and 4.7 μM. Tc30 has a lysine in position 27 and a tyrosine at position 36 identical to those of charybdotoxin. These two positions conform the dyad considered essential for activity. On the contrary, Tc32 has a serine in the position equivalent to lysine 27 of charybdotoxin and does not contain any aromatic amino acid. Due to its unique primary sequence and to its distinctive preference for K+-channels of T lymphocytes, it was classified as the first example of a new subfamily of K+-channel-specific peptides (α-KTx18.1). Tc30 is a member of the Tityus toxin II-9 subfamily and was given the number α-KTx4.4.

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