Title: A novel conotoxin inhibiting vertebrate voltage-sensitive potassium channels
Authors: Kauferstein, Silke ×
Huys, Isabelle
Lamthanh, Hung
Stöcklin, Reto
Sotto, Filipina
Menez, André
Tytgat, Jan
Mebs, Dietrich #
Issue Date: Jul-2003
Series Title: Toxicon vol:42 issue:1 pages:43-52
Abstract: Toxins from cone snail (Conus species) venoms are multiple disulfide bonded peptides. Based on their pharmacological target (ion channels, receptors) and their disulfide pattern, they have been classified into several toxin families and superfamilies. Here, we report a new conotoxin, which is the first member of a structurally new superfamily of Conus peptides and the first conotoxin affecting vertebrate K+ channels. The new toxin, designated conotoxin ViTx, has been isolated from the venom of Conus virgo and comprises a single chain of 35 amino acids cross-linked by four disulfide bridges. Its amino acid sequence (SRCFPPGIYCTSYLPCCWGICCSTCRNVCHLRIGK) was partially determined by Edman degradation and deduced from the nucleotide sequence of the toxin cDNA. Nucleic acid sequencing also revealed a prepropeptide comprising 67 amino acid residues and demonstrated a posttranslational modification of the protein by releasing a six-residue peptide from the C-terminal. Voltage clamp studies on various ion channels indicated that the toxin inhibits the vertebrate K+ channels Kv1.1 and Kv1.3 but not Kv1.2. The chemically synthesized product exhibited the same physiological activity and identical molecular mass (3933.7 Da) as the native toxin.
ISSN: 0041-0101
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Toxicology and Pharmacology
Research Centre for Pharmaceutical Care and Pharmaco-economics (-)
Research Unit KU Leuven Centre for IT & IP Law (CiTiP)
× corresponding author
# (joint) last author

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