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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker

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Author(s):
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Orts, Diego J. B. [1] ; Moran, Yehu [2] ; Cologna, Camila T. [3] ; Peigneur, Steve [4] ; Madio, Bruno [1] ; Praher, Daniela [2] ; Quinton, Loic [3] ; De Pauw, Edwin [3] ; Bicudo, Jose E. P. W. [1] ; Tytgat, Jan [4] ; de Freitas, Jose C. [1]
Total Authors: 11
Affiliation:
[1] Univ Sao Paulo, Inst Biosci, Dept Physiol, BR-05508 Sao Paulo - Brazil
[2] Univ Vienna, Fac Life Sci, Dept Mol Evolut & Dev, A-1010 Vienna - Austria
[3] Univ Liege, Dept Chem, Lab Mass Spectrometry, B-4000 Liege - Belgium
[4] Univ Leuven, Toxicol Lab, Louvain - Belgium
Total Affiliations: 4
Document type: Journal article
Source: FEBS Journal; v. 280, n. 19, p. 4839-4852, OCT 2013.
Web of Science Citations: 15
Abstract

Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a Bunodosomacaissarum (population captured at the Saint Peter and Saint Paul Archipelago, Brazil) was purified and biochemically and pharmacologically characterized. The pharmacological effects were studied on 12 different subtypes of voltage-gated potassium channels (K(V)1.1-K(V)1.6; K(V)2.1; K(V)3.1; K(V)4.2; K(V)4.3; hERG and Shaker IR) and three cloned voltage-gated sodium channel isoforms (Na(V)1.2, Na(V)1.4 and BgNa(V)1.1) expressed in Xenopuslaevis oocytes. BcsTx3 shows a high affinity for Drosophila Shaker IR channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on Na-V channels. Biochemical characterization reveals that BcsTx3 is a 50 amino acid peptide crosslinked by four disulfide bridges, and sequence comparison allowed BcsTx3 to be classified as a novel type of sea anemone toxin acting on K-V channels. Moreover, putative toxins homologous to BcsTx3 from two additional actiniarian species suggest an ancient origin of this newly discovered toxin family. (AU)

FAPESP's process: 11/21031-6 - Analysis of the mechanism of action involved in the selective activity of Abe III 1.3 in voltage-dependent K+ channels
Grantee:Diego Jose Orts y Belato
Support Opportunities: Scholarships abroad - Research Internship - Master's degree
FAPESP's process: 09/07128-7 - Sea anemones neurotoxins as tools to study the physiology of voltage-gated potassium channels
Grantee:Diego Jose Orts y Belato
Support Opportunities: Scholarships in Brazil - Master