期刊
FEBS JOURNAL
卷 280, 期 19, 页码 4839-4852出版社
WILEY
DOI: 10.1111/febs.12456
关键词
Bunodosomacaissarum; potassium channel toxin; Saint Peter and Saint Paul Archipelago; sea anemone; sequence alignment
资金
- CNPq [563874/2005-8]
- FAPESP [2009/07128-7, 2011/21031-6]
- PROAP-CAPES
- F.W.O. Vlaanderen [G.0433.12, G.A071.10N, G.0257.08]
- EU-FP7-MAREX
- IUAP [7/10]
- KU Leuven [OT/12/081]
- FNRS
- FEDER (Walloon region)
- Austrian Science Fund (FWF) [P 22618] Funding Source: researchfish
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.
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