Reference : BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/164149
BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker
English
Orts, Diego []
Moran, Yehu []
Cologna, Camila mailto []
Peigneur, Steeve []
Bruno, Madio []
Praher, Daniela []
Quinton, Loïc mailto [Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique >]
De Pauw, Edwin mailto [Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Bicudo, José []
Tytgat, jan []
de Freitas, José []
2013
FEBS Journal
Blackwell Publishing
280
4839-4852
Yes (verified by ORBi)
International
1742-464X
Oxford
United Kingdom
[en] venomics ; sea anemone ; potassium channel
[en] 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 Bunodosoma
caissarum (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 (KV1.1–KV1.6; KV2.1;
KV3.1; KV4.2; KV4.3; hERG and Shaker IR) and three cloned voltagegated
sodium channel isoforms (NaV1.2, NaV1.4 and BgNaV1.1) expressed
in Xenopus laevis oocytes. BcsTx3 shows a high affinity for Drosophila
Shaker IR channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on
NaV 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 KV channels. Moreover, putative toxins homologous to
BcsTx3 from two additional actiniarian species suggest an ancient origin of
this newly discovered toxin family.
Researchers ; Professionals
http://hdl.handle.net/2268/164149
10.1111/febs.12456

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