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View Proteins belonging to: The Sea Anemone K+ Channel Blocker Toxin, BcsTx3 (BcsTx3) Family

8.B.19 The Sea Anemone K+ Channel Blocker Toxin, BcsTx3 (BcsTx3) Family

Sea anemone venoms are a rich source of peptide toxins which provide tools for studying the structures and functions of ion channels.  BcsTx3, a toxin found in the venom of a Bunodosoma caissarum (from Brazil) has been purified and biochemically and pharmacologically characterized (Orts et al. 2013). 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), all expressed in Xenopus laevis oocytes. BcsTx3 showed a high affinity for Drosophila Shaker IR channels over rKv1.2, hKv1.3 and rKv1.6, and was not active on NaV channels. Biochemical characterization revealed 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. Putative toxins homologous to BcsTx3 from two additional actiniarian species were identified (Orts et al. 2013). 

These sea anemone toxins (subfamily 1) are clearly related to spider toxins (subfamily 2), and families 8.B.6 and 8.B.19 seem to be related to each other as well as possibly to 1.C.52, 8.B.3 and 8.B.5.  These tentative possibilities need to be confirmed.  However 8.B.3 and 8.B.5 are for sure related.

This family belongs to the: Huwentoxin Superfamily.
View Proteins belonging to: The Sea Anemone K+ Channel Blocker Toxin, BcsTx3 (BcsTx3) Family

References associated with 8.B.19 family:

Agwa, A.J., L.V. Blomster, D.J. Craik, G.F. King, and C.I. Schroeder. (2018). Efficient Enzymatic Ligation of Inhibitor Cystine Knot Spider Venom Peptides: Using Sortase A To Form Double-Knottins That Probe Voltage-Gated Sodium Channel Na1.7. Bioconjug Chem. [Epub: Ahead of Print] 30148615
Cassola, A.C., H. Jaffe, H.M. Fales, S.C. Afeche, F. Magnoli, and J. Cipolla-Neto. (1998). ω-Phonetoxin-IIA: a calcium channel blocker from the spider Phoneutria nigriventer. Pflugers Arch 436: 545-552. 9683727
Clémençon, B., L. Kuhn-Nentwig, N. Langenegger, L. Kopp, S. Peigneur, J. Tytgat, W. Nentwig, and B.P. Lüscher. (2020). Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider to Potentiate Toxicity on Insects. Toxins (Basel) 12:. 32290562
Kubista, H., R.A. Mafra, Y. Chong, G.M. Nicholson, P.S. Beirão, J.S. Cruz, S. Boehm, W. Nentwig, and L. Kuhn-Nentwig. (2007). CSTX-1, a toxin from the venom of the hunting spider Cupiennius salei, is a selective blocker of L-type calcium channels in mammalian neurons. Neuropharmacology 52: 1650-1662. 17517422
Kuhn-Nentwig, L., I.M. Fedorova, B.P. Lüscher, L.S. Kopp, C. Trachsel, J. Schaller, X.L. Vu, T. Seebeck, K. Streitberger, W. Nentwig, E. Sigel, and L.G. Magazanik. (2012). A venom-derived neurotoxin, CsTx-1, from the spider Cupiennius salei exhibits cytolytic activities. J. Biol. Chem. 287: 25640-25649. 22613721
Orts, D.J., Y. Moran, C.T. Cologna, S. Peigneur, B. Madio, D. Praher, L. Quinton, E. De Pauw, J.E. Bicudo, J. Tytgat, and J.C. de Freitas. (2013). BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker. FEBS J. 280: 4839-4852. 23895459
Pinheiro, A.C., A.J. da Silva, M.A. Prado, M.d.o.N. Cordeiro, M. Richardson, M.C. Batista, C.J. de Castro Junior, A.R. Massensini, C. Guatimosim, M.A. Romano-Silva, C. Kushmerick, and M.V. Gomez. (2009). Phoneutria spider toxins block ischemia-induced glutamate release, neuronal death, and loss of neurotransmission in hippocampus. Hippocampus 19: 1123-1129. 19370546
Reis, H.J., M.A. Prado, E. Kalapothakis, M.N. Cordeiro, C.R. Diniz, L.A. De Marco, M.V. Gomez, and M.A. Romano-Silva. (1999). Inhibition of glutamate uptake by a polypeptide toxin (phoneutriatoxin 3-4) from the spider Phoneutria nigriventer. Biochem. J. 343Pt2: 413-418. 10510308
Sachkova, M.Y., A.A. Slavokhotova, E.V. Grishin, and A.A. Vassilevski. (2014). Structure of the yellow sac spider Cheiracanthium punctorium genes provides clues to evolution of insecticidal two-domain knottin toxins. Insect Mol Biol 23: 527-538. 24717175
Schalle, J., U. Kämpfer, S. Schürch, L. Kuhn-Nentwig, S. Haeberli, and W. Nentwig. (2001). CSTX-9, a toxic peptide from the spider Cupiennius salei: amino acid sequence, disulphide bridge pattern and comparison with other spider toxins containing the cystine knot structure. Cell Mol Life Sci 58: 1538-1545. 11693532
Vassilevski, A.A., I.M. Fedorova, E.E. Maleeva, Y.V. Korolkova, S.S. Efimova, O.V. Samsonova, L.V. Schagina, A.V. Feofanov, L.G. Magazanik, and E.V. Grishin. (2010). Novel class of spider toxin: active principle from the yellow sac spider Cheiracanthium punctorium venom is a unique two-domain polypeptide. J. Biol. Chem. 285: 32293-32302. 20657014
Wullschleger, B., W. Nentwig, and L. Kuhn-Nentwig. (2005). Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei. J Exp Biol 208: 2115-2121. 15914655