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Toxins 2016, 8(10), 288; doi:10.3390/toxins8100288

Structural and Functional Elucidation of Peptide Ts11 Shows Evidence of a Novel Subfamily of Scorpion Venom Toxins

1
Laboratório de Toxinas Animais, Departamento de Física e Química, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo (USP), Ribeirão Preto 14040-903, São Paulo, Brasil
2
Laboratory for Medicinal Chemistry, Rega Institute for Medical Research, University of Leuven (KU Leuven), P.O. Box 922, Leuven 3000, Belgium
3
Toxicology & Pharmacology, University of Leuven (KU Leuven), Campus Gasthuisberg O&N2, P.O. Box 922, Leuven 3000, Belgium
4
Laboratório de Venenos e Toxinas Animais, Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais (UFMG), Belo Horizonte 31270-901, Brasil
5
Laboratory of Protein Phosphorylation and Proteomics, University of Leuven (KU Leuven), P.O. Box 922, Leuven 3000, Belgium
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Eivind Undheim
Received: 26 July 2016 / Revised: 25 September 2016 / Accepted: 26 September 2016 / Published: 30 September 2016
(This article belongs to the Section Animal Venoms)
View Full-Text   |   Download PDF [3738 KB, uploaded 30 September 2016]   |  

Abstract

To date, several families of peptide toxins specifically interacting with ion channels in scorpion venom have been described. One of these families comprise peptide toxins (called KTxs), known to modulate potassium channels. Thus far, 202 KTxs have been reported, belonging to several subfamilies of KTxs (called α, β, γ, κ, δ, and λ-KTxs). Here we report on a previously described orphan toxin from Tityus serrulatus venom, named Ts11. We carried out an in-depth structure-function analysis combining 3D structure elucidation of Ts11 and electrophysiological characterization of the toxin. The Ts11 structure is highlighted by an Inhibitor Cystine Knot (ICK) type scaffold, completely devoid of the classical secondary structure elements (α-helix and/or β-strand). This has, to the best of our knowledge, never been described before for scorpion toxins and therefore represents a novel, 6th type of structural fold for these scorpion peptides. On the basis of their preferred interaction with voltage-gated K channels, as compared to all the other targets tested, it can be postulated that Ts11 is the first member of a new subfamily, designated as ε-KTx. View Full-Text
Keywords: Tityus serrulatus; scorpion toxin; Ts11; neurotoxin; NMR; protein structure; ICK fold; electrophysiology; potassium channel Tityus serrulatus; scorpion toxin; Ts11; neurotoxin; NMR; protein structure; ICK fold; electrophysiology; potassium channel
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Cremonez, C.M.; Maiti, M.; Peigneur, S.; Cassoli, J.S.; Dutra, A.A.A.; Waelkens, E.; Lescrinier, E.; Herdewijn, P.; de Lima, M.E.; Pimenta, A.M.C.; Arantes, E.C.; Tytgat, J. Structural and Functional Elucidation of Peptide Ts11 Shows Evidence of a Novel Subfamily of Scorpion Venom Toxins. Toxins 2016, 8, 288.

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