Isolation and characterization of Ts19 Fragment II, a new long-chain potassium channel toxin from Tityus serrulatus venom

Cerni, Felipe Augusto; Pucca, Manuela Berto; Amorim, Fernanda Gobbi; Bordon, Karla de Castro Figueiredo; Echterbille, Julien; Quinton, Loïc; Pauw, Edwin De; Peigneur, Steve; Tytgat, Jan; Arantes, Eliane Candiani

doi:10.1016/j.peptides.2015.06.004

Cited by 27 publications

(25 citation statements)

References 43 publications

(68 reference statements)

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“…This new 49 amino acid long peptide had three disulphide bridges, a measured monoisotopic mass of 5534.54 Da to be compared to the theoretical one 5518.55 Da. This 16 Da difference could be due to an oxidation event (Cerni et al, 2015). It was classified, as the previously described Ts19 (Alvarenga et al, 2012), in the subfamily class 2 of the beta-KTxs.…”

Section: Ts8 Previously Tstx Kbeta and Its Ortholog Ts19mentioning

confidence: 79%

“…Now both toxins Ts6 and BuTX are considered as the same toxin. However, they were still classified as α-KTx12.1 (TsTX-IV vs Ts6) and α-KTx12.2 (BuTX), since they derived from Tityus species from different geographic regions (Cerni et al, 2015). In fact, the C-terminal Asn 41 described in TsTX-IV and missing in Butantoxin is probably resulting of a wrong mass determination.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…The amino acid residues in blue correspond to the oligopeptidase inhibitor (Carvalho et al, 2013); those in red to the Ts19 Frag-II with cytolytic activity and the rest of the molecule to Ts19 Fragment III, a K v 1.2specific blocker (Cerni et al, 2015).…”

Section: Fig 6tstx Kbeta (Ts8) and Its Ortholog Ts19mentioning

confidence: 99%

“…ACCEPTED MANUSCRIPTRogowski et al, 1994;Legros et al, 1998 Unpublished resultsAlvarenga et al, 2012Cerni et al, 2015 Table 1: Toxins from Tityus serrulatus venom targeting K + channel…”

mentioning

confidence: 99%

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Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Martin‐Eauclaire

Pimenta

Bougis

et al. 2016

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Section: Ts8 Previously Tstx Kbeta and Its Ortholog Ts19mentioning

confidence: 79%

Section: Accepted Manuscriptmentioning

confidence: 99%

Section: Fig 6tstx Kbeta (Ts8) and Its Ortholog Ts19mentioning

confidence: 99%

“…ACCEPTED MANUSCRIPTRogowski et al, 1994;Legros et al, 1998 Unpublished resultsAlvarenga et al, 2012Cerni et al, 2015 Table 1: Toxins from Tityus serrulatus venom targeting K + channel…”

mentioning

confidence: 99%

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Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Martin‐Eauclaire

Pimenta

Bougis

et al. 2016

Toxicon

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“…2), such as NaTxs (in red and orange) and KTxs (in violet and pink). An outstanding observation is that Ts10 shares 92.3 % of identity with Ts5 and Ts17, α-NaTxs; ---5971 P86822 7354 P86822 6458 (Carmanhan et al, 2013) P86822 5519 (Cerni et al, 2013) ---6700-6800 4 P86824 --- ---4489 4,5 (Ferreira et al, 1998) Ts18 α-NaTx (Fletcher et al, 2010) Other components ------ ---7549 4 (Sampaio et al, 1983) P84686 --- --- (Richardson et al, 2008a) JK732086 5842 Estimated by SDS-PAGE -, no data …, the primary sequence was not completely determined * Reported by Cys residues are in blue. The β-KTxs (in pink in Fig.…”

Section: Composition Of the Venommentioning

confidence: 99%

Scorpion Venoms

2015

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In recent years, the field of toxinology has expanded substantially. On the one hand it studies venomous animals, plants and micro organisms in detail to understand their mode of action on targets. While on the other, it explores the biochemical composition, genomics and proteomics of toxins and venoms to understand their three interaction with life forms (especially humans), development of antidotes and exploring their pharmacological potential. Therefore, toxinology has deep linkages with biochemistry, molecular biology, anatomy and pharmacology. In addition, there is a fast-developing applied subfield, clinical toxinology, which deals with understanding and managing medical effects of toxins on human body. Given the huge impact of toxin-based deaths globally, and the potential of venom in generation of drugs for so-far incurable diseases (for example, diabetes, chronic pain), the continued research and growth of the field is imminent. This has led to the growth of research in the area and the consequent scholarly output by way of publications in journals and books. Despite this ever-growing body of literature within biomedical sciences, there is still no all-inclusive reference work available that collects all of the important biochemical, biomedical and clinical insights relating to toxinology. Composed of 11 volumes, Toxinology provides comprehensive and authoritative coverage of the main areas in toxinology, from fundamental concepts to new developments and applications in the field. Each volume comprises a focused and carefully chosen collection of contributions from leading names in the subject.

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Solution structure and antiparasitic activity of scorpine‐like peptides from Hoffmannihadrurus gertschi

et al. 2016

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Edited by Maurice MontalScorpine-like peptides are two domain peptides found in different scorpion venoms displaying various antimicrobial, cytolytic, and potassium channelblocking activities. The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine-like peptide from the venom of Hoffmannihadrurus gertschi. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel-blocking and antiparasitic activities. Our results are important to rationalize the structure-function relationships of a pharmacologically versatile molecular scaffold.

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Isolation and characterization of Ts19 Fragment II, a new long-chain potassium channel toxin from Tityus serrulatus venom

Cited by 27 publications

References 43 publications

Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Scorpion Venoms

Solution structure and antiparasitic activity of scorpine‐like peptides from Hoffmannihadrurus gertschi

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