ArticleToxins2015
Revealing the Function and the Structural Model of Ts4: Insights into the "Non-Toxic" Toxin from Tityus serrulatus Venom.
Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- Venom-loaded cationic-functionalized poly(lactic acid) nanoparticles for serum production againstBeilstein journal of nanotechnology · 2025Article
- The nociceptive response induced by different classes of Tityus serrulatus neurotoxins: The important role of Ts5 in venom-induced nociception.PLoS neglected tropical diseases · 2023Article
- Reduced Toxicity ofToxins · 2021Article
- Pioneering Study onFrontiers in immunology · 2020Article
- Subtype Specificity of β-Toxin Tf1a fromToxins · 2018Article
- Effects of Brazilian scorpion venoms on the central nervous system.The journal of venomous animals and toxins including tropical diseases · 2018Review
- Tityus serrulatus Scorpion Venom: In Vitro Tests and Their Correlation with In Vivo Lethal Dose Assay.Toxins · 2017Article
- Electrophysiological Characterization of the Antarease Metalloprotease from Tityus serrulatus Venom.Toxins · 2017Article
- Immunosuppressive evidence of Tityus serrulatus toxins Ts6 and Ts15: insights of a novel K(+) channel pattern in T cells.Immunology · 2016Article
- Tityus serrulatus envenoming in non-obese diabetic mice: a risk factor for severity.The journal of venomous animals and toxins including tropical diseases · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The toxin, previously described as a "non-toxic" toxin, was isolated from the scorpion venom of Tityus serrulatus (Ts), responsible for the most severe and the highest number of accidents in Brazil. In this study, the subtype specificity and selectivity of Ts4 was investigated using six mammalian Nav channels (Nav1.2→Nav1.6 and Nav1.8) and two insect Nav channels (DmNav1 and BgNav). The electrophysiological assays showed that Ts4 specifically inhibited the fast inactivation of Nav1.6 channels, the most abundant sodium channel expressed in the adult central nervous system, and can no longer be classified as a "non-toxic peptide". Based on the results, we could classify the Ts4 as a classical α-toxin. The Ts4 3D-structural model was built based on the solved X-ray Ts1 3D-structure, the major toxin from Ts venom with which it shares high sequence identity (65.57%). The Ts4 model revealed a flattened triangular shape constituted by three-stranded antiparallel β-sheet and one α-helix stabilized by four disulfide bonds. The absence of a Lys in the first amino acid residue of the N-terminal of Ts4 is probably the main responsible for its low toxicity. Other key amino acid residues important to the toxicity of α- and β-toxins are discussed here.
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