ArticleThe Journal of biological chemistry2015
Neurotoxins from snake venoms and α-conotoxin ImI inhibit functionally active ionotropic γ-aminobutyric acid (GABA) receptors.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 55 citations in OpenAlex.
- Structural basis for activation and potentiation in a human α5β3 GABANature communications · 2026Article
- Estimation of genome-wide coupling in rattlesnake hybrids provides insight into the process of speciation and its progress.Nature communications · 2025Article
- The Need for and Importance of Thorough and Comprehensive Studies on the Molecular Mechanisms of Action of Animal Toxins, Venoms, and Antivenoms.International journal of molecular sciences · 2025Article
- Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions.International journal of molecular sciences · 2025Review
- Decoding the structural and functional diversity of GABAFrontiers in pharmacology · 2025Review
- Shining a Light on Venom-Peptide Receptors: Venom Peptides as Targeted Agents for In Vivo Molecular Imaging.Toxins · 2024Review
- The Cloning and Characterization of a Three-Finger Toxin Homolog (NXH8) from the CoralsnakeToxins · 2024Article
- Fifty Years of Animal Toxin Research at the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS.International journal of molecular sciences · 2023Review
- Pharmacological Screening of Venoms from Five BrazilianInternational journal of molecular sciences · 2022Article
- Sea anemone Bartholomea annulata venom inhibits voltage-gated NaScientific reports · 2022Article
- Article
- Marine Origin Ligands of Nicotinic Receptors: Low Molecular Compounds, Peptides and Proteins for Fundamental Research and Practical Applications.Biomolecules · 2022Review
- Three-Finger Toxins from Brazilian Coral Snakes: From Molecular Framework to Insights in Biological Function.Toxins · 2021Article
- Novel Three-Finger Neurotoxins fromToxins · 2021Article
- Biomedical applications of snake venom: from basic science to autoimmunity and rheumatology.Journal of translational autoimmunity · 2021Review
- Snake Toxins Labeled by Green Fluorescent Protein or Its Synthetic Chromophore are New Probes for Nicotinic acetylcholine Receptors.Frontiers in molecular biosciences · 2021Article
- Interaction of α9α10 Nicotinic Receptors With Peptides and Proteins From Animal Venoms.Frontiers in cellular neuroscience · 2021Article
- SLURP-1 Controls Growth and Migration of Lung Adenocarcinoma Cells, Forming a Complex With α7-nAChR and PDGFR/EGFR Heterodimer.Frontiers in cell and developmental biology · 2021Article
- Human Three-Finger Protein Lypd6 Is a Negative Modulator of the Cholinergic System in the Brain.Frontiers in cell and developmental biology · 2021Article
- Effects of two kinds of fishery drugs on the expressions of GAD and GABA-T mRNA in crucian carp (Carassius auratus gibelio).Fish physiology and biochemistry · 2020Article
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Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ionotropic receptors of γ-aminobutyric acid (GABAAR) regulate neuronal inhibition and are targeted by benzodiazepines and general anesthetics. We show that a fluorescent derivative of α-cobratoxin (α-Ctx), belonging to the family of three-finger toxins from snake venoms, specifically stained the α1β3γ2 receptor; and at 10 μm α-Ctx completely blocked GABA-induced currents in this receptor expressed in Xenopus oocytes (IC50 = 236 nm) and less potently inhibited α1β2γ2 ≈ α2β2γ2 > α5β2γ2 > α2β3γ2 and α1β3δ GABAARs. The α1β3γ2 receptor was also inhibited by some other three-finger toxins, long α-neurotoxin Ls III and nonconventional toxin WTX. α-Conotoxin ImI displayed inhibitory activity as well. Electrophysiology experiments showed mixed competitive and noncompetitive α-Ctx action. Fluorescent α-Ctx, however, could be displaced by muscimol indicating that most of the α-Ctx-binding sites overlap with the orthosteric sites at the β/α subunit interface. Modeling and molecular dynamic studies indicated that α-Ctx or α-bungarotoxin seem to interact with GABAAR in a way similar to their interaction with the acetylcholine-binding protein or the ligand-binding domain of nicotinic receptors. This was supported by mutagenesis studies and experiments with α-conotoxin ImI and a chimeric Naja oxiana α-neurotoxin indicating that the major role in α-Ctx binding to GABAAR is played by the tip of its central loop II accommodating under loop C of the receptors.
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