ArticleThe Journal of biological chemistry2010
Novel class of spider toxin: active principle from the yellow sac spider Cheiracanthium punctorium venom is a unique two-domain polypeptide.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Ancient origin and dynamic evolution of bivalent spider toxins.Molecular biology and evolution · 2026Article
- Web of Potentials: Neuroactive Components of Spider Venom and Their Emerging Pharmacologic Applications in Neurologic Diseases.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Comparative venomics suggests an evolutionary adaption of spider venom from predation to defense.Communications biology · 2025Article
- Exploring the SARS-CoV-2 spike protein destabilizer toxin from the scorpion, spider, and wasp group of toxins as a promising candidate for the identification of pharmacophores against viral infections.Open veterinary journal · 2025Article
- Spider-Venom Peptides: Structure, Bioactivity, Strategy, and Research Applications.Molecules (Basel, Switzerland) · 2023Review
- A bivalent remipede toxin promotes calcium release via ryanodine receptor activation.Nature communications · 2023Article
- Evaluation of Efficient Non-reducing Enzymatic and Chemical Ligation Strategies for Complex Disulfide-Rich Peptides.Bioconjugate chemistry · 2021Article
- Enzymatic Ligation of Disulfide-Rich Animal Venom Peptides: Using Sortase A to Form Double-Knotted Peptides.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Article
- Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses.Toxins · 2019Review
- Article
- Can we resolve the taxonomic bias in spider venom research?Toxicon: X · 2019Article
- Secreted Cysteine-Rich Repeat Proteins "SCREPs": A Novel Multi-Domain Architecture.Frontiers in pharmacology · 2018Article
- Yellow sac spider (Cheiracanthium punctorium) bites in Slovenia: case series and review.Wiener klinische Wochenschrift · 2017Review
- Venomics of Remipede Crustaceans Reveals Novel Peptide Diversity and Illuminates the Venom's Biological Role.Toxins · 2017Article
- Modular toxin from the lynx spider Oxyopes takobius: Structure of spiderine domains in solution and membrane-mimicking environment.Protein science : a publication of the Protein Society · 2017Article
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- Dramatic expansion of the black widow toxin arsenal uncovered by multi-tissue transcriptomics and venom proteomics.BMC genomics · 2014Article
- Article
- Receptor-targeting mechanisms of pain-causing toxins: How ow?Toxicon : official journal of the International Society on Toxinology · 2012Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Venom of the yellow sac spider Cheiracanthium punctorium (Miturgidae) was found unique in terms of molecular composition. Its principal toxic component CpTx 1 (15.1 kDa) was purified, and its full amino acid sequence (134 residues) was established by protein chemistry and mass spectrometry techniques. CpTx 1 represents a novel class of spider toxin with modular architecture. It consists of two different yet homologous domains (modules) each containing a putative inhibitor cystine knot motif, characteristic of the widespread single domain spider neurotoxins. Venom gland cDNA sequencing provided precursor protein (prepropeptide) structures of three CpTx 1 isoforms (a-c) that differ by single residue substitutions. The toxin possesses potent insecticidal (paralytic and lethal), cytotoxic, and membrane-damaging activities. In both fly and frog neuromuscular preparations, it causes stable and irreversible depolarization of muscle fibers leading to contracture. This effect appears to be receptor-independent and is inhibited by high concentrations of divalent cations. CpTx 1 lyses cell membranes, as visualized by confocal microscopy, and destabilizes artificial membranes in a manner reminiscent of other membrane-active peptides by causing numerous defects of variable conductance and leading to bilayer rupture. The newly discovered class of modular polypeptides enhances our knowledge of the toxin universe.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.