ArticleToxins2015
The Cystine Knot Is Responsible for the Exceptional Stability of the Insecticidal Spider Toxin ω-Hexatoxin-Hv1a.
Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 106 citations in OpenAlex.
- Structural basis for inhibition of the voltage-gated sodium channel NaThe Journal of biological chemistry · 2026Article
- Synthesis and preclinical evaluation of aEuropean journal of nuclear medicine and molecular imaging · 2025Article
- Ecosystem services provided by spiders.Biological reviews of the Cambridge Philosophical Society · 2025Review
- Proteolytic stabilization of a spider venom peptide results in an orally active bioinsecticide.Pest management science · 2025Article
- Spider venom potency exhibits phylogenetic prey specificity but does not trade-off with body size or silk use in prey capture.Biology letters · 2025Article
- A conservedMicrobiology (Reading, England) · 2025Article
- Enhancing Sensitivity of Nuclear Magnetic Resonance in Biomolecules: Parahydrogen-Induced Hyperpolarization in Synthetic Disulfide-Rich Miniproteins.Journal of the American Chemical Society · 2024Article
- Enlightening the toxinological dark matter of spider venom enzymes.npj biodiversity · 2024Article
- Coat protein of a whitefly-vectored plant virus as a delivery system to target whitefly.Microbial biotechnology · 2024Article
- A phage-displayed disulfide constrained peptide discovery platform yields novel human plasma protein binders.PloS one · 2024Article
- Exploring behavioral traits over different contexts in four species of Australian funnel-web spiders.Current zoology · 2023Article
- Vasodilator activity ofToxicon: X · 2023Article
- Structural Conformation and Activity of Spider-Derived Inhibitory Cystine Knot Peptide Pn3a Are Modulated by pH.ACS omega · 2023Article
- Two Novel Mosquitocidal Peptides Isolated from the Venom of the Bahia Scarlet Tarantula (Toxins · 2023Article
- A subfraction obtained from the venom of the tarantulaToxicon: X · 2023Article
- Article
- A Review on Genotoxic and Genoprotective Effects of Biologically Active Compounds of Animal Origin.Toxins · 2023Review
- Enhancing the oral and topical insecticidal efficacy of a commercialized spider venom peptide biopesticide via fusion to the carrier snowdrop lectin (Galanthus nivalis agglutinin).Pest management science · 2023Article
- Composition and toxicity of venom produced by araneophagous white-tailed spiders (Lamponidae: Lampona sp.).Scientific reports · 2022Article
- Spider Toxin SNX-482 Gating Modifier Spontaneously Partitions in the Membrane Guided by Electrostatic Interactions.Membranes · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inhibitor cystine knot (ICK) is an unusual three-disulfide architecture in which one of the disulfide bonds bisects a loop formed by the two other disulfide bridges and the intervening sections of the protein backbone. Peptides containing an ICK motif are frequently considered to have high levels of thermal, chemical and enzymatic stability due to cross-bracing provided by the disulfide bonds. Experimental studies supporting this contention are rare, in particular for spider-venom toxins, which represent the largest diversity of ICK peptides. We used ω-hexatoxin-Hv1a (Hv1a), an insecticidal toxin from the deadly Australian funnel-web spider, as a model system to examine the contribution of the cystine knot to the stability of ICK peptides. We show that Hv1a is highly stable when subjected to temperatures up to 75 °C, pH values as low as 1, and various organic solvents. Moreover, Hv1a was highly resistant to digestion by proteinase K and when incubated in insect hemolymph and human plasma. We demonstrate that the ICK motif is essential for the remarkable stability of Hv1a, with the peptide's stability being dramatically reduced when the disulfide bonds are eliminated. Thus, this study demonstrates that the ICK motif significantly enhances the chemical and thermal stability of spider-venom peptides and provides them with a high level of protease resistance. This study also provides guidance to the conditions under which Hv1a could be stored and deployed as a bioinsecticide.
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