ArticleThe Biochemical journal2007
Molecular analysis of the sea anemone toxin Av3 reveals selectivity to insects and demonstrates the heterogeneity of receptor site-3 on voltage-gated Na+ channels.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 56 citations in OpenAlex.
- Cnidarian Venoms in the Omics Era: Toxin Discovery and Bioactive Potential.Marine drugs · 2026Review
- Structural insights into insect-selective sodium channel toxins drive AI-enhanced biopesticide design.Nature communications · 2026Article
- Anthozoan Chemical Defenses: Integrating Compounds, Enzymatic Activities, and Omics-Based Discoveries.International journal of molecular sciences · 2025Review
- Review
- Voltage-Gated Sodium Channels: A Prominent Target of Marine Toxins.Marine drugs · 2021Review
- Charge substitutions at the voltage-sensing module of domain III enhance actions of site-3 and site-4 toxins on an insect sodium channel.Insect biochemistry and molecular biology · 2021Article
- Interactions of Sea Anemone Toxins with Insect Sodium Channel-Insights from Electrophysiology and Molecular Docking Studies.Molecules (Basel, Switzerland) · 2021Article
- Article
- Sea Anemone Toxins: A Structural Overview.Marine drugs · 2019Review
- The Anemonia viridis Venom: Coupling Biochemical Purification and RNA-Seq for Translational Research.Marine drugs · 2018Review
- Ancient Venom Systems: A Review on Cnidaria Toxins.Toxins · 2015Review
- Molecular biology of insect sodium channels and pyrethroid resistance.Insect biochemistry and molecular biology · 2014Article
- Sequence variations at I260 and A1731 contribute to persistent currents in Drosophila sodium channels.Neuroscience · 2014Article
- Improved insecticidal toxicity by fusing Cry1Ac of Bacillus thuringiensis with Av3 of Anemonia viridis.Current microbiology · 2014Article
- Voltage-Gated Sodium Channels as Insecticide Targets.Advances in insect physiology · 2014Article
- The insecticidal potential of venom peptides.Cellular and molecular life sciences : CMLS · 2013Review
- Expression and isotopic labelling of the potassium channel blocker ShK toxin as a thioredoxin fusion protein in bacteria.Toxicon : official journal of the International Society on Toxinology · 2012Article
- Sea anemone (Cnidaria, Anthozoa, Actiniaria) toxins: an overview.Marine drugs · 2012Review
- Neurotoxin localization to ectodermal gland cells uncovers an alternative mechanism of venom delivery in sea anemones.Proceedings. Biological sciences · 2012Article
- Elucidation of the molecular basis of selective recognition uncovers the interaction site for the core domain of scorpion alpha-toxins on sodium channels.The Journal of biological chemistry · 2011Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Av3 is a short peptide toxin from the sea anemone Anemonia viridis shown to be active on crustaceans and inactive on mammals. It inhibits inactivation of Na(v)s (voltage-gated Na+ channels) like the structurally dissimilar scorpion alpha-toxins and type I sea anemone toxins that bind to receptor site-3. To examine the potency and mode of interaction of Av3 with insect Na(v)s, we established a system for its expression, mutagenized it throughout, and analysed it in toxicity, binding and electrophysiological assays. The recombinant Av3 was found to be highly toxic to blowfly larvae (ED50=2.65+/-0.46 pmol/100 mg), to compete well with the site-3 toxin LqhalphaIT (from the scorpion Leiurus quinquestriatus) on binding to cockroach neuronal membranes (K(i)=21.4+/-7.1 nM), and to inhibit the inactivation of Drosophila melanogaster channel, DmNa(v)1, but not that of mammalian Na(v)s expressed in Xenopus oocytes. Moreover, like other site-3 toxins, the activity of Av3 was synergically enhanced by ligands of receptor site-4 (e.g. scorpion beta-toxins). The bioactive surface of Av3 was found to consist mainly of aromatic residues and did not resemble any of the bioactive surfaces of other site-3 toxins. These analyses have portrayed a toxin that might interact with receptor site-3 in a different fashion compared with other ligands of this site. This assumption was corroborated by a D1701R mutation in DmNa(v)1, which has been shown to abolish the activity of all other site-3 ligands, except Av3. All in all, the present study provides further evidence for the heterogeneity of receptor site-3, and raises Av3 as a unique model for design of selective anti-insect compounds.
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