ArticleThe Journal of general physiology2021
Evidence that toxin resistance in poison birds and frogs is not rooted in sodium channel mutations and may rely on "toxin sponge" proteins.
Article in The Journal of general physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 43 citations in OpenAlex.
- Batrachotoxin-sensitive sodium channels in toxic birds challenge "target mutation" strategy of toxin autoresistance.iScience · 2026Article
- Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.Structure (London, England : 1993) · 2026Article
- Saxiphilin functions as a toxin sponge protein that counteracts the effects of saxitoxin poisoning.Nature communications · 2026Article
- Ingestion of the potent neurotoxin epibatidine does not compromise locomotion or behavior in the poison frogbioRxiv : the preprint server for biology · 2026Article
- Development of an Automated Cell-Based Assay for the Detection of the Functional Activity of Saxitoxin.Toxins · 2026Article
- Snakes (Colubridae: Erythrolamprus) With a Complex Toxic Diet Show Convergent yet Highly Heterogeneous Voltage-gated Sodium Channel Evolution.Genome biology and evolution · 2026Article
- Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.bioRxiv : the preprint server for biology · 2026Article
- Saxiphilin functions as a 'toxin sponge' protein that counteracts the effects of saxitoxin poisoning.bioRxiv : the preprint server for biology · 2025Article
- Structural basis for saxitoxin congener binding and neutralization by anuran saxiphilins.Nature communications · 2025Article
- A draft genome assembly for the dart-poison frogGigaByte (Hong Kong, China) · 2025Article
- A review of the venom microbiome and its utility in ecology and evolution including future directions for emerging research.Symbiosis (Philadelphia, Pa.) · 2025Article
- Article
- The Amphibian Genomics Consortium: advancing genomic and genetic resources for amphibian research and conservation.BMC genomics · 2024Review
- Passive accumulation of alkaloids in inconspicuously colored frogs refines the evolutionary paradigm of acquired chemical defenses.bioRxiv : the preprint server for biology · 2024Article
- The Amphibian Genomics Consortium: advancing genomic and genetic resources for amphibian research and conservation.bioRxiv : the preprint server for biology · 2024Article
- Where Does All the Poison Go? Investigating Toxicokinetics of Newt (Taricha) Tetrodotoxin (TTX) in Garter Snakes (Thamnophis).Journal of chemical ecology · 2024Article
- Article
- Toxic to the touch: The makings of lethal mantles in pitohui birds and poison dart frogs.Molecular ecology · 2024Article
- Sodium Channel β Subunits-An Additional Element in Animal Tetrodotoxin Resistance?International journal of molecular sciences · 2024Article
- Peptide toxins that target vertebrate voltage-gated sodium channels underly the painful stings of harvester ants.The Journal of biological chemistry · 2024Article
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11 authors at 5 institutions in 1 country.
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Abstract
Many poisonous organisms carry small-molecule toxins that alter voltage-gated sodium channel (NaV) function. Among these, batrachotoxin (BTX) from Pitohui poison birds and Phyllobates poison frogs stands out because of its lethality and unusual effects on NaV function. How these toxin-bearing organisms avoid autointoxication remains poorly understood. In poison frogs, a NaV DIVS6 pore-forming helix N-to-T mutation has been proposed as the BTX resistance mechanism. Here, we show that this variant is absent from Pitohui and poison frog NaVs, incurs a strong cost compromising channel function, and fails to produce BTX-resistant channels in poison frog NaVs. We also show that captivity-raised poison frogs are resistant to two NaV-directed toxins, BTX and saxitoxin (STX), even though they bear NaVs sensitive to both. Moreover, we demonstrate that the amphibian STX "toxin sponge" protein saxiphilin is able to protect and rescue NaVs from block by STX. Taken together, our data contradict the hypothesis that BTX autoresistance is rooted in the DIVS6 N→T mutation, challenge the idea that ion channel mutations are a primary driver of toxin resistance, and suggest the possibility that toxin sequestration mechanisms may be key for protecting poisonous species from the action of small-molecule toxins.
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