ArticleNature communications2019
Horse immunization with short-chain consensus α-neurotoxin generates antibodies against broad spectrum of elapid venomous species.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 67 citations in OpenAlex.
- Engineering Antivenom: Research Progress and Future Directions in Snakebite Envenoming Therapy.Annals of the New York Academy of Sciences · 2026Review
- Immunogenicity of two representative American consensus scorpion neurotoxins from the genera Tityus and Centruroides.PLoS neglected tropical diseases · 2026Article
- Discovery of broadly neutralizing VmAbs · 2025Article
- Structural mechanisms behind the neutralisation of long-chain α-neurotoxins by broadly neutralising VCommunications chemistry · 2025Article
- First Look at the Venoms of TwoToxins · 2025Article
- Evaluation of cellular immune response in rabbits after exposure to cobra venom and purified toxin fraction.Environmental analysis, health and toxicology · 2024Article
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- Discovery of broadly-neutralizing antibodies against brown recluse spider and Gadim scorpion sphingomyelinases using consensus toxins as antigens.Protein science : a publication of the Protein Society · 2024Article
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- An in vitro assay to investigate venom neurotoxin activity on muscle-type nicotinic acetylcholine receptor activation and for the discovery of toxin-inhibitory molecules.Biochemical pharmacology · 2023Article
- Towards better antivenoms: navigating the road to new types of snakebite envenoming therapies.The journal of venomous animals and toxins including tropical diseases · 2023Article
- The molecular mechanism of snake short-chain α-neurotoxin binding to muscle-type nicotinic acetylcholine receptors.Nature communications · 2022Article
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- Review
- Article
- Synthetic antibodies block receptor binding and current-inhibiting effects of α-cobratoxin from Naja kaouthia.Protein science : a publication of the Protein Society · 2022Article
- Heterologous expression of four recombinant toxins from Panamanian scorpions of the genusToxicon: X · 2022Article
- Terrestrial venomous animals, the envenomings they cause, and treatment perspectives in the Middle East and North Africa.PLoS neglected tropical diseases · 2021Review
- Promoting co-existence between humans and venomous snakes through increasing the herpetological knowledge base.Toxicon: X · 2021Article
- Clinical management of snakebite envenoming: Future perspectives.Toxicon: X · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antivenoms are fundamental in the therapy for snakebites. In elapid venoms, there are toxins, e.g. short-chain α-neurotoxins, which are quite abundant, highly toxic, and consequently play a major role in envenomation processes. The core problem is that such α-neurotoxins are weakly immunogenic, and many current elapid antivenoms show low reactivity towards them. We have previously developed a recombinant consensus short-chain α-neurotoxin (ScNtx) based on sequences from the most lethal elapid venoms from America, Africa, Asia, and Oceania. Here we report that an antivenom generated by immunizing horses with ScNtx can successfully neutralize the lethality of pure recombinant and native short-chain α-neurotoxins, as well as whole neurotoxic elapid venoms from diverse genera such as Micrurus, Dendroaspis, Naja, Walterinnesia, Ophiophagus and Hydrophis. These results provide a proof-of-principle for using recombinant proteins with rationally designed consensus sequences as universal immunogens for developing next-generation antivenoms with higher effectiveness and broader neutralizing capacity.
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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.