ArticleApplied microbiology and biotechnology2023
Characterization of a novel tetravalent botulism antitoxin based on receptor-binding domain of BoNTs.
Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Antibody-based alternatives to animal testing for toxin detection and antitoxin evaluation.Frontiers in toxicology · 2025Review
- Recombinant expression of receptor binding domains of all eight subtypes of botulinum neurotoxin type A for generation of antitoxins with broad reactivity.F1000Research · 2025Article
- Passive Immunisation in the Treatment of Infectious Diseases Related to Highly Potent Bacterial Toxins.Biomedicines · 2024Review
- Novel platform for engineering stable and effective vaccines against botulinum neurotoxins A, B and E.Frontiers in immunology · 2024Article
- Efficacy and Safety Analysis of Botox Application and Iatrogenic Botulism: Panacea or Peril?Current pharmaceutical design · 2024Review
- Isolation and characterization of Hc-targeting chimeric heavy chain antibodies neutralizing botulinum neurotoxin type B.Frontiers in immunology · 2024Article
- Tetanus toxin and botulinum neurotoxin-derived fusion molecules are effective bivalent vaccines.Applied microbiology and biotechnology · 2023Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Botulinum neurotoxin (BoNTs; serotypes A, B, E, and F) cause botulism disease in humans, which could be effectively treated using antitoxins. Herein, we established a novel receptor-binding domain (RBD)-based antitoxin using recombinant C terminal heavy chain (Hc) domains of BoNTs as immunogens. Immunization of horses with these recombinant Hc domains allowed the purification and digestion of IgGs from hyper-immune sera to produce high-quality and high-efficiency monovalent botulism antitoxin F(ab')
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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.