ArticleMolecular biotechnology2013
In vivo neutralization of botulinum neurotoxins serotype E with heavy-chain camelid antibodies (VHH).
Article in Molecular biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 2 of them syntheses that pooled it.
What it found
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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
27 citing papers in PubMed, 2 syntheses or guidelines pooled it, 49 citations in OpenAlex.
- Outlook of therapeutic and diagnostic competency of nanobodies against SARS-CoV-2: A systematic review.Analytical biochemistry · 2022Pooled it
- Nanobodies, the potent agents to detect and treat the Coronavirus infections: A systematic review.Molecular and cellular probes · 2021Pooled it
- Development of Effective Medical Countermeasures Against the Main Biowarfare Agents: The Importance of Antibodies.Microorganisms · 2024Review
- A human bispecific antibody neutralizes botulinum neurotoxin serotype A.Scientific reports · 2023Article
- Review
- Nanobodies; new molecular instruments with special specifications for targeting, diagnosis and treatment of triple-negative breast cancer.Cancer cell international · 2022Review
- Functional EL-HN Fragment as a Potent Candidate Vaccine for the Prevention of Botulinum Neurotoxin Serotype E.Toxins · 2022Article
- Single Domain Antibody application in bacterial infection diagnosis and neutralization.Frontiers in immunology · 2022Review
- Nanobodies: a tool to open new horizons in diagnosis and treatment of prostate cancer.Cancer cell international · 2021Review
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- Emerging Technologies for the Treatment of COVID-19.Advances in experimental medicine and biology · 2021Article
- Camelid VHH Antibodies that Neutralize Botulinum Neurotoxin Serotype E Intoxication or Protease Function.Toxins · 2020Article
- Antibodies and Vaccines against Botulinum Toxins: Available Measures and Novel Approaches.Toxins · 2019Review
- Development and Characterization of Monoclonal Antibodies to Botulinum Neurotoxin Type E.Toxins · 2019Article
- A Two-Step Approach for the Design and Generation of Nanobodies.International journal of molecular sciences · 2018Article
- A Three Monoclonal Antibody Combination Potently Neutralizes Multiple Botulinum Neurotoxin Serotype E Subtypes.Toxins · 2018Article
- The European AntibotABE Framework Program and Its Update: Development of Innovative Botulinum Antibodies.Toxins · 2017Review
- Targeting Colorectal Cancer Cell Lines Using Nanobodies; AgSK1as a Potential Target.Iranian journal of biotechnology · 2017Article
- Monoclonal Antibodies and Antibody Like Fragments Derived from Immunised Phage Display Libraries.Advances in experimental medicine and biology · 2017Review
- Recombinant antibodies for diagnostics and therapy against pathogens and toxins generated by phage display.Proteomics. Clinical applications · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ingestion of botulinum neurotoxin (BoNT) results in botulism, a severe and frequent fatal disease known in the world. Current treatments rely on antitoxins, such as equine antitoxin and human botulism immunoglobulin. In some cases, side effects have been reported, including early anaphylactic shock and late serum sickness. Thus, diagnosis and treatment measure of BoNT are necessary and crucial. In the present study, a single-domain variable heavy-chain (VHH) antibody fragment was obtained from an immune dromedary phage display library against the putative binding domain of botulinum neurotoxin E (BoNT/E), a non-toxic 50-kDa fragment. The characteristics of nanobody VHH include excellent production, superior heat stability and specific binding capacity to soluble antigen without cross-reaction to other relevant or irrelevant antigens. A total of 150 ng/Kg of nanobody entirely neutralized 3LD50 of the BoNT/E in an in vivo challenge of the mice. This phenomenon indicates BoNT/E toxin neutralizing capacity of the produced nanobody. These results also suggest possession of unique properties by the nanobody applicable in diagnostics or therapeutic purposes.
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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.