ReviewToxins2011
Botulinum neurotoxins and botulism: a novel therapeutic approach.
Review in Toxins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Nanobody-Functionalized Magnetic Beads for Enrichment of Foodborne Botulinum Toxin Type A Light Chain.Journal of microbiology and biotechnology · 2025Article
- Botulinum Neurotoxins as Two-Faced Janus Proteins.Biomedicines · 2025Review
- Selection of Candidate Monoclonal Antibodies for Therapy of Botulinum Toxin Type A Intoxications.Toxins · 2024Article
- Article
- Isolation and characterization of Hc-targeting chimeric heavy chain antibodies neutralizing botulinum neurotoxin type B.Frontiers in immunology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- How Botulinum Neurotoxin Light Chain A1 Maintains Stable Association with the Intracellular Neuronal Plasma Membrane.Toxins · 2022Article
- Camelid VHH Antibodies that Neutralize Botulinum Neurotoxin Serotype E Intoxication or Protease Function.Toxins · 2020Article
- Docking Simulation and Sandwich Assay for Aptamer-Based Botulinum Neurotoxin Type C Detection.Biosensors · 2020Article
- Camelid VHHs Fused to Human Fc Fragments Provide Long Term Protection Against Botulinum Neurotoxin A in Mice.Toxins · 2019Article
- Genetically engineered red cells expressing single domain camelid antibodies confer long-term protection against botulinum neurotoxin.Nature communications · 2017Article
- Antibody Engineering for Pursuing a Healthier Future.Frontiers in microbiology · 2017Review
- Article
- Botulinum neurotoxins: genetic, structural and mechanistic insights.Nature reviews. Microbiology · 2014Review
- Designing and analyzing the structure of Tat-BoNT/A(1-448) fusion protein: AnMolecular biology research communications · 2014Article
- Comparison of assembled Clostridium botulinum A1 genomes revealed their evolutionary relationship.Genomics · 2014Article
- Phage display--a powerful technique for immunotherapy: 1. Introduction and potential of therapeutic applications.Human vaccines & immunotherapeutics · 2012Review
- Article
- Cell penetrable humanized-VH/V(H)H that inhibit RNA dependent RNA polymerase (NS5B) of HCV.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Specific treatment is not available for human botulism. Current remedial mainstay is the passive administration of polyclonal antibody to botulinum neurotoxin (BoNT) derived from heterologous species (immunized animal or mouse hybridoma) together with supportive and symptomatic management. The antibody works extracellularly, probably by blocking the binding of receptor binding (R) domain to the neuronal receptors; thus inhibiting cellular entry of the holo-BoNT. The antibody cannot neutralize the intracellular toxin. Moreover, a conventional antibody with relatively large molecular size (150 kDa) is not accessible to the enzymatic groove and, thus, cannot directly inhibit the BoNT zinc metalloprotease activity. Recently, a 15-20 kDa single domain antibody (V(H)H) that binds specifically to light chain of BoNT serotype A was produced from a humanized-camel VH/V(H)H phage display library. The V(H)H has high sequence homology (>80%) to the human VH and could block the enzymatic activity of the BoNT. Molecular docking revealed not only the interface binding between the V(H)H and the toxin but also an insertion of the V(H)H CDR3 into the toxin enzymatic pocket. It is envisaged that, by molecular linking the V(H)H to a cell penetrating peptide (CPP), the CPP-V(H)H fusion protein would be able to traverse the hydrophobic cell membrane into the cytoplasm and inhibit the intracellular BoNT. This presents a novel and safe immunotherapeutic strategy for botulism by using a cell penetrating, humanized-single domain antibody that inhibits the BoNT by means of a direct blockade of the groove of the menace enzyme.
Indexed as
Identifiers
What OpenQuestion holds
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.