ArticlePLoS pathogens2022
Probing the structure and function of the protease domain of botulinum neurotoxins using single-domain antibodies.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed.
- AVIDbase: A biologically accurate structural dataset of nanobody-antigen complexes.Protein science : a publication of the Protein Society · 2026Article
- A belt-buckle checkpoint regulates the onset of botulinum neurotoxin intoxication.Nature communications · 2026Article
- Comprehensive Mapping of Immune Nanobody Repertoires with NanoMAP.bioRxiv : the preprint server for biology · 2026Article
- Proteolytic Activities and Immunological Effects of Light Chains of Botulinum Neurotoxin A1, A2 and A3 Subtypes.Toxins · 2025Article
- Nanobody-Functionalized Magnetic Beads for Enrichment of Foodborne Botulinum Toxin Type A Light Chain.Journal of microbiology and biotechnology · 2025Article
- A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex.Science advances · 2025Article
- Passive Immunisation in the Treatment of Infectious Diseases Related to Highly Potent Bacterial Toxins.Biomedicines · 2024Review
- Bacterial cell surface characterization by phage display coupled to high-throughput sequencing.Nature communications · 2024Article
- A DARPin promotes faster onset of botulinum neurotoxin A1 action.Nature communications · 2023Article
- Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue fromInternational journal of molecular sciences · 2023Article
- Structural basis for botulinum neurotoxin E recognition of synaptic vesicle protein 2.Nature communications · 2023Article
- Biological and Immunological Characterization of a Functional L-HN Derivative of Botulinum Neurotoxin Serotype F.Toxins · 2023Article
- Enteric pharmacokinetics of monomeric and multimeric camelid nanobody single-domain antibodies.PloS one · 2023Article
- Yeast Display Enables Identification of Covalent Single-Domain Antibodies against Botulinum Neurotoxin Light Chain A.ACS chemical biology · 2022Article
- Identification and analysis of B cell epitopes of hemagglutinin of H1N1 influenza virus.Archives of microbiology · 2022Article
- Single Domain Antibody application in bacterial infection diagnosis and neutralization.Frontiers in immunology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Botulinum neurotoxins (BoNTs) are among the deadliest of bacterial toxins. BoNT serotype A and B in particular pose the most serious threat to humans because of their high potency and persistence. To date, there is no effective treatment for late post-exposure therapy of botulism patients. Here, we aim to develop single-domain variable heavy-chain (VHH) antibodies targeting the protease domains (also known as the light chain, LC) of BoNT/A and BoNT/B as antidotes for post-intoxication treatments. Using a combination of X-ray crystallography and biochemical assays, we investigated the structures and inhibition mechanisms of a dozen unique VHHs that recognize four and three non-overlapping epitopes on the LC of BoNT/A and BoNT/B, respectively. We show that the VHHs that inhibit the LC activity occupy the extended substrate-recognition exosites or the cleavage pocket of LC/A or LC/B and thus block substrate binding. Notably, we identified several VHHs that recognize highly conserved epitopes across BoNT/A or BoNT/B subtypes, suggesting that these VHHs exhibit broad subtype efficacy. Further, we identify two novel conformations of the full-length LC/A, that could aid future development of inhibitors against BoNT/A. Our studies lay the foundation for structure-based engineering of protein- or peptide-based BoNT inhibitors with enhanced potencies and cross-subtypes properties.
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.