ArticleThe Journal of biological chemistry2014
Structural basis for antibody recognition in the receptor-binding domains of toxins A and B from Clostridium difficile.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 53 citations in OpenAlex.
- Development of Peptide Glucosyltransferase Inhibitors With Comprehensive Coverage Across Clostridioides difficile Toxin B Sub-Types.Biotechnology and bioengineering · 2026Article
- Chimeric Immunoglobulin and human Immunoglobulin M structures provide insights on joining-chain independent assembly and function.bioRxiv : the preprint server for biology · 2025Article
- De novo design of mini-protein binders broadly neutralizing Clostridioides difficile toxin B variants.Nature communications · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Engineered Secretory Immunoglobulin A provides insights on antibody-based effector mechanisms targetingbioRxiv : the preprint server for biology · 2023Article
- Design of 8-mer peptides that block Clostridioides difficile toxin A in intestinal cells.Communications biology · 2023Article
- Design of 8-mer Peptides that BlockbioRxiv : the preprint server for biology · 2023Article
- Structure-guided design of a potentFrontiers in microbiology · 2023Article
- Structure and conformational dynamics ofLife science alliance · 2022Article
- Clostridioides difficile toxins: mechanisms of action and antitoxin therapeutics.Nature reviews. Microbiology · 2022Review
- Neutralizing epitopes onFrontiers in immunology · 2022Article
- Application of recombinant antibodies for treatment ofFrontiers in immunology · 2022Review
- Novel structural insights for a pair of monoclonal antibodies recognizing non-overlapping epitopes of the glucosyltransferase domain ofCurrent research in structural biology · 2022Article
- A tetravalent single-chain variable fragment antibody for the detection of staphylococcal enterotoxin A.Journal of Zhejiang University. Science. B · 2021Article
- Structure of the full-length Clostridium difficile toxin B.Nature structural & molecular biology · 2019Article
- Application of Assisted Design of Antibody and Protein Therapeutics (ADAPT) improves efficacy of a Clostridium difficile toxin A single-domain antibody.Scientific reports · 2018Article
- Neutralization of Clostridium difficile toxin B with VHH-Fc fusions targeting the delivery and CROPs domains.PloS one · 2018Article
- Use of a neutralizing antibody helps identify structural features critical for binding ofThe Journal of biological chemistry · 2017Article
- Epitopes and Mechanism of Action of the Clostridium difficile Toxin A-Neutralizing Antibody Actoxumab.Journal of molecular biology · 2017Article
- Clostridium difficile Toxins A and B: Insights into Pathogenic Properties and Extraintestinal Effects.Toxins · 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 5 institutions in 1 country.
Funding
Abstract
Clostridium difficile infection is a serious and highly prevalent nosocomial disease in which the two large, Rho-glucosylating toxins TcdA and TcdB are the main virulence factors. We report for the first time crystal structures revealing how neutralizing and non-neutralizing single-domain antibodies (sdAbs) recognize the receptor-binding domains (RBDs) of TcdA and TcdB. Surprisingly, the complexes formed by two neutralizing antibodies recognizing TcdA do not show direct interference with the previously identified carbohydrate-binding sites, suggesting that neutralization of toxin activity may be mediated by mechanisms distinct from steric blockage of receptor binding. A camelid sdAb complex also reveals the molecular structure of the TcdB RBD for the first time, facilitating the crystallization of a strongly negatively charged protein fragment that has resisted previous attempts at crystallization and structure determination. Electrospray ionization mass spectrometry measurements confirm the stoichiometries of sdAbs observed in the crystal structures. These studies indicate how key epitopes in the RBDs from TcdA and TcdB are recognized by sdAbs, providing molecular insights into toxin structure and function and providing for the first time a basis for the design of highly specific toxin-specific therapeutic and diagnostic agents.
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.