ArticleThe Journal of biological chemistry2014
The molecular mechanism of Shiga toxin Stx2e neutralization by a single-domain antibody targeting the cell receptor-binding domain.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Structural Basis of Shiga Toxin Neutralization by Human Antibodies Targeting Canonical Receptor-Binding and Non-Canonical Assembly Sites.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Practical Review on Aetio-Pathogenesis and Symptoms in Pigs Affected by Clinical and Subclinical Oedema Disease and the Use of Commercial Vaccines Under Field Conditions.Animals : an open access journal from MDPI · 2025Review
- Small but Mighty: Nanobodies in the Fight Against Infectious Diseases.Biomolecules · 2025Review
- Single domain antibodies from camelids in the treatment of microbial infections.Frontiers in immunology · 2024Review
- A Multi-Specific DARPin Potently Neutralizes Shiga Toxin 2 via Simultaneous Modulation of Both Toxin Subunits.Bioengineering (Basel, Switzerland) · 2022Article
- Single Domain Antibody application in bacterial infection diagnosis and neutralization.Frontiers in immunology · 2022Review
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- Identification of Nanobodies Blocking Intimate Adherence of Shiga Toxin-Producing Escherichia coli to Epithelial Cells.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Structural basis of nanobody recognition of grapevine fanleaf virus and of virus resistance loss.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Development and Evaluation of a Novel VHH-Based Immunocapture Assay for High-Sensitivity Detection of Shiga Toxin Type 2 (Stx2) in Stool Samples.Journal of clinical microbiology · 2020Article
- Optimizing the Design of Diatom Biosilica-Targeted Fusion Proteins in Biosensor Construction forBiology · 2020Article
- Use of camel single-domain antibodies for the diagnosis and treatment of zoonotic diseases.Comparative immunology, microbiology and infectious diseases · 2018Review
- Structural basis of VThe Journal of biological chemistry · 2018Article
- Structural Basis for the Specific Neutralization of Stx2a with a Camelid Single Domain Antibody Fragment.Toxins · 2018Article
- A neutralizing antibody that blocks delivery of the enzymatic cargo ofThe Journal of biological chemistry · 2018Article
- Escherichia coli surface display for the selection of nanobodies.Microbial biotechnology · 2017Review
- Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies.Veterinary research · 2015Article
- New Stx2e Monoclonal Antibodies for Immunological Detection and Distinction of Stx2 Subtypes.PloS one · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shiga toxin Stx2e is the major known agent that causes edema disease in newly weaned pigs. This severe disease is characterized by neurological disorders, hemorrhagic lesions, and frequent fatal outcomes. Stx2e consists of an enzymatically active A subunit and five B subunits that bind to a specific glycolipid receptor on host cells. It is evident that antibodies binding to the A subunit or the B subunits of Shiga toxin variants may have the capability to inhibit their cytotoxicity. Here, we report the discovery and characterization of a VHH single domain antibody (nanobody) isolated from a llama phage display library that confers potent neutralizing capacity against Stx2e toxin. We further present the crystal structure of the complex formed between the nanobody (NbStx2e1) and the Stx2e toxoid, determined at 2.8 Å resolution. Structural analysis revealed that for each B subunit of Stx2e, one NbStx2e1 is interacting in a head-to-head orientation and directly competing with the glycolipid receptor binding site on the surface of the B subunit. The neutralizing NbStx2e1 can in the future be used to prevent or treat edema disease.
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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.