ArticleToxins2012
Interaction between Shiga toxin and monoclonal antibodies: binding characteristics and in vitro neutralizing abilities.
Article in Toxins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
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Who cites it
26 citing papers in PubMed, 38 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
- Shiga toxin-centered pathophysiology defines the therapeutic limits of enterohemorrhagic Escherichia coli infection.Archives of microbiology · 2026Review
- SARS-CoV-2 Rapid Antigen Test Based on a New Anti-Nucleocapsid Protein Monoclonal Antibody: Development and Real-Time Validation.Microorganisms · 2023Article
- Identification of Zika Virus NS1-Derived Peptides with Potential Applications in Serological Tests.Viruses · 2023Article
- Detection of Shiga Toxin-ProducingFrontiers in endocrinology · 2022Article
- Therapeutic Antibodies Against Shiga Toxins: Trends and Perspectives.Frontiers in cellular and infection microbiology · 2022Review
- The Deleterious Effects of Shiga Toxin Type 2 Are Neutralized In Vitro by FabF8:Stx2 Recombinant Monoclonal Antibody.Toxins · 2021Article
- Article
- Zebrafish embryo sensitivity test as in vivo platform to anti-Shiga toxin compound screening.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Article
- Article
- Development and Validation of Shiga Toxin-ProducingMicroorganisms · 2019Article
- Endocytosis, Cytotoxicity, and Translocation of Shiga Toxin-2 Are Stimulated by Infection of Human Intestinal (HCT-8) Monolayers With an HypervirulentFrontiers in cellular and infection microbiology · 2019Article
- Article
- Structural Changes in Stx1 Engineering Monoclonal Antibody Improves Its Functionality as Diagnostic Tool for a Rapid Latex Agglutination Test.Antibodies (Basel, Switzerland) · 2018Article
- Epitope Sequences in Dengue Virus NS1 Protein Identified by Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2017Article
- ppGpp and cytotoxicity diversity in Shiga toxin-producing Escherichia coli (STEC) isolates.Epidemiology and infection · 2017Article
- Diarrheagenic Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2016Review
- Characterization of the universal stress protein F from atypical enteropathogenic Escherichia coli and its prevalence in Enterobacteriaceae.Protein science : a publication of the Protein Society · 2016Article
- Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones.Sensors (Basel, Switzerland) · 2016Article
- Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (MAbs) have been employed either for diagnosis or treatment of infections caused by different pathogens. Specifically for Shiga toxin-producing Escherichia coli (STEC), numerous immunoassays have been developed for STEC diagnosis, showing variability in sensitivity and specificity when evaluated by reference laboratories, and no therapy or vaccines are currently approved. Thus, the aim of this work was the characterization of the interaction between MAbs against Stx1 and Stx2 toxins and their neutralizing abilities to enable their use as tools for diagnosis and therapy. The selected clones designated 3E2 (anti-Stx1) and 2E11 (anti-Stx2) were classified as IgG1. 3E2 recognized the B subunit of Stx1 with an affinity constant of 2.5 × 10(-10) M, detected as little as 6.2 ng of Stx1 and was stable up to 50 ºC. In contrast, 2E11 recognized the A subunit of Stx2, was stable up to 70 ºC, had a high dissociation constant of 6.1 × 10(-10) M, and detected as little as 12.5 ng of Stx2. Neutralization tests showed that 160 ng of 3E2 MAb inhibited 80% of Stx1 activity and 500 µg 2E11 MAb were required for 60% inhibition of Stx2 activity. These MAb amounts reversed 25 to 80% of the cytotoxicity triggered by different STEC isolates. In conclusion, these MAbs show suitable characteristics for their use in STEC diagnosis and encourage future studies to investigate their protective efficacy.
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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.