ArticleInfection and immunity2006
The Bacteroides fragilis toxin binds to a specific intestinal epithelial cell receptor.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 2 of them syntheses that pooled it.
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.
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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
67 citing papers in PubMed, 2 syntheses or guidelines pooled it, 95 citations in OpenAlex.
- Identification of host gene-microbiome associations in colorectal cancer patients using mendelian randomization.Journal of translational medicine · 2023Pooled it
- A systemic review of the role of enterotoxic Bacteroides fragilis in colorectal cancer.Neoplasia (New York, N.Y.) · 2022Pooled it
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- An anaerobic pathogen rewires host metabolism to fuel oxidative growth in the inflamed gut.Cell · 2026Article
- Orally available designed miniproteins inhibit enterotoxigenicbioRxiv : the preprint server for biology · 2026Article
- Gut Bacteria: A Beneficial Symbiosis or a Hidden Threat? Investigating the Dual Role of Bacteria in Gastrointestinal Diseases.Current microbiology · 2026Review
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- Repurposing Drugs as Bacteroides fragilis BFT-3 Inhibitors in the Animal Infection Model Galleria mellonella.Annals of the New York Academy of Sciences · 2026Article
- The Barrier-Microbiota-Inflammation Axis in Colorectal Cancer: Mechanisms and Emerging Diagnostic & Therapeutic Strategies.Cancers · 2026Review
- The Ambivalent Nature ofToxins · 2025Review
- Modeling ETBF-Mediated Colorectal Tumorigenesis Using AOM/DSS in Wild-Type Mice.International journal of molecular sciences · 2025Article
- Biological Mechanisms of EnterotoxigenicToxins · 2025Review
- Article
- Clinical Detection and Management of Colorectal Cancer Concerning the Gut Microbiome.Scientifica · 2025Review
- Keystone pathobionts associated with colorectal cancer promote oncogenic reprograming.PloS one · 2024Article
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- Keystone pathobionts associated with colorectal cancer promote oncogenic reprograming.bioRxiv : the preprint server for biology · 2023Article
- Review
- Gut microbiota, an emergent target to shape the efficiency of cancer therapy.Exploration of targeted anti-tumor therapy · 2023Review
7 more citing papers are in PubMed but not listed here.
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 at 2 institutions in 1 country.
Funding
Abstract
The Bacteroides fragilis toxin (BFT) is the only known virulence factor of enterotoxigenic B. fragilis. BFT has previously been shown to act, at least in part, through cleavage of the intercellular adhesion protein E-cadherin. A specific cellular receptor for BFT has not been identified. The goal of this study was to determine if the initial interaction of BFT with intestinal epithelial cells was consistent with binding to a specific cellular receptor. Purified BFT was labeled with a fluorophore or iodide to assess specific cellular binding and the properties of BFT cellular binding. BFT binds specifically to intestinal epithelial cell lines in vitro in a polarized manner. However, specific binding occurs only at 37 degrees C and requires BFT metalloprotease activity. The BFT receptor is predicted to be a membrane protein other than E-cadherin or a known protease-activated receptor (PAR1 to PAR4). BFT binding is resistant to acid washing, suggesting an irreversible interaction. Sugar or lipid residues do not appear to be involved in the mechanism of BFT cellular binding, but binding is sensitive to membrane cholesterol depletion. We conclude that intestinal epithelial cells in vitro possess a specific membrane BFT receptor that is distinct from E-cadherin. The data favor a model in which the metalloprotease domain of BFT processes its receptor protein, initiating cellular signal transduction that mediates the biological activity of BFT. However, activation of recognized protease-activated receptors does not mimic or block BFT biological activity or binding, suggesting that additional protease-activated receptors on intestinal epithelial cells remain to be identified.
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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.