ArticleApplied and environmental microbiology2009
Novel cell-based method to detect Shiga toxin 2 from Escherichia coli O157:H7 and inhibitors of toxin activity.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 72 citations in OpenAlex.
- Rapid Enzymatic Detection of Shiga-Toxin-ProducingACS infectious diseases · 2024Article
- Genomic and Phenotypic Characterization of Shiga Toxin-ProducingMicroorganisms · 2023Article
- Pathogenicity assessment of Shiga toxin-producingFrontiers in microbiology · 2023Article
- Comparative genomic and phenotypic analyses of the virulence potential in Shiga toxin-producingFrontiers in cellular and infection microbiology · 2022Article
- Plant Bioactive Compounds as an Intrinsic and Sustainable Tool to Enhance the Microbial Safety of Crops.Microorganisms · 2021Review
- Dietary Modulation of Bacteriophages as an Additional Player in Inflammation and Cancer.Cancers · 2021Review
- Therapeutic Strategies to Protect the Central Nervous System against Shiga Toxin from EnterohemorrhagicCurrent neuropharmacology · 2021Article
- Article
- Interplay between enterohaemorrhagicEmerging microbes & infections · 2020Article
- Role of the Nitric Oxide Reductase NorVW in the Survival and Virulence of EnterohaemorrhagicPathogens (Basel, Switzerland) · 2020Article
- Plant Phenolics and Phenolic-Enriched Extracts as Antimicrobial Agents against Food-Contaminating Microorganisms.Antioxidants (Basel, Switzerland) · 2020Review
- Fruit extracts to control pathogenicHeliyon · 2020Review
- Bimodal Response to Shiga Toxin 2 Subtypes Results from Relatively Weak Binding to the Target Cell.Infection and immunity · 2019Article
- Article
- Draft Genome Sequences of Shiga Toxin-Producing Escherichia coli O157:H7 Strains Recovered from a Major Production Region for Leafy Greens in California.Microbiology resource announcements · 2019Article
- Inhibition of bacterial toxin recognition of membrane components as an anti-virulence strategy.Journal of biological engineering · 2019Review
- Three Dimensional Vero Cell-Platform for Rapid and Sensitive Screening of Shiga-Toxin ProducingFrontiers in microbiology · 2019Article
- Catechin-mediated restructuring of a bacterial toxin inhibits activity.Biochimica et biophysica acta. General subjects · 2019Article
- Cellular recovery from exposure to sub-optimal concentrations of AB toxins that inhibit protein synthesis.Scientific reports · 2018Article
- Degradation and inactivation of Shiga toxins by nitrogen gas plasma.AMB Express · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli O157:H7 is a leading cause of food-borne illness. This human pathogen produces Shiga toxins (Stx1 and Stx2) which inhibit protein synthesis by inactivating ribosome function. The present study describes a novel cell-based assay to detect Stx2 and inhibitors of toxin activity. A Vero cell line harboring a destabilized variant (half-life, 2 h) of the enhanced green fluorescent protein (d2EGFP) was used to monitor the toxin-induced inhibition of protein synthesis. This Vero-d2EGFP cell line produced a fluorescent signal which could be detected by microscopy or with a plate reader. However, a greatly attenuated fluorescent signal was detected in Vero-d2EGFP cells that had been incubated overnight with either purified Stx2 or a cell-free culture supernatant from Stx1- and Stx2-producing E. coli O157:H7. Dose-response curves demonstrated that the Stx2-induced inhibition of enhanced green fluorescent protein fluorescence mirrored the Stx2-induced inhibition of overall protein synthesis and identified a picogram-per-milliliter threshold for toxin detection. To establish our Vero-d2EGFP assay as a useful tool for the identification of toxin inhibitors, we screened a panel of plant compounds for antitoxin activities. Fluorescent signals were maintained when Vero-d2EGFP cells were exposed to Stx1- and Stx2-containing medium in the presence of either grape seed or grape pomace extract. The antitoxin properties of the grape extracts were confirmed with an independent toxicity assay that monitored the overall level of protein synthesis in cells treated with purified Stx2. These results indicate that the Vero-d2EGFP fluorescence assay is an accurate and sensitive method to detect Stx2 activity and can be utilized to identify toxin inhibitors.
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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.