ReviewMicrobiology spectrum2014
Shiga Toxin (Stx) Classification, Structure, and Function.
Review in Microbiology spectrum, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 291 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
291 citing papers in PubMed, 497 citations in OpenAlex.
- Milk-derived peptone reduces EHEC virulence by inhibiting the type III secretion system.Virulence · 2026Article
- Shiga Toxin-ProducingAntibiotics (Basel, Switzerland) · 2026Review
- Ribosome-inactivating proteins in bacteria.Microbial genomics · 2026Review
- 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
- Algorithm and Software to Type Stx Operons Accurately from Assembled Genomic Sequence.Microorganisms · 2026Article
- Susceptibility of Human B-Lymphoblastoid Cells to Shiga Toxin Intoxication Homologues.Microorganisms · 2026Article
- Molecular Characterization of Multidrug-ResistantAntibiotics (Basel, Switzerland) · 2026Article
- Structure and function of a fungal AB toxin-like chimerolectin involved in anti-nematode defense.The EMBO journal · 2026Article
- Shiga toxin delivery in extracellular vesicles induces high mortality and severe kidney injury in a Gb3-dependent manner.PLoS pathogens · 2026Article
- Prevalence, virulence profiling, and latent antimicrobial resistance determinants ofVeterinary world · 2026Article
- Plasma membrane invaginations and their diverse cellular functions.BMC biology · 2026Review
- Phage toxin variants are linked to protection specificity in a defensive symbiont.Molecular biology and evolution · 2026Article
- Comparative Genomics ofPathogens (Basel, Switzerland) · 2026Article
- Subverting Host Defense from Within: Innate Immune Modulation byPathogens (Basel, Switzerland) · 2026Review
- AnMicrobiology spectrum · 2026Article
- Comparison of hybrid-and mono-pathotype Escherichia coli isolates from South Korea based on whole genome analysis and cytotoxicity assay.Journal of biomedical science · 2026Article
- Carbohydrate-based biosensors for enhanced pathogen detection.Analytical and bioanalytical chemistry · 2026Review
- Use of GbAnalytical and bioanalytical chemistry · 2026Article
- Factors Governing the Cross-Species Virulence of Shiga Toxin-ProducingPathogens (Basel, Switzerland) · 2026Article
- Shiga toxin increases intestinal transit to displace resident microbes and facilitate pathogen colonization.PLoS pathogens · 2026Article
231 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
1 author at 1 institution in 1 country.
Funding
Abstract
Shiga toxin (Stx) is one of the most potent bacterial toxins known. Stx is found in Shigella dysenteriae 1 and in some serogroups of Escherichia coli (called Stx1 in E. coli). In addition to or instead of Stx1, some E. coli strains produce a second type of Stx, Stx2, that has the same mode of action as Stx/Stx1 but is antigenically distinct. Because subtypes of each toxin have been identified, the prototype toxin for each group is now designated Stx1a or Stx2a. The Stxs consist of two major subunits, an A subunit that joins noncovalently to a pentamer of five identical B subunits. The A subunit of the toxin injures the eukaryotic ribosome and halts protein synthesis in target cells. The function of the B pentamer is to bind to the cellular receptor, globotriaosylceramide, Gb3, found primarily on endothelial cells. The Stxs traffic in a retrograde manner within the cell, such that the A subunit of the toxin reaches the cytosol only after the toxin moves from the endosome to the Golgi and then to the endoplasmic reticulum. In humans infected with Stx-producing E. coli, the most serious manifestation of the disease, hemolytic-uremic syndrome, is more often associated with strains that produce Stx2a rather than Stx1a, and that relative toxicity is replicated in mice and baboons. Stx1a and Stx2a also exhibit differences in cytotoxicity to various cell types, bind dissimilarly to receptor analogs or mimics, induce differential chemokine responses, and have several distinctive structural characteristics.
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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.