ArticleInfection and immunity2016
The A1 Subunit of Shiga Toxin 2 Has Higher Affinity for Ribosomes and Higher Catalytic Activity than the A1 Subunit of Shiga Toxin 1.
Article in Infection and immunity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 36 citations in OpenAlex.
- Evolution of specialized toxin arsenals in a bacterial symbiont of arthropods.The ISME journal · 2025Article
- Comparative genomics of Shiga toxin-producingFrontiers in veterinary science · 2025Article
- Rapid Enzymatic Detection of Shiga-Toxin-ProducingACS infectious diseases · 2024Article
- Fragment Screening to Identify Inhibitors Targeting Ribosome Binding of Shiga Toxin 2.ACS infectious diseases · 2024Article
- Structure-Function Analysis of the A1 Subunit of Shiga Toxin 2 with Peptides That Target the P-Stalk Binding Site and Inhibit Activity.Biochemistry · 2024Article
- A Comprehensive Review on Shiga Toxin Subtypes and Their Niche-Related Distribution Characteristics in Shiga-Toxin-ProducingMicroorganisms · 2024Review
- Genetic and virulence characteristics of hybrid Shiga toxin-producing and atypical enteropathogenicFrontiers in microbiology · 2024Article
- The diverse landscape of AB5-type toxins.Engineering microbiology · 2023Review
- Platelets andBiomedicines · 2022Review
- EnterohemorrhagicInternational journal of molecular sciences · 2022Review
- Characterization of Atypical Shiga Toxin Gene Sequences and Description of Stx2j, a New Subtype.Journal of clinical microbiology · 2022Article
- ABToxins · 2022Review
- Mucoricin is a ricin-like toxin that is critical for the pathogenesis of mucormycosis.Nature microbiology · 2021Article
- Shiga toxin suppresses noncanonical inflammasome responses to cytosolic LPS.Science immunology · 2020Article
- Molecular Biology ofToxins · 2020Review
- Production of functional mimics of human milk oligosaccharides by enzymatic glycosylation of bovine milk oligosaccharides.International dairy journal · 2020Article
- Bimodal Response to Shiga Toxin 2 Subtypes Results from Relatively Weak Binding to the Target Cell.Infection and immunity · 2019Article
- Shiga toxin-producingCanada communicable disease report = Releve des maladies transmissibles au Canada · 2019Article
- How Ricin Damages the Ribosome.Toxins · 2019Review
- Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins.Toxins · 2018Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Shiga toxin (Stx)-producing Escherichia coli (STEC) infections can lead to life-threatening complications, including hemorrhagic colitis (HC) and hemolytic-uremic syndrome (HUS), which is the most common cause of acute renal failure in children in the United States. Stx1 and Stx2 are AB5 toxins consisting of an enzymatically active A subunit associated with a pentamer of receptor binding B subunits. Epidemiological evidence suggests that Stx2-producing E. coli strains are more frequently associated with HUS than Stx1-producing strains. Several studies suggest that the B subunit plays a role in mediating toxicity. However, the role of the A subunits in the increased potency of Stx2 has not been fully investigated. Here, using purified A1 subunits, we show that Stx2A1 has a higher affinity for yeast and mammalian ribosomes than Stx1A1. Biacore analysis indicated that Stx2A1 has faster association and dissociation with ribosomes than Stx1A1. Analysis of ribosome depurination kinetics demonstrated that Stx2A1 depurinates yeast and mammalian ribosomes and an RNA stem-loop mimic of the sarcin/ricin loop (SRL) at a higher catalytic rate and is a more efficient enzyme than Stx1A1. Stx2A1 depurinated ribosomes at a higher level in vivo and was more cytotoxic than Stx1A1 in Saccharomyces cerevisiae. Stx2A1 depurinated ribosomes and inhibited translation at a significantly higher level than Stx1A1 in human cells. These results provide the first direct evidence that the higher affinity for ribosomes in combination with higher catalytic activity toward the SRL allows Stx2A1 to depurinate ribosomes, inhibit translation, and exhibit cytotoxicity at a significantly higher level than Stx1A1.
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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.