ArticlePloS one2010
Molecular basis of differential B-pentamer stability of Shiga toxins 1 and 2.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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
19 citing papers in PubMed, 42 citations in OpenAlex.
- Cryo-EM structures of engineered Shiga toxin-based immunogens capable of eliciting neutralizing antibodies with therapeutic potential against hemolytic uremic syndrome.Protein science : a publication of the Protein Society · 2025Article
- Excess A-subunits of Shiga toxin 2a are produced in enterohemorrhagic Escherichia coli.Scientific reports · 2025Article
- Lectin-anticancer peptide fusion demonstrates a significant cancer-cell-selective cytotoxic effect and inspires the production of "clickable" anticancer peptide in Escherichia coli.Protein science : a publication of the Protein Society · 2023Article
- Cytotoxic Effects of Recombinant StxA2-His in the Absence of Its Corresponding B-Subunit.Toxins · 2021Article
- Verotoxin Receptor-Based Pathology and Therapies.Frontiers in cellular and infection microbiology · 2020Review
- AB5 Preassembly Is Not Required for Shiga Toxin Activity.Journal of bacteriology · 2016Article
- Review
- Mass Spectrometry-Based Method of Detecting and Distinguishing Type 1 and Type 2 Shiga-Like Toxins in Human Serum.Toxins · 2015Article
- Shiga Toxin (Stx) Classification, Structure, and Function.Microbiology spectrum · 2014Review
- Shiga-like toxin B subunit of Escherichia coli as scaffold for high-avidity display of anti-immunocomplex peptides.Analytical chemistry · 2014Article
- Article
- Glycolipid binding preferences of Shiga toxin variants.PloS one · 2014Article
- Binding of Pk-trisaccharide analogs of globotriaosylceramide to Shiga toxin variants.Infection and immunity · 2013Article
- Analyzing of expression of novel polypeptide complexes consisting of Shiga toxin B subunit and Adherence Fimbriae of Escherichia coli based on in silico modeling.Journal of molecular modeling · 2012Article
- Beta-strand interfaces of non-dimeric protein oligomers are characterized by scattered charged residue patterns.PloS one · 2012Article
- Shiga toxin binding to glycolipids and glycans.PloS one · 2012Article
- Interaction of ricin and Shiga toxins with ribosomes.Current topics in microbiology and immunology · 2012Review
- Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2.The international journal of biochemistry & cell biology · 2011Article
- Shiga toxin subtypes display dramatic differences in potency.Infection and immunity · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Escherichia coli strain O157:H7 is a major cause of food poisoning that can result in severe diarrhea and, in some cases, renal failure. The pathogenesis of E. coli O157:H7 is in large part due to the production of Shiga toxin (Stx), an AB(5) toxin that consists of a ribosomal RNA-cleaving A-subunit surrounded by a pentamer of receptor-binding B subunits. There are two major isoforms, Stx1 and Stx2, which differ dramatically in potency despite having 57% sequence identity. Animal studies and epidemiological studies show Stx2 is associated with more severe disease. Although the molecular basis of this difference is unknown, data suggest it is associated with the B-subunit. Mass spectrometry studies have suggested differential B-pentamer stability between Stx1 and Stx2. We have examined the relative stability of the B-pentamers in solution. Analytical ultracentrifugation using purified B-subunits demonstrates that Stx2B, the more deadly isoform, shows decreased pentamer stability compared to Stx1B (EC(50) = 2.3 µM vs. EC(50) = 0.043 µM for Stx1B). X-ray crystal structures of Stx1B and Stx2B identified a glutamine in Stx2 (versus leucine in Stx1) within the otherwise strongly hydrophobic interface between B-subunits. Interchanging these residues switches the stability phenotype of the B-pentamers of Stx1 and Stx2, as demonstrated by analytical ultracentrifugation and circular dichroism. These studies demonstrate a profound difference in stability of the B-pentamers in Stx1 and Stx2, illustrate the mechanistic basis for this differential stability, and provide novel reagents to test the basis for differential pathogenicity of these toxins.
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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.