ArticleCellular microbiology2019
The structure of the Shiga toxin 2a A-subunit dictates the interactions of the toxin with blood components.
Article in Cellular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Advancing Medical Diagnostics: Rapid, Label-Free Detection and Differentiation of Shiga Toxin Variants in Human Serum Using a Cost-Effective PCA-Assisted SERS Platform.ACS applied materials & interfaces · 2025Article
- Diagnostic oriented discrimination of different Shiga toxins via PCA-assisted SERS-based plasmonic metasurface.Nanophotonics (Berlin, Germany) · 2025Article
- Article
- Enzymatic Cleavage of Stx2a in the Gut and Identification of Pancreatic Elastase and Trypsin as Possible Main Cleavers.Microorganisms · 2023Article
- Article
- Plasmonic Metasurfaces for Specific SERS Detection of Shiga Toxins.ACS applied materials & interfaces · 2022Article
- Shiga Toxin 2a Induces NETosis via NOX-Dependent Pathway.Biomedicines · 2021Article
- Cytotoxic Effects of Recombinant StxA2-His in the Absence of Its Corresponding B-Subunit.Toxins · 2021Article
- Method for the Detection of the Cleaved Form of Shiga Toxin 2a Added to Normal Human Serum.Toxins · 2021Article
- Shiga Toxin 2a Binds to Complement Components C3b and C5 and Upregulates Their Gene Expression in Human Cell Lines.Toxins · 2020Article
- Article
- Molecular Biology ofToxins · 2020Review
- Verotoxin Receptor-Based Pathology and Therapies.Frontiers in cellular and infection microbiology · 2020Review
- The structure of the Shiga toxin 2a A-subunit dictates the interactions of the toxin with blood components.Cellular microbiology · 2019Article
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 2 countries.
Funding
Abstract
Hemolytic uremic syndrome (eHUS) is a severe complication of human infections with Shiga toxins (Stxs)-producing Escherichia coli. A key step in the pathogenesis of eHUS is the interaction of Stxs with blood components before the targeting of renal endothelial cells. Here, we show that a single proteolytic cleavage in the Stx2a A-subunit, resulting into two fragments (A1 and A2) linked by a disulfide bridge (cleaved Stx2a), dictates different binding abilities. Uncleaved Stx2a was confirmed to bind to human neutrophils and to trigger leukocyte/platelet aggregate formation, whereas cleaved Stx2a was ineffective. Conversely, binding of complement factor H was confirmed for cleaved Stx2a and not for uncleaved Stx2a. It is worth noting that uncleaved and cleaved Stx2a showed no differences in cytotoxicity for Vero cells or Raji cells, structural conformation, and contaminating endotoxin. These results have been obtained by comparing two Stx2a batches, purified in different laboratories by using different protocols, termed Stx2a(cl; cleaved toxin, Innsbruck) and Stx2a(uncl; uncleaved toxin, Bologna). Stx2a(uncl) behaved as Stx2a(cl) after mild trypsin treatment. In this light, previous controversial results obtained with purified Stx2a has to be critically re-evaluated; furthermore, characterisation of the structure of circulating Stx2a is mandatory to understand eHUS-pathogenesis and to develop therapeutic approaches.
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Registered trials
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