ArticleScientific reports2016
Two common structural motifs for TCR recognition by staphylococcal enterotoxins.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Preliminary assessment of the therapeutic potential of staphylococcal enterotoxin-like W via biological activity and TCR binding sites analysis.Virulence · 2025Article
- Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025Article
- Targeting staphylococcal enterotoxin B binding to CD28 as a new strategy for dampening superantigen-mediated intestinal epithelial barrier dysfunctions.Frontiers in immunology · 2024Article
- The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL.FEBS open bio · 2023Article
- Bivalent binding of staphylococcal superantigens to the TCR and CD28 triggers inflammatory signals independently of antigen presenting cells.Frontiers in immunology · 2023Article
- Binding of Staphylococcal Enterotoxin B (SEB) to B7 Receptors Triggers TCR- and CD28-Mediated Inflammatory Signals in the Absence of MHC Class II Molecules.Frontiers in immunology · 2021Article
- Determining the immunological characteristics of a novel human monoclonal antibody developed against staphylococcal enterotoxin B.Human vaccines & immunotherapeutics · 2020Article
- Structure of Staphylococcal Enterotoxin N: Implications for Binding Properties to Its Cellular Proteins.International journal of molecular sciences · 2019Article
- Staphylococcal and Streptococcal Superantigens Trigger B7/CD28 Costimulatory Receptor Engagement to Hyperinduce Inflammatory Cytokines.Frontiers in immunology · 2019Article
- Binding of Catechins to Staphylococcal Enterotoxin A.Molecules (Basel, Switzerland) · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Superantigens are toxins produced by Staphylococcus aureus, called staphylococcal enterotoxins (abbreviated SEA to SEU). They can cross-link the T cell receptor (TCR) and major histocompatibility complex class II, triggering a massive T cell activation and hence disease. Due to high stability and toxicity, superantigens are potential agents of bioterrorism. Hence, antagonists may not only be useful in the treatment of disease but also serve as countermeasures to biological warfare. Of particular interest are inhibitors against SEA and SEB. SEA is the main cause of food poisoning, while SEB is a common toxin manufactured as a biological weapon. Here, we present the crystal structures of SEA in complex with TCR and SEE in complex with the same TCR, complemented with computational alanine-scanning mutagenesis of SEA, SEB, SEC3, SEE, and SEH. We have identified two common areas that contribute to the general TCR binding for these superantigens. This paves the way for design of single antagonists directed towards multiple toxins.
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