ArticleNature communications2010
The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation.
Article in Nature communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 70 citations in OpenAlex.
- S. aureus exposure during cutaneous antigen sensitization causes basophil- and interleukin-4-dependent exaggerated food anaphylaxis.Immunity · 2025Article
- The identification of a SARs-CoV2 S2 protein derived peptide with super-antigen-like stimulatory properties on T-cells.Communications biology · 2025Article
- Novel insights into the immune response to bacterial T cell superantigens.Nature reviews. Immunology · 2024Review
- Review
- Article
- Innate TCRβ-chain engagement drives human T cells toward distinct memory-like effector phenotypes with immunotherapeutic potentials.Science advances · 2023Article
- The superantigens SpeC and TSST-1 specifically activate TRBV12-3/12-4Communications biology · 2023Article
- Superantigens, a Paradox of the Immune Response.Toxins · 2022Review
- A Sensitive Immunodetection Assay Using Antibodies Specific to Staphylococcal Enterotoxin B Produced by Baculovirus Expression.Biosensors · 2022Article
- Article
- The Inflammatory Cytokine Imbalance for Miscarriage, Pregnancy Loss and COVID-19 Pneumonia.Frontiers in immunology · 2022Review
- Editorial: Understanding and Engineering Antibody-Superantigen Interactions.Frontiers in immunology · 2022Article
- Longitudinal analysis of SARS-CoV-2 spike and RNA-dependent RNA polymerase protein sequences reveals the emergence and geographic distribution of diverse mutations.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2022Article
- HLA class I-associated expansion of TRBV11-2 T cells in multisystem inflammatory syndrome in children.The Journal of clinical investigation · 2021Article
- Mechanistic and Structural Features of PROTAC Ternary Complexes.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Superantigen Recognition and Interactions: Functions, Mechanisms and Applications.Frontiers in immunology · 2021Review
- Identification of a unique TCR repertoire, consistent with a superantigen selection process in Children with Multi-system Inflammatory Syndrome.bioRxiv : the preprint server for biology · 2020Article
- Superantigenic character of an insert unique to SARS-CoV-2 spike supported by skewed TCR repertoire in patients with hyperinflammation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- T Cell Immunity to Bacterial Pathogens: Mechanisms of Immune Control and Bacterial Evasion.International journal of molecular sciences · 2020Review
- An insertion unique to SARS-CoV-2 exhibits superantigenic character strengthened by recent mutations.bioRxiv : the preprint server for biology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable β-domain of TCR (TCRVβ). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic shock syndrome. In this study, we report the X-ray structure of the ternary complex between staphylococcal enterotoxin H (SEH) and its human receptors, MHC class II and TCR. The structure demonstrates that SEH predominantly interacts with the variable α-domain of TCR (TCRVα), which is supported by nuclear magnetic resonance (NMR) analyses. Furthermore, there is no contact between MHC and TCR upon complex formation. Structural analyses suggest that the major contact points to TCRVα are conserved among other bacterial SAgs. Consequently, a new dimension of SAg biology emerges, suggesting that in addition to the conventional interactions with the TCRVβ domain, SAgs can also activate T cells through the TCRVα domain.
Identifiers
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.