ArticleThe Journal of experimental medicine1995
Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II.
Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 174 citations in OpenAlex.
- Staphylococcal Enterotoxin A Shapes Monocyte Transcription and Macrophage Polarization: Implications for Immune Responses in Infection and Inflammation.European journal of immunology · 2025Article
- Current Views about the Inflammatory Damage Triggered by Bacterial Superantigens and Experimental Attempts to Neutralize Superantigen-Mediated Toxic Effects with Natural and Biological Products.Pathophysiology : the official journal of the International Society for Pathophysiology · 2024Review
- Blocking Superantigen-Mediated Diseases: Challenges and Future Trends.Journal of immunology research · 2024Review
- Development of Thermally Stable Nanobodies for Detection and Neutralization of Staphylococcal Enterotoxin B.Toxins · 2023Article
- Bivalent binding of staphylococcal superantigens to the TCR and CD28 triggers inflammatory signals independently of antigen presenting cells.Frontiers in immunology · 2023Article
- Hyperimmune Targeting Staphylococcal Toxins Effectively Protect Against USA 300 MRSA Infection in Mouse Bacteremia and Pneumonia Models.Frontiers in immunology · 2022Article
- Superantigen Recognition and Interactions: Functions, Mechanisms and Applications.Frontiers in immunology · 2021Review
- Review
- TBAScientific reports · 2019Article
- FDA-approved immunosuppressants targeting staphylococcal superantigens: mechanisms and insights.ImmunoTargets and therapy · 2017Review
- Tagging staphylococcal enterotoxin B (SEB) with TGFaL3 for breast cancer therapy.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Staphylococcal Superantigens Spark Host-Mediated Danger Signals.Frontiers in immunology · 2016Review
- Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.PloS one · 2015Article
- T-cell activation or tolerization: the Yin and Yang of bacterial superantigens.Frontiers in microbiology · 2015Article
- Staphylococcal enterotoxins in the etiopathogenesis of mucosal autoimmunity within the gastrointestinal tract.Toxins · 2014Review
- Update on staphylococcal superantigen-induced signaling pathways and therapeutic interventions.Toxins · 2013Review
- Staphylococcal and streptococcal superantigen exotoxins.Clinical microbiology reviews · 2013Review
- PI3K/Akt/mTOR, a pathway less recognized for staphylococcal superantigen-induced toxicity.Toxins · 2012Review
- Staphylococcal superantigens in colonization and disease.Frontiers in cellular and infection microbiology · 2012Review
- Gram-positive bacterial superantigen outside-in signaling causes toxic shock syndrome.The FEBS journal · 2011Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The superantigen staphylococcal enterotoxin A (SEA) binds to major histocompatibility complex (MHC) class II molecules at two sites on either side of the peptide groove. Two separate but cooperative interactions to the human class II molecule HLA-DR1 were detected. The first high affinity interaction to the DR1 beta chain is mediated by a zinc atom coordinated by H187, H225, and D227 in SEA and H81 in the polymorphic DR1 beta chain. The second low affinity site is to the DR1 alpha chain analogous to SEB binding and is mediated by residue F47 in SEA. Binding of one SEA to the DR1 beta chain enhances the binding of a second SEA molecule to the DR1 alpha chain. The zinc site is on the opposite side of the SEA molecule from residue F47 so that one SEA molecule can readily bind two class II molecules. Both binding sites on SEA are required for maximal activity. Thus, unlike, SEB, SEA requires two separate binding sites for optimal activity, which may allow it to stabilize SEA interaction with T cell receptors, as well as to activate the antigen-presenting cell by cross-linking MHC class II.
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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.