ArticleInfection and immunity2001
Inhibition of bacterial superantigens by peptides and antibodies.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 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.
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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
29 citing papers in PubMed, 70 citations in OpenAlex.
- The SEB1741 Aptamer Is an Efficient Tool for Blocking CD4+ T Cell Activation Induced by Staphylococcal Enterotoxin B.Molecules (Basel, Switzerland) · 2023Article
- Allergy-A New Role for T Cell Superantigens ofToxins · 2020Review
- Potent Neutralization of Staphylococcal Enterotoxin B In Vivo by Antibodies that Block Binding to the T-Cell Receptor.Journal of molecular biology · 2019Review
- Sepsis: mechanisms of bacterial injury to the patient.Scandinavian journal of trauma, resuscitation and emergency medicine · 2019Review
- Neutralization of staphylococcal enterotoxin B by an aptamer antagonist.Antimicrobial agents and chemotherapy · 2015Article
- Article
- Mesenchymal stromal (stem) cells suppress pro-inflammatory cytokine production but fail to improve survival in experimental staphylococcal toxic shock syndrome.BMC immunology · 2014Article
- Bacterial Toxins-Staphylococcal Enterotoxin B.Microbiology spectrum · 2013Article
- The staphylococcal enterotoxin (SE) family: SEB and siblings.Virulence · 2013Review
- Update on staphylococcal superantigen-induced signaling pathways and therapeutic interventions.Toxins · 2013Review
- PI3K/Akt/mTOR, a pathway less recognized for staphylococcal superantigen-induced toxicity.Toxins · 2012Review
- Immune aspects of sepsis and hope for new therapeutics.Current infectious disease reports · 2012Article
- Article
- Article
- Generation and characterization of high affinity human monoclonal antibodies that neutralize staphylococcal enterotoxin B.Journal of immune based therapies and vaccines · 2010Article
- Therapeutic down-modulators of staphylococcal superantigen-induced inflammation and toxic shock.Toxins · 2010Review
- Potent neutralization of staphylococcal enterotoxin B by synergistic action of chimeric antibodies.Infection and immunity · 2010Article
- Rapamycin protects mice from staphylococcal enterotoxin B-induced toxic shock and blocks cytokine release in vitro and in vivo.Antimicrobial agents and chemotherapy · 2010Article
- Dexamethasone attenuates staphylococcal enterotoxin B-induced hypothermic response and protects mice from superantigen-induced toxic shock.Antimicrobial agents and chemotherapy · 2006Article
- Bacillus anthracis edema toxin inhibits Staphylococcus aureus enterotoxin B effects in vitro: a potential protein therapeutic?Infection and immunity · 2005Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pyrogenic exotoxins of group A streptococci and staphylococcal enterotoxins are a family of structurally related superantigens with similar biological activity. Two distinct areas have been identified which have a highly conserved amino acid homology in all of the toxin families. A number of peptides were constructed from these regions, some of which were concatenated and polymerized to enhance their immunogenicity in animals. Antibodies prepared against these polymerized peptides were used to serologically identify the majority of the superantigen toxins, block the biological activities of the superantigens, and protect an experimental animal model against shock. In addition certain peptides were able per se to block up to 90% of the proliferative responses induced by the toxins. The peptide also proved protective in a septic shock model in mice. Binding experiments indicate that the peptide binds tightly to the major histocompatibility complex class II molecule, thus preventing binding and hence activation of the superantigen. The selective and rapid binding of the peptide to the major histocompatibility complex class II molecule may lead to a novel therapeutic modality in treatment of superantigen-mediated diseases.
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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.