Evidence map›Paper›PMID 23161916›Full record

ArticleProtein engineering, design & selection : PEDS2013

Engineering a soluble high-affinity receptor domain that neutralizes staphylococcal enterotoxin C in rabbit models of disease.

D M Mattis, A R Spaulding, O N Chuang-Smith, E J Sundberg, P M Schlievert, D M Kranz

Open access · bronzeAbstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. The virulence toolkit of Staphylococcus aureus: a comprehensive review of toxin diversity, molecular mechanisms, and clinical implications.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Review
  3. Toxins · 2021
    Review
  4. Review
  5. TBAScientific reports · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

D M MattisDepartment of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
A R Spaulding
O N Chuang-Smith
E J Sundberg
P M Schlievert
D M Kranz
University of Minnesota · USUniversity of Illinois Urbana-Champaign · USBoston Biomedical Research Institute · US

Funding

Vaccines and Therapies Against BotulismU54AI057153 · NIAID · UNIVERSITY OF CHICAGO · PI CROSSON, SEAN · 2003 to 2013
$87.6M
Development of Superantigen AntagonistsR01AI065690 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI SUNDBERG, ERIC JOHN · 2008 to 2011
$1.8M
Receptor-Based Therapeutics for EnterotoxinsR01AI064611 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KRANZ, DAVID M. · 2005 to 2009
$1.5M
Engineering Soluble T Cell Receptors to Treat Exotoxin Induced Pulmonary DiseaseF30HL096352 · NHLBI · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MATTIS, DAIVA MARIA · 2009 to 2014
$278k
NHLBI NIH HHS F30 HL096352NHLBI NIH HHS F30-HL096352-01NIAID NIH HHS R01-AI064611NIAID NIH HHS R01-AI065690NIAID NIH HHS U54 AI57153
6 · The paper itself

Abstract

Superantigens (SAgs) are a class of immunostimulatory exotoxins that activate large numbers of T cells, leading to overproduction of cytokines and subsequent inflammatory reactions and systemic toxicity. Staphylococcal enterotoxin C (SEC), a SAg secreted by Staphylococcus aureus, has been implicated in various illnesses including non-menstrual toxic shock syndrome (TSS) and necrotizing pneumonia. SEC has been shown to cause TSS illness in rabbits and the toxin contributes to lethality associated with methicillin-resistant S.aureus (MRSA) in a rabbit model of pneumonia. With the goal of reducing morbidity and mortality associated with SEC, a high-affinity variant of the extracellular variable domain of the T-cell receptor beta-chain for SEC (~14 kDa) was generated by directed evolution using yeast display. This protein was characterized biochemically and shown to cross-react with the homologous (65% identical) SAg staphylococcal enterotoxin B (SEB). The soluble, high-affinity T-cell receptor protein neutralized SEC and SEB in vitro and also significantly reduced the bacterial burden of an SEC-positive strain of MRSA (USA400 MW2) in an infective endocarditis model. The neutralizing agent also prevented lethality due to MW2 in a necrotizing pneumonia rabbit model. These studies characterize a soluble high-affinity neutralizing agent against SEC, which is cross-reactive with SEB, and that has potential to be used intravenously with antibiotics to manage staphylococcal diseases that involve these SAgs.

Indexed as

AnimalsAnti-Bacterial AgentsCell LineCell Surface Display TechniquesDirected Molecular EvolutionDisease Models, AnimalEndocarditis, BacterialEnterotoxinsHumansInterleukin-2Lymphocyte ActivationMethicillin-Resistant Staphylococcus aureusPneumonia, StaphylococcalProtein BindingProtein EngineeringRabbitsAnti-Bacterial Agentsenterotoxin C, staphylococcalEnterotoxinsInterleukin-2Receptors, Antigen, T-Cell, alpha-betaRecombinant ProteinsSuperantigens

Identifiers

PMID23161916
PMCPMC3542526
OpenAlexW2124677962

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.