Evidence map›Paper›PMID 20861327›Full record

ArticleClinical and vaccine immunology : CVI2010

A single, engineered protein therapeutic agent neutralizes exotoxins from both Staphylococcus aureus and Streptococcus pyogenes.

Ningyan Wang, Daiva M Mattis, Eric J Sundberg, Patrick M Schlievert, David M Kranz

Open access · diamondAbstract read
In one paragraph

Article in Clinical and vaccine immunology : CVI, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. 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
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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

5 authors at 3 institutions in 1 country.

Ningyan WangDepartment of Biochemistry, University of Illinois, 600 S. Mathews Ave., Urbana, IL 61801, USA.
Daiva M Mattis
Eric J Sundberg
Patrick M Schlievert
David M Kranz
Boston Biomedical Research Institute · USUniversity of Minnesota Medical Center · USUniversity of Illinois Urbana-Champaign · 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 HL096352NIAID NIH HHS AI064611NIAID NIH HHS AI065690NIAID NIH HHS R01 AI064611NIAID NIH HHS R01 AI065690NIAID NIH HHS U54 AI057153NIAID NIH HHS U54 AI57153
6 · The paper itself

Abstract

Staphylococcus aureus and Streptococcus pyogenes secrete exotoxins that act as superantigens, proteins that cause hyperimmune reactions by binding the variable domain of the T-cell receptor beta chain (Vβ), leading to stimulation of a large fraction of the T-cell repertoire. To develop potential neutralizing agents, we engineered Vβ mutants with high affinity for the superantigens staphylococcal enterotoxin B (SEB), SEC3, and streptococcal pyrogenic exotoxin A (SpeA). Unexpectedly, the high-affinity Vβ mutants generated against SEB cross-reacted with SpeA to a greater extent than they did with SEC3, despite greater sequence similarity between SEB and SEC3. Likewise, the Vβ mutants generated against SpeA cross-reacted with SEB to a greater extent than with SEC3. The structural basis of the high affinity and cross-reactivity was examined by single-site mutational analyses. The cross-reactivity seems to involve only one or two toxin residues. Soluble forms of the cross-reactive Vβ regions neutralized both SEB and SpeA in vivo, suggesting structure-based strategies for generating high-affinity neutralizing agents that can cross-react with multiple exotoxins.

Indexed as

AnimalsAntitoxinsBacterial ProteinsCross ReactionsEnterotoxinsExotoxinsMembrane ProteinsProtein BindingRabbitsReceptors, Antigen, T-Cell, alpha-betaRecombinant ProteinsStaphylococcus aureusStreptococcus pyogenesSuperantigensSurvival AnalysisVirulence FactorsAntitoxinsBacterial Proteinsenterotoxin B, staphylococcalEnterotoxinsExotoxinsMembrane ProteinsReceptors, Antigen, T-Cell, alpha-betaRecombinant ProteinsSpeA protein, Streptococcus pyogenesSuperantigensVirulence Factors

Identifiers

PMID20861327
PMCPMC2976085
OpenAlexW2161739915

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.