Evidence map›Paper›PMID 17268555›Full record

ArticleThe EMBO journal2007

Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1.

Beenu Moza, Ashok K Varma, Rebecca A Buonpane, Penny Zhu, Christine A Herfst, Melissa J Nicholson, Anne-Kathrin Wilbuer, Nilufer P Seth, Kai W Wucherpfennig, John K McCormick and 2 more

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 61 citations in OpenAlex.

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  14. T cell receptor variableOpen journal of immunology · 2013
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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

12 authors at 4 institutions in 2 countries.

Beenu MozaBoston Biomedical Research Institute, Watertown, MA 02472, USA.
Ashok K Varma
Rebecca A Buonpane
Penny Zhu
Christine A Herfst
Melissa J Nicholson
Anne-Kathrin Wilbuer
Nilufer P Seth
Kai W Wucherpfennig
John K McCormick
David M Kranz
Eric J Sundberg
Boston Biomedical Research Institute · USHarvard University · USUniversity of Illinois Urbana-Champaign · USWestern University · CA

Funding

Cellular and Molecular Biology Training GrantT32GM007283 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI MORRISSEY, JAMES H. · 1985 to 2011
$4.7M
TCR Crossreactivity in Autoimmune DiseasesR01AI064177 · NIAID · DANA-FARBER CANCER INSTITUTE · PI WUCHERPFENNIG, KAI W · 2005 to 2009
$1.9M
Receptor-Based Therapeutics for EnterotoxinsR01AI064611 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KRANZ, DAVID M. · 2005 to 2009
$1.5M
Development of Superantigen AntagonistsR21AI055882 · NIAID · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI SUNDBERG, ERIC J · 2003 to 2004
$523k
NIAID NIH HHS AI064177NIAID NIH HHS AI064611NIAID NIH HHS AI55882NIAID NIH HHS R01 AI064177NIAID NIH HHS R01 AI064611NIAID NIH HHS R21 AI055882NIGMS NIH HHS T32 GM007283NIGMS NIH HHS T32 GM 07283
6 · The paper itself

Abstract

Superantigens (SAGs) bind simultaneously to major histocompatibility complex (MHC) and T-cell receptor (TCR) molecules, resulting in the massive release of inflammatory cytokines that can lead to toxic shock syndrome (TSS) and death. A major causative agent of TSS is toxic shock syndrome toxin-1 (TSST-1), which is unique relative to other bacterial SAGs owing to its structural divergence and its stringent TCR specificity. Here, we report the crystal structure of TSST-1 in complex with an affinity-matured variant of its wild-type TCR ligand, human T-cell receptor beta chain variable domain 2.1. From this structure and a model of the wild-type complex, we show that TSST-1 engages TCR ligands in a markedly different way than do other SAGs. We provide a structural basis for the high TCR specificity of TSST-1 and present a model of the TSST-1-dependent MHC-SAG-TCR T-cell signaling complex that is structurally and energetically unique relative to those formed by other SAGs. Our data also suggest that protein plasticity plays an exceptionally significant role in this affinity maturation process that results in more than a 3000-fold increase in affinity.

Indexed as

Models, MolecularBacterial ToxinsCrystallographyEnterotoxinsEpitopesHumansModels, BiologicalProtein BindingReceptors, Antigen, T-Cell, alpha-betaSignal TransductionSuperantigensSurface Plasmon ResonanceT-Cell Antigen Receptor SpecificityBacterial Toxinsenterotoxin F, StaphylococcalEnterotoxinsEpitopesReceptors, Antigen, T-Cell, alpha-betaSuperantigens

Identifiers

PMID17268555
PMCPMC1852840
OpenAlexW2143157762

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.