Evidence map›Paper›PMID 15699071›Full record

ArticleThe Journal of experimental medicine2005

The adaptor molecules LAT and SLP-76 are specifically targeted by Yersinia to inhibit T cell activation.

Christiane Gerke, Stanley Falkow, Yueh-hsiu Chien

Open access · greenAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  9. Unraveling neutrophil-F1000Research · 2019
    Review
  10. European journal of microbiology & immunology · 2018
    Article
  11. Article
  12. Review
  13. Injection of T3SS effectors not resulting in invasion is the main targeting mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. A Novel Function for theFrontiers in immunology · 2017
    Article
  16. Article
  17. Yersinia type III effectors perturb host innate immune responses.World journal of biological chemistry · 2016
    Review
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Christiane GerkeDepartment of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Stanley Falkow
Yueh-hsiu Chien
Stanford University · US

Funding

Proteomics/GenomicsP30DK056339 · NIDDK · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 2001 to 2010
$10.4M
NIDDK NIH HHS DK56339NIDDK NIH HHS P30 DK056339
6 · The paper itself

Abstract

T cell responses are critical to the survival of Yersinia-infected animals. Yersinia have the ability to directly suppress T lymphocyte activation through the virulence factor YopH, a tyrosine phosphatase. Using single cell video microscopy and FACS analysis, here we show that even an average of one Yersinia per T cell is sufficient to inhibit or alter T cell responses. This efficient inhibition is traced to specific targeting by YopH of the adaptor proteins, linker for activation of T cells (LAT) and SH2-domain-containing leukocyte protein of 76 kD (SLP-76), which are crucial for T cell antigen receptor (TCR) signaling. A catalytically inactive YopH translocated via the type III secretory pathway from the bacteria into T cells primarily binds to LAT and SLP-76. Furthermore, among the proteins of the TCR signaling pathway, the tyrosine phosphorylation levels of LAT and SLP-76 are the most affected in T cells exposed to low numbers of Yersinia pseudotuberculosis. This is the first example showing that a pathogen targets these adaptor proteins in the TCR signaling pathway, suggesting a novel mechanism by which pathogens may efficiently alter T cell-mediated immune responses.

Indexed as

Lymphocyte ActivationAdaptor Proteins, Signal TransducingAnimalsBacterial Outer Membrane ProteinsCalciumHumansJurkat CellsMembrane ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Tyrosine PhosphatasesSignal TransductionT-LymphocytesTyrosineYersinia InfectionsAdaptor Proteins, Signal TransducingBacterial Outer Membrane ProteinsCalciumLAT protein, humanMembrane ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsProtein Tyrosine PhosphatasesSLP-76 signal Transducing adaptor proteinsTyrosineyopH protein, Yersinia

Identifiers

PMID15699071
PMCPMC2213036
OpenAlexW2105438508

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.