Evidence map›Paper›PMID 9449712›Full record

ArticleThe Journal of experimental medicine1998

Mycoplasma superantigen is a CDR3-dependent ligand for the T cell antigen receptor.

A S Hodtsev, Y Choi, E Spanopoulou, D N Posnett

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

18 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. A general platform for targeting MHC-II antigens via a single loop.bioRxiv : the preprint server for biology · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. A single point mutation changes the crystallization behavior of Mycoplasma arthritidis-derived mitogen.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006
    Article
  9. Crystal structures of T cell receptor (beta) chains related to rheumatoid arthritis.Protein science : a publication of the Protein Society · 2005
    Article
  10. Article
  11. Article
  12. Bacterial superantigens.Clinical and experimental immunology · 2003
    Review
  13. T cell Vbeta repertoires in childhood vasculitides.Clinical and experimental immunology · 2003
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

4 authors at 3 institutions in 1 country.

A S HodtsevRuttenberg Cancer Center, Mount Sinai School of Medicine, New York 10029, USA. andrew_hodtsev@smtplink.mssm.edu
Y Choi
E Spanopoulou
D N Posnett
Howard Hughes Medical Institute · USCornell University · USRockefeller University · US

Funding

HIV-1-ASSOCIATED SUPERANTIGENR01AI033322 · NIAID · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI POSNETT, DAVID N · 1993 to 2001
$905k
MOLECULAR SITES REACTIVE WITH A SUPERANTIGEN (MAM)R01AI031140 · NIAID · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI POSNETT, DAVID N · 1991 to 1995
–
RETROVIRUS-ENCODED SUPERANTIGENSR29CA059751 · NCI · ROCKEFELLER UNIVERSITY · PI CHOI, YONGWON · 1993 to 1997
–
NCI NIH HHS CA-59751NIAID NIH HHS AI-31140NIAID NIH HHS AI-33322
6 · The paper itself

Abstract

Superantigens are defined as proteins that activate a large number of T cells through interaction with the Vbeta region of the T cell antigen receptor (TCR). Here we demonstrate that the superantigen produced by Mycoplasma arthritidis (MAM), unlike six bacterial superantigens tested, interacts not only with the Vbeta region but also with the CDR3 (third complementarity-determining region) of TCR-beta. Although MAM shares typical features with other superantigens, direct interaction with CDR3-beta is a feature of nominal peptide antigens situated in the antigen groove of major histocompatibility complex (MHC) molecules rather than superantigens. During peptide recognition, Vbeta and Valpha domains of the TCR form contacts with MHC and the complex is stabilized by CDR3-peptide interactions. Similarly, recognition of MAM is Vbeta-dependent and is apparently stabilized by direct contacts with the CDR3-beta region. Thus, MAM represents a new type of ligand for TCR, distinct from both conventional peptide antigens and other known superantigens.

Indexed as

Antigens, BacterialArthritis, RheumatoidAutoimmunityBacterial ProteinsCD4-Positive T-LymphocytesClone CellsCloning, MolecularHumansLigandsMajor Histocompatibility ComplexMutagenesisMycoplasmaPeptidesReceptors, Antigen, T-CellSequence AlignmentSuperantigensAntigens, BacterialBacterial ProteinsLigandsPeptidesReceptors, Antigen, T-CellSuperantigens

Identifiers

PMID9449712
PMCPMC2212128
OpenAlexW1990341452

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.