Evidence map›Paper›PMID 10051632›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Crossreactive recognition of viral, self, and bacterial peptide ligands by human class I-restricted cytotoxic T lymphocyte clonotypes: implications for molecular mimicry in autoimmune disease.

I S Misko, S M Cross, R Khanna, S L Elliott, C Schmidt, S J Pye, S L Silins

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Observational
  3. Article
  4. Article
  5. Article
  6. Review
  7. Mechanism of cellular rejection in transplantation.Pediatric nephrology (Berlin, Germany) · 2010
    Review
  8. Inducing efficient cross-priming using antigen-coated yeast particles.Journal of immunotherapy (Hagerstown, Md. : 1997) · 2008
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The immunology of Epstein-Barr virus infection.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2001
    Review
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

7 authors at 2 institutions in 1 country.

I S MiskoEpstein-Barr Virus Unit, Queensland Institute of Medical Research and Joint Experimental Oncology, University of Queensland, Brisbane, 4029, Australia. ihorM@qimr.edu.au
S M Cross
R Khanna
S L Elliott
C Schmidt
S J Pye
S L Silins
QIMR Berghofer Medical Research Institute · AUUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The immunodominant, CD8(+) cytotoxic T lymphocyte (CTL) response to the HLA-B8-restricted peptide, RAKFKQLL, located in the Epstein-Barr virus immediate-early antigen, BZLF1, is characterized by a diverse T cell receptor (TCR) repertoire. Here, we show that this diversity can be partitioned on the basis of crossreactive cytotoxicity patterns involving the recognition of a self peptide-RSKFRQIV-located in a serine/threonine kinase and a bacterial peptide-RRKYKQII-located in Staphylococcus aureus replication initiation protein. Thus CTL clones that recognized the viral, self, and bacterial peptides expressed a highly restricted alphabeta TCR phenotype. The CTL clones that recognized viral and self peptides were more oligoclonal, whereas clones that strictly recognized the viral peptide displayed a diverse TCR profile. Interestingly, the self and bacterial peptides equally were substantially less effective than the cognate viral peptide in sensitizing target cell lysis, and also resulted only in a weak reactivation of memory CTLs in limiting dilution assays, whereas the cognate peptide was highly immunogenic. The described crossreactions show that human antiviral, CD8(+) CTL responses can be shaped by peptide ligands derived from autoantigens and environmental bacterial antigens, thereby providing a firm structural basis for molecular mimicry involving class I-restricted CTLs in the pathogenesis of autoimmune disease.

Indexed as

Molecular MimicryAmino Acid SequenceAutoimmune DiseasesBacterial ProteinsBase SequenceCytotoxicity, ImmunologicDNA-Binding ProteinsDNA HelicasesGene Rearrangement, alpha-Chain T-Cell Antigen ReceptorGene Rearrangement, beta-Chain T-Cell Antigen ReceptorHerpesvirus 4, HumanHistocompatibility Antigens Class IHLA-B8 AntigenHumansMolecular Sequence DataPeptide FragmentsBacterial ProteinsBZLF1 protein, Herpesvirus 4, HumanDNA-Binding ProteinsDNA HelicasesHistocompatibility Antigens Class IHLA-B8 AntigenPeptide FragmentsReceptors, Antigen, T-Cell, alpha-betareplication initiator proteinTrans-ActivatorsViral Proteins

Identifiers

PMID10051632
PMCPMC26774
OpenAlexW1990236642

What OpenQuestion holds

Texttitle and abstract
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.