Evidence map›Paper›PMID 7533788›Full record

ArticleThe Journal of clinical investigation1995

Epstein-Barr virus-induced autoimmune responses. I. Immunoglobulin M autoantibodies to proteins mimicking and not mimicking Epstein-Barr virus nuclear antigen-1.

J H Vaughan, J R Valbracht, M D Nguyen, H H Handley, R S Smith, K Patrick, G H Rhodes

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Autoimmunity and infection in Sjögren's syndrome.Current opinion in rheumatology · 2013
    Review
  10. Article
  11. Article
  12. Endogenous retroviral pathogenesis in lupus.Current opinion in rheumatology · 2010
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Epitope spreading.Current opinion in immunology · 1996
    Review
  18. Article
  19. Article
  20. The Epstein-Barr virus in autoimmunity.Springer seminars in immunopathology · 1995
    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.

J H VaughanDepartment of Medicine, University of California, San Diego, La Jolla 92093-0663.
J R Valbracht
M D Nguyen
H H Handley
R S Smith
K Patrick
G H Rhodes
Johnson & Johnson (United States) · USUniversity of California San Diego · US

Funding

THE EPSTEIN-BARR VIRUS AND AUTOIMMUNE DISEASER01AR021175 · NIAMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI VAUGHAN, JOHN H · 1986 to 1992
–
NIAMS NIH HHS AR21175
6 · The paper itself

Abstract

In previous studies of infectious mononucleosis, we found IgM autoantibodies which react with hematopoietic cell antigens. Many of these were inhibited by synthetic glycine/alanine peptides representing the glycine/alanine repeat of Epstein-Barr virus nuclear antigen-1. We have cloned and expressed fragments of genes encoding two of these autoantigens. One gene (p542) encodes a protein containing a glycine-rich 28-mer, which is its chief autoantigenic epitope and which represents a newly identified class of evolutionarily conserved autoepitopes. The other gene (p554) encodes a protein that is not demonstrably cross-reactive with Epstein-Barr virus nuclear antigen-1 or with any other EBV protein, but forms complexes with other proteins. Immunoaffinity-purified anti-p542 and anti-p554 have relatively high binding affinities, as evidenced by inhibition at 10(6)-10(8) M-1, and neither autoantibody showed polyreactivity with other common antigens. The data thus suggest that neither autoantibody is simply an expression of polyclonal B cell activation. We conclude that the two autoantigens stimulate autoantibody synthesis by different mechanisms. One autoantigen shares homology to a viral protein which generates cross-reacting antibodies to the autoantigenic epitope. The other has no recognizable cross-reaction with the infecting pathogen and may become immunogenic through complexing with other proteins.

Indexed as

Amino Acid SequenceAntibody SpecificityAntigens, ViralAutoantibodiesAutoantigensCells, CulturedDNA-Binding ProteinsEpitopesEpstein-Barr Virus Nuclear AntigensHumansImmunoglobulin MInfectious MononucleosisLeukocytesMolecular MimicryMolecular Sequence DataRecombinant Fusion ProteinsAntigens, ViralAutoantibodiesAutoantigensDNA-Binding ProteinsEpitopesEpstein-Barr Virus Nuclear AntigensImmunoglobulin MRecombinant Fusion Proteins

Identifiers

PMID7533788
PMCPMC441470
OpenAlexW1987576902

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.