Evidence map›Paper›PMID 28002483›Full record

ArticlePloS one2016

Physical Characteristics of a Citrullinated Pro-Filaggrin Epitope Recognized by Anti-Citrullinated Protein Antibodies in Rheumatoid Arthritis Sera.

Nicole Hartwig Trier, Bettina Eide Holm, Ole Slot, Henning Locht, Hanne Lindegaard, Anders Svendsen, Gunnar Houen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Antibody Cross-Reactivity in Auto-Immune Diseases.International journal of molecular sciences · 2023
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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 5 institutions in 1 country.

Nicole Hartwig TrierDepartment of Autoimmunology and Biomarkers, Statens Serum Institut, Artillerivej, Copenhagen S, Denmark.
Bettina Eide HolmDepartment of Autoimmunology and Biomarkers, Statens Serum Institut, Artillerivej, Copenhagen S, Denmark.
Ole SlotDepartment of Rheumatology, Glostrup Hospital, Nordre Ringvej, Glostrup, Denmark.
Henning LochtDepartment of Rheumatology, Frederiksberg Hospital, Nordre Fasanvej, Frederiksberg, Denmark.
Hanne LindegaardDepartment of Rheumatology, Odense University Hospital, Søndre Boulevard, Odense C, Denmark.
Anders SvendsenDepartment of Epidemiology, Biostatistics and Bio-demography, Institute of Public Health, University of Southern Denmark, Campusvej, Odense M, Denmark.
Gunnar HouenDepartment of Autoimmunology and Biomarkers, Statens Serum Institut, Artillerivej, Copenhagen S, Denmark.
Statens Serum Institut · DKFrederiksberg Hospital · DKGlostrup Hospital · DKOdense University Hospital · DKUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rheumatoid arthritis (RA) is an autoimmune disease of complex etiology. A characteristic feature of a subset of RA is the presence of anti-citrullinated protein antibodies (ACPA), which correlate with a progressive disease course. In this study, we employed streptavidin capture enzyme-linked immunosorbent assay to analyze ACPA reactivity. Using the pro-filaggrin peptide HQCHQEST-Cit-GRSRGRCGRSGS, as template, we analyzed the reactivity of RA sera and healthy donor sera to various peptides in order to determine the physical characteristics of the citrullinated pro-filaggrin epitope and to examine whether biotin labelling influence antibody recognition. The full-length cyclic pro-filaggrin peptide and a linear form with a N-terminal biotin, was recognized to the same level, whereas, a notable difference in ACPA reactivity to the linear peptides with a C-terminal biotin was found, probably due to steric hindrance. Screening of linear and cyclic truncated peptides, revealed that small cyclic peptides containing 10-12 amino acids are favored over the linear. Moreover, the charged amino acids C-terminal to citrulline were found to be essential for antibody reactivity, most important was the charged amino acid in position 4 C-terminal to citrulline. Collectively, peptide structure, length, the presence of charged amino acids and biotin labelling markedly influence antibody reactivity. In relation to the clinical diagnostics of ACPA, these findings may reflect the differences in diagnostic assays used for detection of ACPA, which relates to differences in sensitivity and specificity dependent on the assay applied.

Indexed as

Amino Acid SequenceArthritis, RheumatoidAutoantibodiesBiotinCase-Control StudiesCitrullineCross ReactionsEnzyme-Linked Immunosorbent AssayEpitopesFilaggrin ProteinsHumansIntermediate Filament ProteinsPeptidesPeptides, CyclicAutoantibodiesBiotinCitrullineEpitopesFilaggrin ProteinsFLG protein, humanIntermediate Filament ProteinsPeptidesPeptides, Cyclic

Identifiers

PMID28002483
PMCPMC5176188
OpenAlexW2562348661

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.