Evidence map›Paper›PMID 17244159›Full record

ArticleImmunology2007

Studies on the interactions between C-reactive protein and complement proteins.

Adrienn Bíró, Zita Rovó, Diana Papp, László Cervenak, Lilian Varga, George Füst, Nicole M Thielens, Gérard J Arlaud, Zoltán Prohászka

Open access · greenAbstract read
In one paragraph

Article in Immunology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 4% 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

66 citing papers in PubMed, 1 synthesis or guideline pooled it, 125 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Immunity and Coagulation in COVID-19.International journal of molecular sciences · 2024
    Review
  11. Structural basis for surface activation of the classical complement cascade by the short pentraxin C-reactive protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. The Role of Anti-mCRP Autoantibodies in Lupus Nephritis.Kidney diseases (Basel, Switzerland) · 2023
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

6 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 2 countries.

Adrienn Bíró3rd Department of Medicine, Semmelweis University, Budapest, Hungary. adrienn_biro@yahoo.com
Zita Rovó
Diana Papp
László Cervenak
Lilian Varga
George Füst
Nicole M Thielens
Gérard J Arlaud
Zoltán Prohászka
Semmelweis University · HUHungarian Academy of Sciences · HUUniversité Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several studies have investigated the interactions between C-reactive protein (CRP) and various complement proteins but none of them took into consideration the different structural forms of CRP. The aim of our study was to investigate whether the different antigenic forms of CRP are able to bind C1q, to trigger activation of the C1 complex and to study the ability of the various CRP forms to bind complement factor H (FH) and C4b-binding protein (C4BP). Interactions between various CRP forms and complement proteins were analysed in enzyme-linked immunosorbent assay and surface plasmon resonance tests and activation of the C1 complex was followed in a reconstituted system using purified C1q, C1r and C1s in the presence of C1-INH. Native, ligand-unbound CRP activated the classical pathway weakly. After binding to phosphocholine, native CRP bound C1q and significantly activated C1. Native CRP complexed to phosphocholine did not bind the complement regulatory proteins FH and C4BP. After disruption of the pentameric structure of CRP, as achieved by urea-treatment or by site-directed mutagenesis, C1q binding and C1 activation further increased and the ability of CRP to bind complement regulatory proteins was revealed. C1q binds to CRP through its globular head domain. The binding sites on CRP for FH and C4BP seemed to be different from that of C1q. In conclusion, in parallel with the increase in the C1-activating ability of different CRP structural variants, the affinity for complement regulatory proteins also increased, providing the biological basis for limitation of excess complement activation.

Indexed as

Complement ActivationComplement C1qComplement C4b-Binding ProteinComplement Factor HComplement Pathway, ClassicalComplement System ProteinsC-Reactive ProteinEnzyme-Linked Immunosorbent AssayHumansRecombinant ProteinsStructure-Activity RelationshipComplement C1qComplement C4b-Binding ProteinComplement Factor HComplement System ProteinsC-Reactive ProteinRecombinant Proteins

Identifiers

PMID17244159
PMCPMC2265924
OpenAlexW2043835217

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.