Evidence map›Paper›PMID 15056382›Full record

ArticleImmunology2004

The interaction of streptococcal inhibitor of complement (SIC) and its proteolytic fragments with the human beta defensins.

Barbara A Fernie-King, David J Seilly, Peter J Lachmann

Open access · bronzeAbstract read
In one paragraph

Article in Immunology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
6.0field-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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Protein SIC Secreted fromFrontiers in immunology · 2018
    Observational
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Characterization of released polypeptides during an interferon-γ-dependent antibacterial response in airway epithelial cells.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2012
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Barbara A Fernie-KingMicrobial Immunology Group, Centre for Veterinary Science, University of Cambridge, Cambridge, UK. baf22@cam.ac.uk
David J Seilly
Peter J Lachmann
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcal inhibitor of complement (SIC) is a 31 kDa extracellular protein produced by a few highly virulent strains of Streptococcus pyogenes (in particular the M1 strain). It has been shown additionally to inhibit four further components of the mucosal innate response-lysozyme, secretory leucocyte proteinase inhibitor, human alpha-defensin 1 and the cathelicidin LL-37 which are all bactericidal against Group A Streptococci (GAS). We now show that SIC also inhibits variably the antibacterial action of hBD-1, -2 and -3. By enzyme-linked immunosorbent assay (ELISA), SIC binds strongly to hBD-2 and hBD-3, but not at all to hBD-1. Investigation of the antimicrobial action of beta-defensins hBD-1, -2 and -3 against GAS in two different buffer systems shows that both the killing efficiencies of all three defensins, and the binding of SIC to them, occurs more efficiently in 10 mm Tris buffer than in 10 mm phosphate. The lower ionic strength of the Tris buffer may underlie this effect. hBD-1 kills the M1 strain of GAS only in 10 mm Tris, but is able to kill an M6 (SIC negative) strain in 10 mm phosphate. The inhibition of hBD-3 by SIC is clearly of physiological relevance, that of hBD-2 is likely to be so, but the inhibition of hBD-1 occurs only at lower ionic strength than is likely to be encountered in vivo. Elastase digestion of SIC yields three major fragments of MW 3.843 kDa comprising residues 1-33 (fragment A); 10.369 kDa comprising residues 34-126 (fragment B); and MW 16.487 kDa, comprising residues 127-273 (fragment C). By ELISA, only fragment B binds to hBD-2 and hBD-3 and this may indicate the inhibitory portion of the SIC molecule.

Indexed as

Antimicrobial Cationic PeptidesBacterial Proteinsbeta-DefensinsCathelicidinsCulture MediaEnzyme-Linked Immunosorbent AssayHumansImmune TolerancePeptide FragmentsPhosphatesStreptococcus pyogenesTromethamineAntimicrobial Cationic PeptidesBacterial Proteinsbeta-DefensinsCathelicidinsCulture MediaPeptide FragmentsPhosphatesSIC protein, StreptococcusTromethamine

Identifiers

PMID15056382
PMCPMC1782441
OpenAlexW2086853751

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.