Evidence map›Paper›PMID 21134964›Full record

ArticleInfection and immunity2011

Native properdin binds to Chlamydia pneumoniae and promotes complement activation.

Claudio Cortes, V P Ferreira, Michael K Pangburn

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-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

33 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
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  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. An Ancient Molecular Arms Race:Frontiers in immunology · 2020
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Human Properdin Modulates Macrophage:Frontiers in immunology · 2018
    Article
  17. Review
  18. Article
  19. Properdin binding to complement activating surfaces depends on initial C3b deposition.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Frontiers in microbiology · 2017
    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 2 institutions in 1 country.

Claudio CortesDepartment of Biochemistry, Center for Biomedical Research, University of Texas Health Science Center, Tyler, Texas 75708, USA. claudio.cortes@utoledo.edu
V P Ferreira
Michael K Pangburn
University of Toledo Medical Center · USThe University of Texas Health Science Center at Tyler · US

Funding

REGULATION OF COMPLEMENT BY MEMBRANE PROTEINSR01DK035081 · NIDDK · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI PANGBURN, MICHAEL K. · 1986 to 2011
$2.5M
The role of complement proteins in cardiovascular diseaseP30HL101317 · NHLBI · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI TAKASHIMA, AKIRA · 2009 to 2010
$1.2M
ACTIVATION OF THE ALTERNATIVE PATHWAY OF COMPLEMENTR37DK035081 · NIDDK · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI PANGBURN, MICHAEL K. · 1993 to 2000
$206k
NHLBI NIH HHS 1P30HL101317-01NHLBI NIH HHS P30 HL101317NIDDK NIH HHS DK-35081NIDDK NIH HHS R01 DK035081NIDDK NIH HHS R37 DK035081
6 · The paper itself

Abstract

Activation of complement represents one means of natural resistance to infection from a wide variety of potential pathogens. Recently, properdin, a positive regulator of the alternative pathway of complement, has been shown to bind to surfaces and promote complement activation. Here we studied whether properdin-mediated complement activation occurs on the surface of Chlamydia pneumoniae, an obligate intracellular Gram-negative bacterium that causes 10 to 20% of community-acquired pneumonia. We have determined for the first time that the physiological P₂, P₃, and P₄ forms of human properdin bind to the surface of Chlamydia pneumoniae directly. The binding of these physiological forms accelerates complement activation on the Chlamydia pneumoniae surface, as measured by C3b and C9 deposition. Finally, properdin-depleted serum could not control Chlamydia pneumoniae infection of HEp-2 cells compared with normal human serum. However, after addition of native properdin, the properdin-depleted serum recovered the ability to control the infection. Altogether, our data suggest that properdin is a pattern recognition molecule that plays a role in resistance to Chlamydia infection.

Indexed as

Antibodies, BacterialCell LineChlamydophila InfectionsChlamydophila pneumoniaeComplement ActivationComplement C9HumansProperdinAntibodies, BacterialComplement C9Properdin

Identifiers

PMID21134964
PMCPMC3028849
OpenAlexW1988094014

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.