Evidence map›Paper›PMID 24349316›Full record

ArticlePloS one2013

Human L-ficolin, a recognition molecule of the lectin activation pathway of complement, activates complement by binding to pneumolysin, the major toxin of Streptococcus pneumoniae.

Youssif M Ali, Hany I Kenawy, Adnan Muhammad, Robert B Sim, Peter W Andrew, Wilhelm J Schwaeble

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Collectins and Ficolins.Advances in experimental medicine and biology · 2025
    Review
  2. Article
  3. The Role of Ficolins in Lung Injury.Journal of innate immunity · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Role ofFrontiers in microbiology · 2017
    Review
  11. Review
  12. Article
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

6 authors at 2 institutions in 2 countries.

Youssif M AliDepartment of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom ; Department of Microbiology, Faculty of Pharmacy, Mansoura University, Mansoura, Egypt.
Hany I KenawyDepartment of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom ; Department of Microbiology, Faculty of Pharmacy, Mansoura University, Mansoura, Egypt.
Adnan MuhammadDepartment of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom.
Robert B SimDepartment of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom.
Peter W AndrewDepartment of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom.
Wilhelm J SchwaebleDepartment of Infection, Immunity and Inflammation, University of Leicester, Leicester, United Kingdom.
University of Leicester · GBMansoura University · EG

Funding

Medical Research Council G0801952
6 · The paper itself

Abstract

The complement system is an essential component of the immune response, providing a critical line of defense against different pathogens including S. pneumoniae. Complement is activated via three distinct pathways: the classical (CP), the alternative (AP) and the lectin pathway (LP). The role of Pneumolysin (PLY), a bacterial toxin released by S. pneumoniae, in triggering complement activation has been studied in vitro. Our results demonstrate that in both human and mouse sera complement was activated via the CP, initiated by direct binding of even non-specific IgM and IgG3 to PLY. Absence of CP activity in C1q(-/-) mouse serum completely abolished any C3 deposition. However, C1q depleted human serum strongly opsonized PLY through abundant deposition of C3 activation products, indicating that the LP may have a vital role in activating the human complement system on PLY. We identified that human L-ficolin is the critical LP recognition molecule that drives LP activation on PLY, while all of the murine LP recognition components fail to bind and activate complement on PLY. This work elucidates the detailed interactions between PLY and complement and shows for the first time a specific role of the LP in PLY-mediated complement activation in human serum.

Indexed as

Complement Pathway, Mannose-Binding LectinAdultBacterial ProteinsComplement ActivationComplement C1qComplement C3Complement System ProteinsFicolinsHumansLectinsProtein BindingRecombinant ProteinsStreptolysinsBacterial ProteinsComplement C1qComplement C3Complement System ProteinsFicolinsLectinsplY protein, Streptococcus pneumoniaeRecombinant ProteinsStreptolysins

Identifiers

PMID24349316
PMCPMC3861440
OpenAlexW1981839261

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.