Evidence map›Paper›PMID 22399010›Full record

ArticleJournal of innate immunity2012

L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo.

Qin Pan, Haidan Chen, Feng Wang, Victor Tunje Jeza, Wei Hou, Yinglan Zhao, Tian Xiang, Ying Zhu, Yuchi Endo, Teizo Fujita and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of innate immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. The Role of Ficolins in Lung Injury.Journal of innate immunity · 2024
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. The Role of Glycosylation in Infectious Diseases.Advances in experimental medicine and biology · 2021
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

11 authors at 3 institutions in 2 countries.

Qin PanState Key Laboratory of Virology, Department of Immunology and Hubei Province, Key Laboratory of Allergy and Immune-Related Diseases, Wuhan University School of Medicine, Wuhan, PR China.
Haidan Chen
Feng Wang
Victor Tunje Jeza
Wei Hou
Yinglan Zhao
Tian Xiang
Ying Zhu
Yuchi Endo
Teizo Fujita
Xiao-Lian Zhang
State Key Laboratory of VirologyFukushima Medical University · JPWuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-ficolin, one of the complement lectins found in human serum, is a novel pattern recognition molecule that can specifically bind to microbial carbohydrates, thereby activating the lectin complement pathway and mounting a protective innate immune response. However, little is known about the role of L-ficolin during viral infections in vivo. In the present study, we used a mouse model of influenza A virus infection to demonstrate that the administration of exogenous L-ficolin or ficolin A (FCNA - an L-ficolin-like molecule in the mouse) is protective against the virus. Furthermore, FCNA-null mice have a greatly increased susceptibility to infection with the influenza A virus. Moreover, we found recombinant human L-ficolin inhibited influenza A virus entry into Madin-Darby canine kidney cells. More importantly, L-ficolin can recognize and bind hemagglutinin (HA) and neuraminidase (NA) glycoproteins and different subtypes of influenza A virus, and these interactions can be competitively inhibited by N-acetyl-D-glucosamine. In addition, the binding of L-ficolin and FCNA may lead to the activation of the lectin complement pathway. To our knowledge, this is the first report demonstrating that L-ficolin can block influenza virus infections both in vitro and in vivo using FCNA-knockout mice, possibly by interacting with the carbohydrates of HA and NA. Therefore, these data may provide new immunotherapeutic strategies based on the innate immune molecule L-ficolin against the influenza A virus.

Indexed as

Virus InternalizationAcetylglucosamineAnimalsCell LineComplement Pathway, Mannose-Binding LectinDisease Models, AnimalFicolinsHemagglutininsHumansInfluenza A virusLectinsMaleMiceMice, Inbred BALB CMice, Inbred C57BLMice, KnockoutAcetylglucosamineFicolinsHemagglutininsLectinsNeuraminidase

Identifiers

PMID22399010
PMCPMC6741490
OpenAlexW2087571895

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.