Evidence map›Paper›PMID 35388026›Full record

ArticleScientific reports2022

Low molecular weight polysialic acid binds to properdin and reduces the activity of the alternative complement pathway.

Anahita Shahraz, Yuchen Lin, Joshua Mbroh, Jonas Winkler, Huan Liao, Marie Lackmann, Annemarie Bungartz, Peter F Zipfel, Christine Skerka, Harald Neumann

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2022. 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
0.9field-weighted citation impact, top 28% 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, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  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

10 authors at 4 institutions in 1 country.

Anahita Shahraz *Neural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Yuchen Lin *Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Jena, Germany.
Joshua MbrohNeural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Jonas WinklerNeural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Huan LiaoNeural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Marie LackmannNeural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Annemarie BungartzNeural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Peter F ZipfelDepartment of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Jena, Germany.
Christine Skerka *Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Jena, Germany.
Harald Neumann *Neural Regeneration Unit, Institute of Reconstructive Neurobiology, Medical Faculty and University Hospital of Bonn, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany. harald.neumann@uni-bonn.de.
University of Bonn · DEUniversity Hospital Bonn · DELeibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DEFriedrich Schiller University Jena · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialic acids as the terminal caps of the cellular glycocalyx play an essential role in self-recognition and were shown to modulate complement processes via interaction between α2,3-linked sialic acids and complement factor H. Previously, it was suggested that low molecular weight α2,8-linked polysialic acid (polySia avDP20) interferes with complement activation, but the exact molecular mechanism is still unclear. Here, we show that soluble polySia avDP20 (molecular weight of ~ 6 kDa) reduced the binding of serum-derived alternative pathway complement activator properdin to the cell surface of lesioned Hepa-1c1c7 and PC-12 neuroblastoma cells. Furthermore, polySia avDP20 added to human serum blocked the alternative complement pathway triggered by plate-bound lipopolysaccharides. Interestingly, no inhibitory effect was observed with monosialic acid or oligosialic acid with a chain length of DP3 and DP5. In addition, polySia avDP20 directly bound properdin, but not complement factor H. These data show that soluble polySia avDP20 binds properdin and reduces the alternative complement pathway activity. Results strengthen the previously described concept of self-recognition of sialylation as check-point control of complement activation in innate immunity.

Indexed as

Complement Pathway, AlternativeProperdinHumansMolecular WeightSialic Acidspolysialic acidProperdinSialic Acids

Identifiers

PMID35388026
PMCPMC8987038
OpenAlexW4223568180

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.