Evidence map›Paper›PMID 27458147›Full record

ArticleScientific reports2016

Addition of lysophospholipids with large head groups to cells inhibits Shiga toxin binding.

Ieva Ailte, Anne Berit Dyve Lingelem, Simona Kavaliauskiene, Jonas Bergan, Audun Sverre Kvalvaag, Anne-Grethe Myrann, Tore Skotland, Kirsten Sandvig

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Examining the thermotropic properties of large circularized nanodiscs.Biochimica et biophysica acta. Biomembranes · 2025
    Article
  2. Nir2 crystal structures reveal a phosphatidic acid-sensing mechanism at ER-PM contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Molecular biology of the cell · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Verotoxin Receptor-Based Pathology and Therapies.Frontiers in cellular and infection microbiology · 2020
    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

8 authors at 3 institutions in 1 country.

Ieva AilteCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Anne Berit Dyve LingelemCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Simona KavaliauskieneCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Jonas BerganCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Audun Sverre KvalvaagCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Anne-Grethe MyrannCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Tore SkotlandCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Kirsten SandvigCentre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
University of Oslo · NOBorregaard (Norway) · NOOslo University Hospital · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shiga toxin (Stx), an AB5 toxin, binds specifically to the neutral glycosphingolipid Gb3 at the cell surface before being transported into cells. We here demonstrate that addition of conical lysophospholipids (LPLs) with large head groups inhibit Stx binding to cells whereas LPLs with small head groups do not. Lysophosphatidylinositol (LPI 18:0), the most efficient LPL with the largest head group, was selected for in-depth investigations to study how the binding of Stx is regulated. We show that the inhibition of Stx binding by LPI is reversible and possibly regulated by cholesterol since addition of methyl-β-cyclodextrin (mβCD) reversed the ability of LPI to inhibit binding. LPI-induced inhibition of Stx binding is independent of signalling and membrane turnover as it occurs in fixed cells as well as after depletion of cellular ATP. Furthermore, data obtained with fluorescent membrane dyes suggest that LPI treatment has a direct effect on plasma membrane lipid packing with shift towards a liquid disordered phase in the outer leaflet, while lysophosphoethanolamine (LPE), which has a small head group, does not. In conclusion, our data show that cellular treatment with conical LPLs with large head groups changes intrinsic properties of the plasma membrane and modulates Stx binding to Gb3.

Indexed as

beta-CyclodextrinsCell MembraneHeLa CellsHumansLysophospholipidsNeutral GlycosphingolipidsProtein BindingShiga Toxinbeta-Cyclodextrinsglycosphingolipid GalGb3Lysophospholipidsmethyl-beta-cyclodextrinNeutral GlycosphingolipidsShiga Toxin

Identifiers

PMID27458147
PMCPMC4960542
OpenAlexW2488698455

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.