Evidence map›Paper›PMID 25136128›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

A lipid zipper triggers bacterial invasion.

Thorsten Eierhoff, Björn Bastian, Roland Thuenauer, Josef Madl, Aymeric Audfray, Sahaja Aigal, Samuel Juillot, Gustaf E Rydell, Stefan Müller, Sophie de Bentzmann and 3 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
–field-weighted citation impact
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

63 citing papers in PubMed.

  1. Article
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  3. Article
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  6. Article
  7. Article
  8. The BacteriumBiomolecules · 2025
    Article
  9. Article
  10. Dual inhibitors ofChemical science · 2024
    Article
  11. Evidence for intracellularJournal of bacteriology · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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

13 authors.

Thorsten EierhoffFaculty of Biology, BIOSS Centre for Biological Signalling Studies, thorsten.eierhoff@bioss.uni-freiburg.de christian.fleck@wur.nl winfried.roemer@bioss.uni-freiburg.de.
Björn BastianCentre for Biological Systems Analysis, and.
Roland ThuenauerFaculty of Biology, BIOSS Centre for Biological Signalling Studies.
Josef MadlFaculty of Biology, BIOSS Centre for Biological Signalling Studies.
Aymeric AudfrayCentre de Recherches sur les Macromolécules Végétales, Université Grenoble Alpes and Centre National de la Recherche Scientifique, F38000 Grenoble, France;
Sahaja AigalFaculty of Biology, BIOSS Centre for Biological Signalling Studies, International Max Planck Research School for Molecular and Cellular Biology, Max Planck Institute of Immunobiology and Epigenetics, 79108 Freiburg, Germany;
Samuel JuillotFaculty of Biology, BIOSS Centre for Biological Signalling Studies, Spemann Graduate School of Biology and Medicine, Albert Ludwigs University Freiburg, 79104 Freiburg, Germany;
Gustaf E RydellDepartment of Infectious Diseases, Section for Clinical Virology, University of Gothenburg, S-413 46 Gothenburg, Sweden;
Stefan MüllerFaculty of Biology, BIOSS Centre for Biological Signalling Studies.
Sophie de BentzmannLaboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR7255 Centre National de la Recherche Scientifique and Aix Marseille University, Institut de Microbiologie de la Méditerranée, 13402 Marseille, France; and.
Anne ImbertyCentre de Recherches sur les Macromolécules Végétales, Université Grenoble Alpes and Centre National de la Recherche Scientifique, F38000 Grenoble, France;
Christian FleckCentre for Biological Systems Analysis, and Laboratory for Systems and Synthetic Biology, Wageningen University, 6703 HB, Wageningen, The Netherlands thorsten.eierhoff@bioss.uni-freiburg.de christian.fleck@wur.nl winfried.roemer@bioss.uni-freiburg.de.
Winfried RömerFaculty of Biology, BIOSS Centre for Biological Signalling Studies, Spemann Graduate School of Biology and Medicine, Albert Ludwigs University Freiburg, 79104 Freiburg, Germany; thorsten.eierhoff@bioss.uni-freiburg.de christian.fleck@wur.nl winfried.roemer@bioss.uni-freiburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosphingolipids are important structural constituents of cellular membranes. They are involved in the formation of nanodomains ("lipid rafts"), which serve as important signaling platforms. Invasive bacterial pathogens exploit these signaling domains to trigger actin polymerization for the bending of the plasma membrane and the engulfment of the bacterium--a key process in bacterial uptake. However, it is unknown whether glycosphingolipids directly take part in the membrane invagination process. Here, we demonstrate that a "lipid zipper," which is formed by the interaction between the bacterial surface lectin LecA and its cellular receptor, the glycosphingolipid Gb3, triggers plasma membrane bending during host cell invasion of the bacterium Pseudomonas aeruginosa. In vitro experiments with Gb3-containing giant unilamellar vesicles revealed that LecA/Gb3-mediated lipid zippering was sufficient to achieve complete membrane engulfment of the bacterium. In addition, theoretical modeling elucidated that the adhesion energy of the LecA-Gb3 interaction is adequate to drive the engulfment process. In cellulo experiments demonstrated that inhibition of the LecA/Gb3 lipid zipper by either lecA knockout, Gb3 depletion, or application of soluble sugars that interfere with LecA binding to Gb3 significantly lowered P. aeruginosa uptake by host cells. Of note, membrane engulfment of P. aeruginosa occurred independently of actin polymerization, thus corroborating that lipid zippering alone is sufficient for this crucial first step of bacterial host-cell entry. Our study sheds new light on the impact of glycosphingolipids in the cellular invasion of bacterial pathogens and provides a mechanistic explication of the initial uptake processes.

Indexed as

ActinsAdhesins, BacterialBacterial AdhesionCell MembraneEpithelial CellsGlycolipidsGlycosphingolipidsLipid BilayersMembrane MicrodomainsModels, BiologicalPseudomonas aeruginosaPseudomonas InfectionsSignal TransductionSphingolipidsActinsAdhesins, Bacterialglobotriaosyl lysosphingolipidGlycolipidsGlycosphingolipidsLecA protein, bacteriaLipid BilayersSphingolipidsglycolipidinfectionmembrane curvature

Identifiers

PMID25136128
PMCPMC4156737

What OpenQuestion holds

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Registered trials

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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.