Evidence map›Paper›PMID 28751750›Full record

ArticleScientific reports2017

N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy.

Joost Te Riet, Ben Joosten, Inge Reinieren-Beeren, Carl G Figdor, Alessandra Cambi

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Posttranslational modifications optimize the ability of SARS-CoV-2 spike for effective interaction with host cell receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Establishing Rules for Self-Adhesion and Aggregation ofLangmuir : the ACS journal of surfaces and colloids · 2020
    Article
  8. Review
  9. Review
  10. What We Do Not Know about Fungal Cell Adhesion Molecules.Journal of fungi (Basel, Switzerland) · 2018
    Review
  11. 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

5 authors at 1 institution in 2 countries.

Joost Te RietDepartment of Tumor Immunology, Radboud Institute for Medical Life Sciences, Radboud University Medical Center, Grooteplein Zuid 26-28, 6525 GA, Nijmegen, The Netherlands.ORCID 0000-0002-9093-010X
Ben JoostenDepartment of Cell Biology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Geert Grooteplein Zuid 26-28, 6525 GA, Nijmegen, The Netherlands.
Inge Reinieren-BeerenDepartment of Tumor Immunology, Radboud Institute for Medical Life Sciences, Radboud University Medical Center, Grooteplein Zuid 26-28, 6525 GA, Nijmegen, The Netherlands.
Carl G FigdorDepartment of Tumor Immunology, Radboud Institute for Medical Life Sciences, Radboud University Medical Center, Grooteplein Zuid 26-28, 6525 GA, Nijmegen, The Netherlands. carl.figdor@radboudumc.nl.
Alessandra CambiDepartment of Cell Biology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Geert Grooteplein Zuid 26-28, 6525 GA, Nijmegen, The Netherlands. alessandra.cambi@radboudumc.nl.ORCID 0000-0003-1597-1582
Radboud University Nijmegen · NL

Funding

European Research Council 269019
6 · The paper itself

Abstract

Glycan-protein lateral interactions have gained increased attention as important modulators of receptor function, by regulating surface residence time and endocytosis of membrane glycoproteins. The pathogen-recognition receptor DC-SIGN is highly expressed at the membrane of antigen-presenting dendritic cells, where it is organized in nanoclusters and binds to different viruses, bacteria and fungi. We recently demonstrated that DC-SIGN N-glycans spatially restrict receptor diffusion within the plasma membrane, favoring its internalization through clathrin-coated pits. Here, we investigated the involvement of the N-glycans of DC-SIGN expressing cells on pathogen binding strengthening when interacting with Candida fungal cells by using atomic force microscope (AFM)-assisted single cell-pathogen adhesion measurements. The use of DC-SIGN mutants lacking the N-glycans as well as blocking glycan-mediated lateral interactions strongly impaired cell stiffening during pathogen binding. Our findings demonstrate for the first time the direct involvement of the cell membrane glycans in strengthening cell-pathogen interactions. This study, therefore, puts forward a possible role for the glycocalyx as extracellular cytoskeleton contributing, possibly in connection with the intracellular actin cytoskeleton, to optimize strengthening of cell-pathogen interactions in the presence of mechanical forces.

Indexed as

Host-Pathogen InteractionsAnimalsBinding SitesBiomechanical PhenomenaCandida albicansCell AdhesionCell Adhesion MoleculesCHO CellsCricetulusDC-Specific ICAM-3 Grabbing NonintegrinDendritic CellsGene ExpressionGlycocalyxHumansLectins, C-TypeMicroscopy, Atomic ForceCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinLectins, C-TypePolysaccharidesReceptors, Cell Surface

Identifiers

PMID28751750
PMCPMC5532264
OpenAlexW2736770530

What OpenQuestion holds

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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.