Evidence map›Paper›PMID 30445439›Full record

ArticlePathogens and disease2018

Listeriolysin O-dependent host surfaceome remodeling modulates Listeria monocytogenes invasion.

Andreas Kühbacher, Karel Novy, Juan J Quereda, Martin Sachse, Maryse Moya-Nilges, Bernd Wollscheid, Pascale Cossart, Javier Pizarro-Cerdá

Open access · hybridAbstract read
In one paragraph

Article in Pathogens and disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Frontiers in microbiology · 2021
    Article
  7. 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 2 countries.

Andreas KühbacherInstitut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France.
Karel NovyInstitute of Molecular Systems Biology and Department of Health Sciences and Technology, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.
Juan J QueredaInstitut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France.
Martin SachseInstitut Pasteur, UTechS Ultrastructural BioImaging, Paris F-75015, France.
Maryse Moya-NilgesInstitut Pasteur, UTechS Ultrastructural BioImaging, Paris F-75015, France.
Bernd WollscheidInstitute of Molecular Systems Biology and Department of Health Sciences and Technology, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.
Pascale CossartInstitut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France.
Javier Pizarro-CerdáInstitut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France.
Inserm · FRInstitut Pasteur · FRETH Zurich · CH

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Listeria monocytogenes is a pathogenic bacterium that invades epithelial cells by activating host signaling cascades, which promote bacterial engulfment within a phagosome. The pore-forming toxin listeriolysin O (LLO), which is required for bacteria phagosomal escape, has also been associated with the activation of several signaling pathways when secreted by extracellular bacteria, including Ca2+ influx and promotion of L. monocytogenes entry. Quantitative host surfaceome analysis revealed significant quantitative remodeling of a defined set of cell surface glycoproteins upon LLO treatment, including a subset previously identified to play a role in the L. monocytogenes infection process. Our data further shows that the lysosomal-associated membrane proteins LAMP-1 and LAMP-2 are translocated to the cellular surface and those LLO-induced Ca2+ fluxes are required to trigger the surface relocalization of LAMP-1. Finally, we identify late endosomes/lysosomes as the major donor compartments of LAMP-1 upon LLO treatment and by perturbing their function, we suggest that these organelles participate in L. monocytogenes invasion.

Indexed as

EndocytosisHost-Pathogen InteractionsBacterial ToxinsEndosomesEpithelial CellsHeat-Shock ProteinsHeLa CellsHemolysin ProteinsHumansListeria monocytogenesLysosomesMembrane ProteinsProteomeBacterial ToxinsHeat-Shock ProteinsHemolysin ProteinshlyA protein, Listeria monocytogenesMembrane ProteinsProteome

Identifiers

PMID30445439
PMCPMC6282100
OpenAlexW2900911847

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.