Evidence map›Paper›PMID 25789808›Full record

ArticlePloS one2015

Pathogenic E. coli exploits SslE mucinase activity to translocate through the mucosal barrier and get access to host cells.

Maria Valeri, Silvia Rossi Paccani, Magdalena Kasendra, Barbara Nesta, Laura Serino, Mariagrazia Pizza, Marco Soriani

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 59 citations in OpenAlex.

  1. Trial
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  7. Review
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  9. Article
  10. Glycocalyx crowding with mucin mimetics strengthens binding of soluble and virus-associated lectins to host cell glycan receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Comparative Pathogenomics ofInfection and immunity · 2021
    Article
  13. Review
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  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Pic Protein From EnteroaggregativeFrontiers in immunology · 2020
    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

7 authors at 2 institutions in 2 countries.

Maria ValeriNovartis Vaccines and Diagnostics S.r.l., Via Fiorentina 1, Siena, Italy.
Silvia Rossi PaccaniNovartis Vaccines and Diagnostics S.r.l., Via Fiorentina 1, Siena, Italy.
Magdalena KasendraChildren's Hospital Boston, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, United States of America.
Barbara NestaNovartis Vaccines and Diagnostics S.r.l., Via Fiorentina 1, Siena, Italy.
Laura SerinoNovartis Vaccines and Diagnostics S.r.l., Via Fiorentina 1, Siena, Italy.
Mariagrazia PizzaNovartis Vaccines and Diagnostics S.r.l., Via Fiorentina 1, Siena, Italy.
Marco SorianiNovartis Vaccines and Diagnostics S.r.l., Via Fiorentina 1, Siena, Italy.
Novartis (Italy) · ITHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SslE is a zinc-metalloprotease involved in the degradation of mucin substrates and recently proposed as a potential vaccine candidate against pathogenic E. coli. In this paper, by exploiting a human in vitro model of mucus-secreting cells, we demonstrated that bacteria expressing SslE have a metabolic benefit which results in an increased growth rate postulating the importance of this antigen in enhancing E. coli fitness. We also observed that SslE expression facilitates E. coli penetration of the mucus favouring bacteria adhesion to host cells. Moreover, we found that SslE-mediated opening of the mucosae contributed to the activation of pro-inflammatory events. Indeed, intestinal cells infected with SslE-secreting bacteria showed an increased production of IL-8 contributing to neutrophil recruitment. The results presented in this paper conclusively designate SslE as an important colonization factor favouring E. coli access to both metabolic substrates and target cells.

Indexed as

Escherichia coliEscherichia coli ProteinsHumansIntestinal MucosaPolysaccharide-LyasesVirulenceVirulence FactorsEscherichia coli Proteinshyaluronate lyasePolysaccharide-LyasesSslE protein, E coliVirulence Factors

Identifiers

PMID25789808
PMCPMC4366376
OpenAlexW2032331568

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.