Evidence map›Paper›PMID 30171791›Full record

ArticleCellular microbiology2019

An extracellular Leptospira interrogans leucine-rich repeat protein binds human E- and VE-cadherins.

Azad Eshghi, Robert A Gaultney, Patrick England, Sébastien Brûlé, Isabelle Miras, Hiromi Sato, Jenifer Coburn, Jacques Bellalou, Tara J Moriarty, Ahmed Haouz and 1 more

Open access · greenAbstract read
In one paragraph

Article in Cellular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Evolutionary insights into the emergence of virulentbioRxiv : the preprint server for biology · 2024
    Article
  8. Leucine-rich repeat proteins ofFrontiers in microbiology · 2024
    Article
  9. New insights into the putative role of leucine-rich repeat proteins ofFrontiers in cellular and infection microbiology · 2024
    Review
  10. Article
  11. Article
  12. Host Cell Binding Mediated byInternational journal of molecular sciences · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. A Review on Host-Frontiers in cellular and infection microbiology · 2021
    Review
  20. Unique Features of Tandem Repeats in Bacteria.Journal of bacteriology · 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

11 authors at 4 institutions in 3 countries.

Azad EshghiUnité de Biologie des Spirochètes, Institut Pasteur, Paris, France.ORCID 0000-0002-8641-273X
Robert A GaultneyUnité de Biologie des Spirochètes, Institut Pasteur, Paris, France.ORCID 0000-0001-9806-2434
Patrick EnglandPlate-forme de Biophysique Moléculaire, Institut Pasteur, CNRS-UMR 3528, Paris, France.
Sébastien BrûléPlate-forme de Biophysique Moléculaire, Institut Pasteur, CNRS-UMR 3528, Paris, France.
Isabelle MirasPlate-forme de Cristallographie, Institut Pasteur, CNRS-UMR 3528, Paris, France.
Hiromi SatoCenter for Infectious Disease Research, Department of Medicine (Division of Infectious Diseases), Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Jenifer CoburnCenter for Infectious Disease Research, Department of Medicine (Division of Infectious Diseases), Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Jacques BellalouPlate-forme de Protéines Recombinantes, Institut Pasteur, CNRS-UMR 3528, Paris, France.
Tara J MoriartyFaculty of Dentistry, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0002-1751-5145
Ahmed HaouzPlate-forme de Cristallographie, Institut Pasteur, CNRS-UMR 3528, Paris, France.
Mathieu PicardeauUnité de Biologie des Spirochètes, Institut Pasteur, Paris, France.
Centre National de la Recherche Scientifique · FRInstitut Pasteur · FRMedical College of Wisconsin · USUniversity of Toronto · CA

Funding

Leptospira interrogans Interactions with Endothelial CellsR01AI112920 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI COBURN, JENIFER L · 2014 to 2017
$1.5M
NIAID NIH HHS R01 AI112920
6 · The paper itself

Abstract

Pathogenic Leptospira bacteria are the causative agents of leptospirosis, a zoonotic disease affecting animals and humans worldwide. These pathogenic species have the ability to rapidly cross host tissue barriers by a yet unknown mechanism. A comparative analysis of pathogens and saprophytes revealed a higher abundance of genes encoding proteins with leucine-rich repeat (LRR) domains in the genomes of pathogens. In other bacterial pathogens, proteins with LRR domains have been shown to be involved in mediating host cell attachment and invasion. One protein from the pathogenic species Leptospira interrogans, LIC10831, has been previously analysed via X-ray crystallography, with findings suggesting it may be an important bacterial adhesin. Herein we show that LIC10831 elicits an antibody response in infected animals, is actively secreted by the bacterium, and binds human E- and VE-cadherins. These results provide biochemical and cellular evidences of LRR protein-mediated host-pathogen interactions and identify a new multireceptor binding protein from this infectious Leptospira species.

Indexed as

Adhesins, BacterialAnimalsAntigens, CDCadherin 5CadherinsCell LineCHO CellsCricetulusGuinea PigsHumansLeptospira interrogansLeptospirosisLeucine-Rich Repeat ProteinsProteinsAdhesins, BacterialAntigens, CDCadherin 5CadherinsCDH1 protein, humanLeucine-Rich Repeat ProteinsProteinsadherencecadherininfectionLeptospiraleucine-richspirochaete

Identifiers

PMID30171791
PMCPMC7560960
OpenAlexW2889214539

What OpenQuestion holds

Textmetadata
LicenceTDM
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.