Evidence map›Paper›PMID 20008530›Full record

ArticleInfection and immunity2010

Pseudomonas aeruginosa-mediated damage requires distinct receptors at the apical and basolateral surfaces of the polarized epithelium.

Iwona Bucior, Keith Mostov, Joanne N Engel

Abstract read
In one paragraph

Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

53 citing papers in PubMed, 70 citations in OpenAlex.

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  9. Infectious medicine · 2023
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  11. Assessment of the Glycan-Binding Profile ofbioRxiv : the preprint server for biology · 2023
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  13. Review
  14. Review
  15. Article
  16. Article
  17. Molecular Mechanisms Involved in Pseudomonas aeruginosa Bacteremia.Advances in experimental medicine and biology · 2022
    Review
  18. Review
  19. Article
  20. Glucocorticoids ElevateFrontiers in microbiology · 2021
    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

3 authors at 2 institutions in 2 countries.

Iwona BuciorDepartment of Medicine, Microbial Pathogenesis and Host Defense Program, University of California, San Francisco, CA 94143, USA.
Keith Mostov
Joanne N Engel
Institute of Molecular Biology and Biophysics · RUUniversity of California, San Francisco · US

Funding

Sulfs and Injury Repair in Mucosal EpitheliaP01AI053194 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ENGEL, JOANNE N. · 2002 to 2012
$13.4M
New approaches to Study Pseudomonas-host interactionsR01AI065902 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ENGEL, JOANNE N. · 2005 to 2013
$2.8M
Control of Orientation of Epithelial PolarityR01DK067153 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MOSTOV, KEITH E · 2004 to 2008
$1.7M
NIAID NIH HHS P01 AI053194NIAID NIH HHS R01 AI065902NIDDK NIH HHS R01 DK067153
6 · The paper itself

Abstract

Pseudomonas aeruginosa, an important opportunistic pathogen of humans, exploits epithelial damage to establish infection. We have rigorously explored the role of N-glycoproteins and heparan sulfate proteoglycans (HSPGs) in P. aeruginosa-mediated attachment and subsequent downstream events at the apical (AP) and basolateral (BL) surfaces of polarized epithelium. We demonstrate that the N-glycan chains at the AP surface are necessary and sufficient for binding, invasion, and cytotoxicity to kidney (MDCK) and airway (Calu-3) cells grown at various states of polarization on Transwell filters. Upregulation of N-glycosylation enhanced binding, whereas pharmacologic inhibition of N-glycosylation or infection of MDCK cells defective in N-glycosylation resulted in decreased binding. In contrast, at the BL surface, the HS moiety of HSPGs mediated P. aeruginosa binding, cytotoxicity, and invasion. In incompletely polarized epithelium, HSPG abundance was increased at the AP surface, explaining its increased susceptibility to P. aeruginosa colonization and damage. Using MDCK cells grown as three-dimensional cysts as a model for epithelial organs, we show that P. aeruginosa specifically colocalized with HS-rich areas at the BL membrane but with complex N-glycans at the AP surface. Finally, P. aeruginosa bound to HS chains and N-glycans coated on plastic surfaces, showing the highest binding affinity toward isolated HS chains. Together, these findings demonstrate that P. aeruginosa recognizes distinct receptors on the AP and BL surfaces of polarized epithelium. Changes in the composition of N-glycan chains and/or in the distribution of HSPGs may explain the enhanced susceptibility of damaged epithelium to P. aeruginosa.

Indexed as

Bacterial AdhesionCell PolarityAnimalsCell LineDogsEpithelial CellsEpitheliumGlycoproteinsHeparan SulfateHumansOrgan Culture TechniquesProtein BindingPseudomonas aeruginosaGlycoproteinsHeparan Sulfate

Identifiers

PMID20008530
PMCPMC2825949
OpenAlexW2105593245

What OpenQuestion holds

Textmetadata
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.