Evidence map›Paper›PMID 23577214›Full record

ArticlePloS one2013

The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells.

Sidney D Taylor, Melissa E Sanders, Nathan A Tullos, Stephen J Stray, Erin W Norcross, Larry S McDaniel, Mary E Marquart

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
1.8field-weighted citation impact, top 15% 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, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Absence ofMicroorganisms · 2022
    Article
  7. Review
  8. Article
  9. Review
  10. iScience · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Lipids in the cell: organisation regulates function.Cellular and molecular life sciences : CMLS · 2018
    Review
  16. Article
  17. The Role of Pneumococcal Virulence Factors in Ocular Infectious Diseases.Interdisciplinary perspectives on infectious diseases · 2018
    Review
  18. Article
  19. Article
  20. 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 1 institution in 1 country.

Sidney D TaylorDepartment of Microbiology, University of Mississippi Medical Center, Jackson, Mississippi, USA.
Melissa E Sanders
Nathan A Tullos
Stephen J Stray
Erin W Norcross
Larry S McDaniel
Mary E Marquart
University of Mississippi Medical Center · US

Funding

Streptococcus pneumoniae ocular pathogenesis and therapyR01EY016195 · NEI · UNIVERSITY OF MISSISSIPPI MED CTR · PI MARQUART, MARY E · 2007 to 2011
$1.5M
NEI NIH HHS R01 EY016195NEI NIH HHS R01EY016195
6 · The paper itself

Abstract

Streptococcus pneumoniae (pneumococcus) is an opportunistic bacterial pathogen responsible for causing several human diseases including pneumonia, meningitis, and otitis media. Pneumococcus is also a major cause of human ocular infections and is commonly isolated in cases of bacterial keratitis, an infection of the cornea. The ocular pathology that occurs during pneumococcal keratitis is partly due to the actions of pneumolysin (Ply), a cholesterol-dependent cytolysin produced by pneumococcus. The lytic mechanism of Ply is a three step process beginning with surface binding to cholesterol. Multiple Ply monomers then oligomerize to form a prepore. The prepore then undergoes a conformational change that creates a large pore in the host cell membrane, resulting in cell lysis. We engineered a collection of single amino acid substitution mutants at residues (A370, A406, W433, and L460) that are crucial to the progression of the lytic mechanism and determined the effects that these mutations had on lytic function. Both Ply(WT) and the mutant Ply molecules (Ply(A370G), Ply(A370E), Ply(A406G), Ply(A406E), Ply(W433G), Ply(W433E), Ply(W433F), Ply(L460G), and Ply(L460E)) were able to bind to the surface of human corneal epithelial cells (HCECs) with similar efficiency. Additionally, Ply(WT) localized to cholesterol-rich microdomains on the HCEC surface, however, only one mutant (Ply(A370G)) was able to duplicate this behavior. Four of the 9 mutant Ply molecules (Ply(A370E), Ply(W433G), Ply(W433E), and Ply(L460E)) were deficient in oligomer formation. Lastly, all of the mutant Ply molecules, except Ply(A370G), exhibited significantly impaired lytic activity on HCECs. The other 8 mutants all experienced a reduction in lytic activity, but 4 of the 8 retained the ability to oligomerize. A thorough understanding of the molecular interactions that occur between Ply and the target cell, could lead to targeted treatments aimed to reduce the pathology observed during pneumococcal keratitis.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsCell LineCholesterolEpithelium, CornealHumansMembrane MicrodomainsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationPerforinProtein BindingProtein MultimerizationProtein Structure, QuaternaryBacterial ProteinsCholesterolPerforinplY protein, Streptococcus pneumoniaeStreptolysins

Identifiers

PMID23577214
PMCPMC3618221
OpenAlexW1977460922

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.