Evidence map›Paper›PMID 24759615›Full record

ArticleOpen biology2014

Incomplete pneumolysin oligomers form membrane pores.

Andreas F-P Sonnen, Jürgen M Plitzko, Robert J C Gilbert

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 94 citations in OpenAlex.

  1. AFM to Study Pore-Forming Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
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  11. Corilagin: A Novel Antivirulence Strategy to AlleviateMolecules (Basel, Switzerland) · 2022
    Article
  12. Review
  13. Article
  14. Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022
    Article
  15. Review
  16. Review
  17. Mitochondrial outer membrane permeabilization at the single molecule level.Cellular and molecular life sciences : CMLS · 2021
    Review
  18. Article
  19. Review
  20. 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

3 authors at 3 institutions in 3 countries.

Andreas F-P SonnenDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Jürgen M Plitzko
Robert J C Gilbert
Centre for Human Genetics · GBMax Planck Institute of Biochemistry · DEUtrecht University · NL

Funding

Wellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

Pneumolysin is a member of the cholesterol-dependent cytolysin (CDC) family of pore-forming proteins that are produced as water-soluble monomers or dimers, bind to target membranes and oligomerize into large ring-shaped assemblies comprising approximately 40 subunits and approximately 30 nm across. This pre-pore assembly then refolds to punch a large hole in the lipid bilayer. However, in addition to forming large pores, pneumolysin and other CDCs form smaller lesions characterized by low electrical conductance. Owing to the observation of arc-like (rather than full-ring) oligomers by electron microscopy, it has been hypothesized that smaller oligomers explain smaller functional pores. To investigate whether this is the case, we performed cryo-electron tomography of pneumolysin oligomers on model lipid membranes. We then used sub-tomogram classification and averaging to determine representative membrane-bound low-resolution structures and identified pre-pores versus pores by the presence of membrane within the oligomeric curve. We found pre-pore and pore forms of both complete (ring) and incomplete (arc) oligomers and conclude that arc-shaped oligomeric assemblies of pneumolysin can form pores. As the CDCs are evolutionarily related to the membrane attack complex/perforin family of proteins, which also form variably sized pores, our findings are of relevance to that class of proteins as well.

Indexed as

Bacterial ProteinsBacterial ToxinsCholesterolLipid BilayersLiposomesMicroscopy, Electron, TransmissionOrganophosphatesPhosphatidylcholinesRecombinant ProteinsStreptolysinsBacterial ProteinsBacterial ToxinsCholesteroldicetylphosphateLipid BilayersLiposomesOrganophosphatesPhosphatidylcholinesplY protein, Streptococcus pneumoniaeRecombinant ProteinsStreptolysinscryo-electron tomographypneumolysinpore formationproteolipid poretoroidal pore

Identifiers

PMID24759615
PMCPMC4043118
OpenAlexW2160293301

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.