Evidence map›Paper›PMID 26403197›Full record

ArticleScientific reports2015

Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.

Sara L Lawrence, Susanne C Feil, Craig J Morton, Allison J Farrand, Terrence D Mulhern, Michael A Gorman, Kristin R Wade, Rodney K Tweten, Michael W Parker

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.

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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

9 authors at 3 institutions in 2 countries.

Sara L LawrenceACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia.
Susanne C FeilACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia.
Craig J MortonACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia.
Allison J FarrandDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
Terrence D MulhernDepartment of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria 3010, Australia.
Michael A GormanACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia.
Kristin R WadeDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
Rodney K TwetenDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
Michael W ParkerACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia.
St Vincents Institute of Medical Research · AUUniversity of Oklahoma Health Sciences Center · USUniversity of Melbourne · AU

Funding

Pore Formation by Cholesterol Dependent CytolysinsR01AI037657 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TWETEN, RODNEY K. · 1997 to 2015
$5.4M
Pore Formation by Cholesterol Dependent CytolysinsR37AI037657 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TWETEN, RODNEY K. · 2016 to 2025
$4.8M
NIAID NIH HHS AI037657NIAID NIH HHS R01 AI037657NIAID NIH HHS R37 AI037657
6 · The paper itself

Abstract

Pore-forming proteins are weapons often used by bacterial pathogens to breach the membrane barrier of target cells. Despite their critical role in infection important structural aspects of the mechanism of how these proteins assemble into pores remain unknown. Streptococcus pneumoniae is the world's leading cause of pneumonia, meningitis, bacteremia and otitis media. Pneumolysin (PLY) is a major virulence factor of S. pneumoniae and a target for both small molecule drug development and vaccines. PLY is a member of the cholesterol-dependent cytolysins (CDCs), a family of pore-forming toxins that form gigantic pores in cell membranes. Here we present the structure of PLY determined by X-ray crystallography and, in solution, by small-angle X-ray scattering. The crystal structure reveals PLY assembles as a linear oligomer that provides key structural insights into the poorly understood early monomer-monomer interactions of CDCs at the membrane surface.

Indexed as

Models, MolecularProtein ConformationBacterial ProteinsBinding SitesCarbohydratesCrystallography, X-RayMannoseMolecular Docking SimulationMutationProtein BindingProtein MultimerizationSolutionsStreptolysinsStructure-Activity RelationshipBacterial ProteinsCarbohydratesMannoseplY protein, Streptococcus pneumoniaeSolutionsStreptolysins

Identifiers

PMID26403197
PMCPMC4585913
OpenAlexW2245269023

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.