Evidence map›Paper›PMID 31015325›Full record

ArticlemBio2019

The Structural Basis for a Transition State That Regulates Pore Formation in a Bacterial Toxin.

Kristin R Wade, Sara L Lawrence, Allison J Farrand, Eileen M Hotze, Michael J Kuiper, Michael A Gorman, Michelle P Christie, Santosh Panjikar, Craig J Morton, Michael W Parker and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
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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

11 authors.

Kristin R Wade *Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Sara L Lawrence *St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Allison J FarrandDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Eileen M HotzeDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Michael J KuiperVictorian Life Sciences Computation Initiative, The University of Melbourne, Carlton, Victoria, Australia.
Michael A GormanSt. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Michelle P ChristieDepartment of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria, Australia.
Santosh PanjikarAustralian Synchrotron, Clayton, Victoria, Australia.
Craig J Morton *St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Michael W Parker *St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia mparker@svi.edu.au Rod-Tweten@ouhsc.edu.
Rodney K Tweten *Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA mparker@svi.edu.au Rod-Tweten@ouhsc.edu.

Funding

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 R37 AI037657
6 · The paper itself

Abstract

The cholesterol-dependent cytolysin (CDC) genes are present in bacterial species that span terrestrial, vertebrate, and invertebrate niches, which suggests that they have evolved to function under widely different environmental conditions. Using a combination of biophysical and crystallographic approaches, we reveal that the relative stability of an intramolecular interface in the archetype CDC perfringolysin O (PFO) plays a central role in regulating its pore-forming properties. The disruption of this interface allows the formation of the membrane spanning β-barrel pore in all CDCs. We show here that the relative strength of the stabilizing forces at this interface directly impacts the energy barrier posed by the transition state for pore formation, as reflected in the Arrhenius activation energy (E

Indexed as

Bacterial ToxinsChemical PhenomenaCrystallography, X-RayDNA Mutational AnalysisHemolysin ProteinsKineticsMolecular Dynamics SimulationPore Forming Cytotoxic ProteinsTemperatureBacterial ToxinsClostridium perfringens theta-toxinHemolysin ProteinsPore Forming Cytotoxic Proteinscold denaturationcomplementgasderminperforinwater network

Identifiers

PMID31015325
PMCPMC6479001

What OpenQuestion holds

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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.