Evidence map›Paper›PMID 40153490›Full record

ArticleScience advances2025

Structural basis for the pore-forming activity of a complement-like toxin.

Bronte A Johnstone, Michelle P Christie, Riya Joseph, Craig J Morton, Hamish G Brown, Eric Hanssen, Tristan C Sanford, Hunter L Abrahamsen, Rodney K Tweten, Michael W Parker

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. 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

10 authors.

Bronte A JohnstoneDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0003-3313-5553
Michelle P ChristieDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0002-7001-3400
Riya JosephDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Craig J MortonDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0001-5452-5193
Hamish G BrownIan Holmes Imaging Centre, Bio21 Molecular Science & Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0003-2292-7766
Eric HanssenARC Centre for Cryo-Electron Microscopy of Membrane Proteins, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0002-4064-1844
Tristan C SanfordDepartment of Microbiology & Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.ORCID 0000-0002-3466-2630
Hunter L AbrahamsenDepartment of Microbiology & Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Rodney K TwetenDepartment of Microbiology & Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Michael W ParkerDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.ORCID 0000-0002-3101-1138

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

Pore-forming proteins comprise a highly diverse group of proteins exemplified by the membrane attack complex/perforin (MACPF), cholesterol-dependent cytolysin (CDC), and gasdermin superfamilies, which all form gigantic pores (>150 angstroms). A recently found family of pore-forming toxins, called CDC-like proteins (CDCLs), are wide-spread in gut microbes and are a prevalent means of antibacterial antagonism. However, the structural aspects of how CDCLs assemble a pore remain a mystery. Here, we report the crystal structure of a proteolytically activated CDCL and cryo-electron microscopy structures of a prepore-like intermediate and a transmembrane pore providing detailed snapshots across the entire pore-forming pathway. These studies reveal a sophisticated array of regulatory features to ensure productive pore formation, and, thus, CDCLs straddle the MACPF, CDC, and gasdermin lineages of the giant pore superfamilies.

Indexed as

Pore Forming Cytotoxic ProteinsComplement Membrane Attack ComplexCryoelectron MicroscopyCrystallography, X-RayHumansModels, MolecularPerforinProtein ConformationComplement Membrane Attack ComplexPerforinPore Forming Cytotoxic Proteins

Identifiers

PMID40153490
PMCPMC11952106

What Socratic 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 Socratic graph.