Evidence map›Paper›PMID 39179651›Full record

ArticleCommunications biology2024

A Clostridioides difficile endolysin modulates toxin secretion without cell lysis.

Milena M Awad, Chathura D Suraweera, Callum J Vidor, Auberon Y Ye-Lin, Galain C Williams, Steven J Mileto, Christopher K Barlow, Sheena McGowan, Dena Lyras

Abstract read
In one paragraph

Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. EndD mediates butyrate-dependent toxin release inbioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. The emerging view on the roles of butyrate inInfection and immunity · 2025
    Review
  5. Article
  6. 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

9 authors.

Milena M Awad *Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.ORCID 0000-0002-9275-3979
Chathura D Suraweera *Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.
Callum J VidorDepartment of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.
Auberon Y Ye-LinDepartment of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.ORCID 0009-0008-0201-551X
Galain C WilliamsDepartment of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.ORCID 0000-0001-9347-7198
Steven J MiletoDepartment of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.ORCID 0000-0003-2599-8957
Christopher K BarlowDepartment of Biochemistry, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.
Sheena McGowanDepartment of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.ORCID 0000-0001-6863-1106
Dena LyrasDepartment of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia. dena.lyras@monash.edu.ORCID 0000-0003-2345-9271

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Clostridia produce and secrete Large Clostridial Glucosylating Toxins (LCGTs) responsible for disease symptoms, but the secretion mechanism is largely unknown. Recently, a holin-like protein was shown to be essential for toxin secretion. Holins, typically bacteriophage-specific proteins, are part of the holin-endo(lysin) system that releases phage progeny. To determine if the clostridia also use a lysin, we investigated two conserved putative lysins, M7404_01910 and M7404_02200, in the release of the LCGTs TcdA and TcdB from a Clostridioides difficile ribotype 027 strain, M7404. Sequence analysis and structural modelling indicates that both proteins are related to N-acetylmuramoyl-l-alanine amidases, similar to CD27L, a lysin from the C. difficile phage ΦCD27. Disruption of these genes reveal that only M7404_02200 contributes to toxin secretion and does so in a non-lytic fashion. Peptidoglycan hydrolysis assays show that recombinant M7404_02200 is an active peptidoglycan amidase, confirming its role in TcdA and TcdB secretion in C. difficile M7404.

Indexed as

Bacterial ProteinsBacterial ToxinsClostridioides difficileEndopeptidasesEnterotoxinsPeptidoglycanBacterial ProteinsBacterial ToxinsendolysinEndopeptidasesEnterotoxinsPeptidoglycantcdA protein, Clostridium difficiletoxB protein, Clostridium difficile

Identifiers

PMID39179651
PMCPMC11344133

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.