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A Clostridioides difficile endolysin modulates toxin secretion without cell lysis.

Milena M Awad1, Chathura D Suraweera1, Callum J Vidor1

  • 1Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, 3800, Australia.

Communications Biology
|August 23, 2024
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Summary
This summary is machine-generated.

Clostridioides difficile secretes toxins via a novel mechanism. A specific peptidoglycan amidase, M7404_02200, facilitates the non-lytic release of Large Clostridial Glucosylating Toxins (LCGTs).

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • Clostridia, including Clostridioides difficile, produce Large Clostridial Glucosylating Toxins (LCGTs) crucial for disease.
  • The secretion mechanism for these toxins remains largely uncharacterized.
  • A holin-like protein was recently identified as essential for toxin release.

Purpose of the Study:

  • To investigate the role of putative lysins in the secretion of TcdA and TcdB from Clostridioides difficile.
  • To determine if Clostridia utilize a lysin-based system for toxin release, analogous to bacteriophages.

Main Methods:

  • Sequence analysis and structural modeling of two conserved putative lysins (M7404_01910 and M7404_02200).
  • Gene disruption experiments to assess the contribution of each putative lysin to toxin secretion.
  • Peptidoglycan hydrolysis assays using recombinant M7404_02200.

Main Results:

  • Both M7404_01910 and M7404_02200 were predicted to be N-acetylmuramoyl-l-alanine amidases.
  • Only M7404_02200 was found to be essential for the secretion of TcdA and TcdB.
  • Toxin secretion mediated by M7404_02200 occurred in a non-lytic manner.
  • Recombinant M7404_02200 demonstrated active peptidoglycan amidase activity.

Conclusions:

  • M7404_02200 functions as a peptidoglycan amidase in Clostridioides difficile.
  • This amidase plays a critical role in the non-lytic secretion of LCGTs, specifically TcdA and TcdB.
  • The findings reveal a novel toxin secretion mechanism in C. difficile distinct from typical phage lysis.