Autor: |
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 |
Jazyk: |
angličtina |
Rok vydání: |
2024 |
Předmět: |
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Zdroj: |
Communications Biology, Vol 7, Iss 1, Pp 1-12 (2024) |
Druh dokumentu: |
article |
ISSN: |
2399-3642 |
DOI: |
10.1038/s42003-024-06730-4 |
Popis: |
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. |
Databáze: |
Directory of Open Access Journals |
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