Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 Sep 2024
11 Sep 2024
Historique:
received:
21
03
2024
accepted:
03
09
2024
medline:
12
9
2024
pubmed:
12
9
2024
entrez:
11
9
2024
Statut:
epublish
Résumé
To withstand their internal turgor pressure and external threats, most bacteria have a protective peptidoglycan (PG) cell wall. The growth of this PG polymer relies on autolysins, enzymes that create space within the structure. Despite extensive research, the regulatory mechanisms governing these PG-degrading enzymes remain poorly understood. Here, we unveil a novel and widespread control mechanism of lytic transglycosylases (LTs), a type of autolysin responsible for breaking down PG glycan chains. Specifically, we show that LD-crosslinks within the PG sacculus act as an inhibitor of LT activity. Moreover, we demonstrate that this regulation controls the release of immunogenic PG fragments and provides resistance against predatory LTs of both bacterial and viral origin. Our findings address a critical gap in understanding the physiological role of the LD-crosslinking mode in PG homeostasis, highlighting how bacteria can enhance their resilience against environmental threats, including phage attacks, through a single structural PG modification.
Identifiants
pubmed: 39261529
doi: 10.1038/s41467-024-52325-2
pii: 10.1038/s41467-024-52325-2
doi:
Substances chimiques
Peptidoglycan
0
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
Bacterial Proteins
0
Glycosyltransferases
EC 2.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7937Informations de copyright
© 2024. The Author(s).
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