Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode.

Autor: Alvarez L; Department of Molecular Biology, Umeå University, Umeå, Sweden., Hernandez SB; Department of Molecular Biology, Umeå University, Umeå, Sweden.; Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Seville, Spain., Torrens G; Department of Molecular Biology, Umeå University, Umeå, Sweden., Weaver AI; Department of Microbiology, Cornell University, Ithaca, New York, USA.; Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.; Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA., Dörr T; Department of Microbiology, Cornell University, Ithaca, New York, USA.; Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.; Cornell Institute of Host-Microbe Interactions and Disease, Cornell University, Ithaca, New York, USA., Cava F; Department of Molecular Biology, Umeå University, Umeå, Sweden. felipe.cava@umu.se.; Umeå Center for Microbial Research (UCMR), Umeå University, Umeå, Sweden. felipe.cava@umu.se.; The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå, Sweden. felipe.cava@umu.se.; Science for Life Laboratory (SciLifeLab), Umeå University, Umeå, Sweden. felipe.cava@umu.se.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Sep 11; Vol. 15 (1), pp. 7937. Date of Electronic Publication: 2024 Sep 11.
DOI: 10.1038/s41467-024-52325-2
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
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