Staphylococcus aureus sacculus mediates activities of M23 hydrolases

Alicja Razew, Cedric Laguri, Alicia Vallet, Catherine Bougault, Magdalena Kaus-Drobek, Izabela Sabala () and Jean-Pierre Simorre ()
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Alicja Razew: Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Cedric Laguri: Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Alicia Vallet: Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Catherine Bougault: Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale
Magdalena Kaus-Drobek: Polish Academy of Sciences
Izabela Sabala: International Institute of Molecular and Cell Biology in Warsaw
Jean-Pierre Simorre: Universite Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract Peptidoglycan, a gigadalton polymer, functions as the scaffold for bacterial cell walls and provides cell integrity. Peptidoglycan is remodelled by a large and diverse group of peptidoglycan hydrolases, which control bacterial cell growth and division. Over the years, many studies have focused on these enzymes, but knowledge on their action within peptidoglycan mesh from a molecular basis is scarce. Here, we provide structural insights into the interaction between short peptidoglycan fragments and the entire sacculus with two evolutionarily related peptidases of the M23 family, lysostaphin and LytM. Through nuclear magnetic resonance, mass spectrometry, information-driven modelling, site-directed mutagenesis and biochemical approaches, we propose a model in which peptidoglycan cross-linking affects the activity, selectivity and specificity of these two structurally related enzymes differently.

Date: 2023
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DOI: 10.1038/s41467-023-42506-w

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