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Dynamics Characterization of Fully Hydrated Bacterial Cell Walls by Solid-State NMR: Evidence for Cooperative Binding of Metal Ions

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  • Life Sciences :: Biochemistry
  • Biophysics & Molecular Biology [F05]
  • Sciences Du Vivant :: Biochimie
  • Biophysique & Biologie Moléculaire [F05]

Abstract

Dynamics Characterization of Fully Hydrated Bacterial Cell Walls by Solid-State NMR: Evidence for Cooperative Binding of Metal Ions Thomas Kern,†,⊥ Mathilde Giffard,‡,⊥ Sabine Hediger,‡ Ana Amoroso,§ Ce´cile Giustini,† Nhat Khai Bui,| Bernard Joris,§ Catherine Bougault,† Waldemar Vollmer,| and Jean-Pierre Simorre*,† Institut de Biologie Structurale, UMR5075 (CEA/CNRS/UJF), 38027 Grenoble, France, Laboratoire de Chimie Inorganique et Biologique, UMR-E3 (CEA/UJF), FRE3200 (CEA/CNRS), INAC, CEA, 38054 Grenoble, France, Centre d’inge´nierie des prote´ines, Institut de Chimie B6A, UniVersite´ de Lie`ge, Sart-Tilman, B4000 Lie`ge, Belgium, and Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle UniVersity, Richardson Road, Newcastle upon Tyne NE2 4AX, United Kingdom Received May 25, 2010; E-mail: [email protected] Abstract: The bacterial cell wall maintains a cell’s integrity while allowing growth and division. It is made up of peptidoglycan (PG), a biopolymer forming a multigigadalton bag-like structure, and, additionally in Gram-positive bacteria, of covalently linked anionic polymers collectively called teichoic acids. These anionic polymers are thought to play important roles in host-cell adhesion, inflammation, and immune activation. In this Article, we compare the flexibility and the organization of peptidoglycans from Gram-negative bacteria (E. coli) with its counterpart from different Gram-positive bacteria using solid-state nuclear magnetic resonance spectroscopy (NMR) under magic-angle sample spinning (MAS). The NMR fingerprints suggest an identical local conformation of the PG in all of these bacterial species. Dynamics in the peptidoglycan network decreases from E. coli to B. subtilis and from B. subtilis to S. aureus and correlates mainly with the degree of peptide cross-linkage. For intact bacterial cells and isolated cell walls, we show that 31P solid-state NMR is particularly well adapted to characterize and differe

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