Multiparametric AFM reveals turgor-responsive net-like peptidoglycan architecture in live streptococci

Ron Saar Dover; Arkady Bitler; Eyal Shimoni; Patrick Trieu-Cuot; Yechiel Shai

doi:10.1038/ncomms8193

Multiparametric AFM reveals turgor-responsive net-like peptidoglycan architecture in live streptococci

Ron Saar Dover, Arkady Bitler, Eyal Shimoni, Patrick Trieu-Cuot, Yechiel Shai

Research output: Contribution to journal › Article › peer-review

49 Scopus citations

Abstract

Cell-wall peptidoglycan (PG) of Gram-positive bacteria is a strong and elastic multi-layer designed to resist turgor pressure and determine the cell shape and growth. Despite its crucial role, its architecture remains largely unknown. Here using high-resolution multiparametric atomic force microscopy (AFM), we studied how the structure and elasticity of PG change when subjected to increasing turgor pressure in live Group B Streptococcus. We show a new net-like arrangement of PG, which stretches and stiffens following osmotic challenge. The same structure also exists in isogenic mutants lacking surface appendages. Cell aging does not alter the elasticity of the cell wall, yet destroys the net architecture and exposes single segmented strands with the same circumferential orientation as predicted for intact glycans. Together, we show a new functional PG architecture in live Gram-positive bacteria.

Original language	English
Article number	7193
Journal	Nature Communications
Volume	6
DOIs	https://doi.org/10.1038/ncomms8193
State	Published - 28 May 2015
Externally published	Yes

Bibliographical note

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© 2015 Macmillan Publishers Limited. All rights reserved.

Funding

We are grateful to A. Ashkenazi, E.M. Reuven, Y. Klug and the present members of the Shai laboratory for their comments and suggestions. The electron microscopy studies were conducted at the Irving and Cherna Moskowitz Center for Nano and Bio-Nano Imaging at the Weizmann Institute of Science. This work was supported by funding from the Israel Ministry of Health (IMOH), Grant No. 3-7291 (to Y.S.), the Conseil Pasteur-Weizmann and the European Community’s Seventh Framework Programme (FP7/2007–2013) under grant agreement n° 278998 (to Y.S.). PTC’s work was supported by the Institut Pasteur, the CNRS, the French Government’s Investissement d’Avenir program, Laboratoire d’Excellence ‘Integrative Biology of Emerging Infectious Diseases’ Grant ANR-10-LABX-62-IBEID and Fondation pour la Recherche Médicale Grant DEQ20130326538.

Funders	Funder number
FP7/2007
Israel Ministry of Health	3-7291
Seventh Framework Programme	278998
Fondation pour la Recherche Médicale	DEQ20130326538
Institut Pasteur
Centre National de la Recherche Scientifique	ANR-10-LABX-62-IBEID
Seventh Framework Programme

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abstract = "Cell-wall peptidoglycan (PG) of Gram-positive bacteria is a strong and elastic multi-layer designed to resist turgor pressure and determine the cell shape and growth. Despite its crucial role, its architecture remains largely unknown. Here using high-resolution multiparametric atomic force microscopy (AFM), we studied how the structure and elasticity of PG change when subjected to increasing turgor pressure in live Group B Streptococcus. We show a new net-like arrangement of PG, which stretches and stiffens following osmotic challenge. The same structure also exists in isogenic mutants lacking surface appendages. Cell aging does not alter the elasticity of the cell wall, yet destroys the net architecture and exposes single segmented strands with the same circumferential orientation as predicted for intact glycans. Together, we show a new functional PG architecture in live Gram-positive bacteria.",

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Multiparametric AFM reveals turgor-responsive net-like peptidoglycan architecture in live streptococci

Abstract

Bibliographical note

Funding

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