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

Ron Saar Dover, Arkady Bitler, Eyal Shimoni, Patrick Trieu-Cuot and Yechiel Shai ()
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Ron Saar Dover: 8 Ulman Building, The Weizmann Institute of Science
Arkady Bitler: Surface Analysis Unit, Goldwurm Building, The Weizmann Institute of Science
Eyal Shimoni: Electron Microscopy Unit, Issac Wolfson Building, The Weizmann Institute of Science
Patrick Trieu-Cuot: Institut Pasteur, Unité de Biologie des Bactéries Pathogènes à Gram-Positif, CNRS ERL3526
Yechiel Shai: 8 Ulman Building, The Weizmann Institute of Science

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8193

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