Abstract
Peptidoglycan is the fundamental structural constituent of the bacterial cell wall. Despite many years of research, the architecture of peptidoglycan is still largely elusive. Here, we report the high-resolution architecture of peptidoglycan from the model Gram-positive bacterium Bacillus subtilis. We provide high-resolution evidence of peptidoglycan architecture remodeling at different growth stages. Side wall peptidoglycan from B. subtilis strain AS1.398 changed from an irregular architecture in exponential growth phase to an ordered cable-like architecture in stationary phase. Thickness of side wall peptidoglycan was found to be related with growth stages, with a slight increase after transition to stationary phase. Septal disks were synthesized progressively toward the center, while the surface features were less clear than those imaged with side walls. Compared with previous studies, our results revealed slight differences in architecture of peptidoglycan from different B. subtilis strains, expanding our knowledge about the architectural features of B. subtilis peptidoglycan.
Highlights
Peptidoglycan is the major constituent of bacterial cell wall, and it is essential for bacteria to maintain their specific shape and to protect the cells from rupture by the internal turgor pressure (Typas et al, 2012)
Bacterial growth was monitored by measuring the optical density at 600 nm (OD600) with a UV/VIS-550 spectrophotometer (Jasco, Japan)
The peptidoglycan of Gram-positive bacteria is significantly thicker and more complex than the peptidoglycan of Gramnegative bacteria, and the three dimensional architectures of Gram-positive peptidoglycan was largely unclear in the past
Summary
Peptidoglycan is the major constituent of bacterial cell wall, and it is essential for bacteria to maintain their specific shape and to protect the cells from rupture by the internal turgor pressure (Typas et al, 2012). Peptidoglycan Architecture From Bacillus subtilis both isolated sacculi and living bacterial cells based on AFM works were reported during the past decade (Hayhurst et al, 2008; Andre et al, 2010; Turner et al, 2010, 2013; Wheeler et al, 2011; Dover et al, 2015). AFM studies on isolated sacculi pieces from B. subtilis showed that septal peptidoglycan was organized into ∼135-nm-wide “cable” like structures forming a spiral appearance toward the center (Hayhurst et al, 2008).
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