Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis

In Escherichia coli, lateral cell-wall expansion during growth occurs by cross-linking of new glycan strands to the existing peptidoglycan network. However, it is unclear whether the same mechanism applies to other rod-shaped bacteria. Here, we use cell imaging and mass spectrometry analysis of isotopically labeled peptidoglycan to study this process in the Gram-positive bacterium Bacillus subtilis. We show that new glycan strands are cross-linked exclusively to other newly synthesized glycan chains, and not to the existing peptidoglycan network. We propose that new peptidoglycan meshes, assembled at the membrane surface, impose a shift on older meshes toward the bacterial surface, where they sustain the cytoplasmic turgor pressure, before their eventual degradation. This outward movement would result in preferential lateral expansion due to the large difference in the strain tensors of the peptidic and glycosidic peptidoglycan components.

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Publication Details

Journal
Nature Communications
Published
2025-07-19
DOI
https://doi.org/10.1038/s41467-025-61900-0
Citations
1
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
1.82

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article

Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis

Filippo Rusconi, Yucheng Liang, Yung‐Sing Wong, Cécile Morlot et al.
1 citations
Nature Communications
Bacterial Genetics and Biotechnology
1.82
article

Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis

Filippo Rusconi, Yucheng Liang, Yung‐Sing Wong, Cécile Morlot, Michel Arthur, Jean‐Emmanuel Hugonnet, Laure Bellard
article en
1 citations

Abstract

In Escherichia coli, lateral cell-wall expansion during growth occurs by cross-linking of new glycan strands to the existing peptidoglycan network. However, it is unclear whether the same mechanism applies to other rod-shaped bacteria. Here, we use cell imaging and mass spectrometry analysis of isotopically labeled peptidoglycan to study this process in the Gram-positive bacterium Bacillus subtilis. We show that new glycan strands are cross-linked exclusively to other newly synthesized glycan chains, and not to the existing peptidoglycan network. We propose that new peptidoglycan meshes, assembled at the membrane surface, impose a shift on older meshes toward the bacterial surface, where they sustain the cytoplasmic turgor pressure, before their eventual degradation. This outward movement would result in preferential lateral expansion due to the large difference in the strain tensors of the peptidic and glycosidic peptidoglycan components.

Nature CommunicationsVol. 16(1)
Centre National de la Recherche Scientifique (FR), Inserm (FR), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR), Université Paris Sciences et Lettres (FR), Université Paris-Saclay (FR), École Normale Supérieure - PSL (FR), CEA Grenoble (FR), Sorbonne Université (FR), Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR), Sorbonne Paris Cité (FR), Institut de Biologie Structurale (FR), Chimie Physique et Chimie du Vivant (FR), Université Grenoble Alpes (FR)
Université Grenoble Alpes, Agence Nationale de la Recherche, Centre National de la Recherche Scientifique, Muséum National d'Histoire Naturelle, French Infrastructure for Integrated Structural Biology
Life in Land
Openalex Percentile: Top 14%
Bacterial Genetics and Biotechnology
1.82
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