Molecular basis for bacterial peptidoglycan recognition by LysM domains

Stéphane Mesnage, Mariano Dellarole, Nicola J. Baxter, Jean Baptiste Rouget, Jordan D. Dimitrov, Ning Wang, Yukari Fujimoto, Andrea M. Hounslow, Sébastien Lacroix-Desmazes, Koichi Fukase, Simon J. Foster, Michael P. Williamson

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Carbohydrate recognition is essential for growth, cell adhesion and signalling in all living organisms. A highly conserved carbohydrate binding module, LysM, is found in proteins from viruses, bacteria, fungi, plants and mammals. LysM modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidoglycan, an essential component of the bacterial cell wall. However, the molecular mechanism underpinning LysM-peptidoglycan interactions remains unclear. Here we describe the molecular basis for peptidoglycan recognition by a multimodular LysM domain from AtlA, an autolysin involved in cell division in the opportunistic bacterial pathogen Enterococcus faecalis. We explore the contribution of individual modules to the binding, identify the peptidoglycan motif recognized, determine the structures of free and bound modules and reveal the residues involved in binding. Our results suggest that peptide stems modulate LysM binding to peptidoglycan. Using these results, we reveal how the LysM module recognizes the GlcNAc-X-GlcNAc motif present in polysaccharides across kingdoms.

Original languageEnglish
Article number4269
JournalNature Communications
Volume5
DOIs
Publication statusPublished - 2014 Jun 30
Externally publishedYes

Fingerprint

Peptidoglycan
modules
polysaccharides
carbohydrates
Polysaccharides
Cells
Carbohydrates
N-Acetylmuramoyl-L-alanine Amidase
Cell signaling
cell division
mammals
Mammals
Acetylglucosamine
pathogens
fungi
Enterococcus faecalis
Cell adhesion
viruses
Pathogens
Fungi

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry(all)
  • Physics and Astronomy(all)

Cite this

Mesnage, S., Dellarole, M., Baxter, N. J., Rouget, J. B., Dimitrov, J. D., Wang, N., ... Williamson, M. P. (2014). Molecular basis for bacterial peptidoglycan recognition by LysM domains. Nature Communications, 5, [4269]. https://doi.org/10.1038/ncomms5269

Molecular basis for bacterial peptidoglycan recognition by LysM domains. / Mesnage, Stéphane; Dellarole, Mariano; Baxter, Nicola J.; Rouget, Jean Baptiste; Dimitrov, Jordan D.; Wang, Ning; Fujimoto, Yukari; Hounslow, Andrea M.; Lacroix-Desmazes, Sébastien; Fukase, Koichi; Foster, Simon J.; Williamson, Michael P.

In: Nature Communications, Vol. 5, 4269, 30.06.2014.

Research output: Contribution to journalArticle

Mesnage, S, Dellarole, M, Baxter, NJ, Rouget, JB, Dimitrov, JD, Wang, N, Fujimoto, Y, Hounslow, AM, Lacroix-Desmazes, S, Fukase, K, Foster, SJ & Williamson, MP 2014, 'Molecular basis for bacterial peptidoglycan recognition by LysM domains', Nature Communications, vol. 5, 4269. https://doi.org/10.1038/ncomms5269
Mesnage S, Dellarole M, Baxter NJ, Rouget JB, Dimitrov JD, Wang N et al. Molecular basis for bacterial peptidoglycan recognition by LysM domains. Nature Communications. 2014 Jun 30;5. 4269. https://doi.org/10.1038/ncomms5269
Mesnage, Stéphane ; Dellarole, Mariano ; Baxter, Nicola J. ; Rouget, Jean Baptiste ; Dimitrov, Jordan D. ; Wang, Ning ; Fujimoto, Yukari ; Hounslow, Andrea M. ; Lacroix-Desmazes, Sébastien ; Fukase, Koichi ; Foster, Simon J. ; Williamson, Michael P. / Molecular basis for bacterial peptidoglycan recognition by LysM domains. In: Nature Communications. 2014 ; Vol. 5.
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