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Molecular basis for bacterial peptidoglycan recognition by LysM domains

Author

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  • Stéphane Mesnage

    (Krebs Institute, University of Sheffield, Firth Court, Western Bank
    University of Sheffield, Firth Court, Western Bank)

  • Mariano Dellarole

    (Centre de Biochimie Structurale, CNRS UMR 5048—UM 1—INSERM UMR 1054
    Present address: Institut Pasteur, Unité de Virologie Structurale, 28 Rue du Docteur Roux, F-75015 Paris, France)

  • Nicola J. Baxter

    (Krebs Institute, University of Sheffield, Firth Court, Western Bank
    University of Sheffield, Firth Court, Western Bank)

  • Jean-Baptiste Rouget

    (Centre de Biochimie Structurale, CNRS UMR 5048—UM 1—INSERM UMR 1054)

  • Jordan D. Dimitrov

    (INSERM, U872, Centre de Recherche des Cordeliers
    Université Pierre et Marie Curie
    Université Paris Descartes)

  • Ning Wang

    (Laboratory for Natural Products Chemistry, Osaka University)

  • Yukari Fujimoto

    (Laboratory for Natural Products Chemistry, Osaka University)

  • Andrea M. Hounslow

    (Krebs Institute, University of Sheffield, Firth Court, Western Bank
    University of Sheffield, Firth Court, Western Bank)

  • Sébastien Lacroix-Desmazes

    (INSERM, U872, Centre de Recherche des Cordeliers
    Université Pierre et Marie Curie
    Université Paris Descartes)

  • Koichi Fukase

    (Laboratory for Natural Products Chemistry, Osaka University)

  • Simon J. Foster

    (Krebs Institute, University of Sheffield, Firth Court, Western Bank
    University of Sheffield, Firth Court, Western Bank)

  • Michael P. Williamson

    (Krebs Institute, University of Sheffield, Firth Court, Western Bank
    University of Sheffield, Firth Court, Western Bank)

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.

Suggested Citation

  • 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 & Si, 2014. "Molecular basis for bacterial peptidoglycan recognition by LysM domains," Nature Communications, Nature, vol. 5(1), pages 1-11, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5269
    DOI: 10.1038/ncomms5269
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