ArticleNature communications2014
Molecular basis for bacterial peptidoglycan recognition by LysM domains.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed, 214 citations in OpenAlex.
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- Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026Article
- Virulence Associated Morphology of Different Strains of Melissococcus plutonius, a Brood Pathogen of Honey Bees.Environmental microbiology reports · 2026Article
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
- A novel temperate phage fromMicrobiology spectrum · 2026Article
- Structural insights into glycan recognition by plant immune receptors: a comparative perspective with animal innate immune systems.The Plant journal : for cell and molecular biology · 2026Review
- Advanced Research on LysM Domain-Containing Proteins: Functional Mechanisms and Roles in Pathogenicity of Plant Fungi.International journal of molecular sciences · 2026Review
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Functional characterization of the polar organizer protein FimV inJournal of bacteriology · 2026Article
- Regulatory RNA Ern0160 controls Enterococcus faecium virulence through direct modulation of expression of LysM domain-containing proteins.BMC genomics · 2026Article
- Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025Review
- Lysosomal control of proteostasis and reproductive capacity by conserved LMD-3 protein inScience advances · 2025Article
- Uncovering differential tolerance to deletions versus substitutions with a protein language model.Cell systems · 2025Article
- Solid-Phase Oligosaccharide Synthesis with Highly Complexed Peptidoglycan Fragments.Molecules (Basel, Switzerland) · 2025Article
- Enterococcal cell wall remodelling underpins pathogenesis via the release of the Enteroccocal Polysaccharide Antigen (EPA).PLoS pathogens · 2025Article
- A Nasal Vaccine Displaying Anthrax Antigen on the Surface ofJournal of microbiology and biotechnology · 2025Article
- Characterization of the host specificity of the SH3 cell wall binding domain of the staphylococcal phage 88 endolysin.Archives of microbiology · 2025Article
- Predicting receptor-ligand pairing preferences in plant-microbe interfaces via molecular dynamics and machine learning.Computational and structural biotechnology journal · 2025Article
51 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.