ArticleJournal of bacteriology2008
Detection and localization of single LysM-peptidoglycan interactions.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- A novel bacterium-like particles platform displaying antigens by new anchoring proteins induces efficacious immune responses.Frontiers in microbiology · 2024Article
- Screening for New Surface Anchoring Domains forFrontiers in microbiology · 2019Article
- Peptidoglycan Muropeptides: Release, Perception, and Functions as Signaling Molecules.Frontiers in microbiology · 2019Review
- LysMD3 is a type II membrane protein without anThe Journal of biological chemistry · 2018Article
- Chitin oligosaccharide binding to the lysin motif of a novel type of chitinase from the multicellular green alga, Volvox carteri.Plant molecular biology · 2017Article
- Identification of a supramolecular functional architecture of Streptococcus mutans adhesin P1 on the bacterial cell surface.The Journal of biological chemistry · 2015Article
- Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications.Applied microbiology and biotechnology · 2014Review
- Binding mechanism of the peptidoglycan hydrolase Acm2: low affinity, broad specificity.Biophysical journal · 2013Article
- O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity.The Journal of biological chemistry · 2013Article
- Critical cell wall hole size for lysis in Gram-positive bacteria.Journal of the Royal Society, Interface · 2013Article
- Measuring kinetic dissociation/association constants between Lactococcus lactis bacteria and mucins using living cell probes.Biophysical journal · 2011Article
- Murein and pseudomurein cell wall binding domains of bacteria and archaea--a comparative view.Applied microbiology and biotechnology · 2011Review
- Immunoproteomic assay of secreted proteins of Streptococcus suis serotype 9 with convalescent sera from pigs.Folia microbiologica · 2011Article
- Recognition of pathogenic microbes by the Drosophila phagocytic pattern recognition receptor Eater.The Journal of biological chemistry · 2011Article
- Exoproteome of Staphylococcus aureus reveals putative determinants of nasal carriage.Journal of proteome research · 2011Article
- A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains.Molecular microbiology · 2010Article
- Imaging the nanoscale organization of peptidoglycan in living Lactococcus lactis cells.Nature communications · 2010Article
- Nanoscale structural and mechanical properties of nontypeable Haemophilus influenzae biofilms.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lysin motif (LysM) is a ubiquitous protein module that binds peptidoglycan and structurally related molecules. Here, we used single-molecule force spectroscopy (SMFS) to measure and localize individual LysM-peptidoglycan interactions on both model and cellular surfaces. LysM modules of the major autolysin AcmA of Lactococcus lactis were bound to gold-coated atomic force microscopy tips, while peptidoglycan was covalently attached onto model supports. Multiple force curves recorded between the LysM tips and peptidoglycan surfaces yielded a bimodal distribution of binding forces, presumably reflecting the occurrence of one and two LysM-peptidoglycan interactions, respectively. The specificity of the measured interaction was confirmed by performing blocking experiments with free peptidoglycan. Next, the LysM tips were used to map single LysM interactions on the surfaces of L. lactis cells. Strikingly, native cells showed very poor binding, suggesting that peptidoglycan was hindered by other cell wall constituents. Consistent with this notion, treatment of the cells with trichloroacetic acid, which removes peptidoglycan-associated polymers, resulted in substantial and homogeneous binding of the LysM tip. These results provide novel insight into the binding forces of bacterial LysMs and show that SMFS is a promising tool for studying the heterologous display of proteins or peptides on bacterial surfaces.
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