ArticleNature chemical biology2020
Two-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 82 citations in OpenAlex.
- Eradication of MRSA biofilm-associated implant infections by low-immunogenic sustained-release lysostaphin fused to thermosensitive polypeptides.Nature communications · 2026Article
- Data mining reveals the diversity of prophage endolysins targeting pathogenic enterococci.The Journal of general virology · 2026Article
- Integrated computational and experimental benchmarking of Bacillus phage endolysins reveals the relationship between peptidoglycan-fragment recognition descriptors and antibacterial performance.Scientific reports · 2026Article
- Peculiarities of the Interaction of the Bacteriolytic Protease Blp fromInternational journal of molecular sciences · 2026Article
- Novel endopeptidase overcoming lysostaphin resistance.Scientific reports · 2026Article
- Designing the Next Generation of Endolysins: A Triple Strategy Integrating Bioinformatics Mining, Engineering Modification and Encapsulation Formulation.Probiotics and antimicrobial proteins · 2026Review
- Detection and identification of pathogens using agents targeting the bacterial cell wall.Folia microbiologica · 2026Review
- Comparative gut microbial enzyme functions in human amoebiasis: Implications for host-microbe interactions and veterinary parasitic models.Open veterinary journal · 2026Article
- Structural and functional analysis reveals the catalytic mechanism and substrate binding mode of the broad-spectrum endolysin Ply2741.Virulence · 2025Article
- The New SH3b_T Domain Increases the Structural and Functional Variability Among SH3b-Like CBDs from Staphylococcal Phage Endolysins.Probiotics and antimicrobial proteins · 2025Article
- A new bacteriolytic amidase Ami of Lysobacter capsici XL1.Scientific reports · 2025Article
- ZAM-CS, a novel chimeric endolysin with enhanced stability and rapid action against methicillin-resistant Staphylococcus aureus.BMC microbiology · 2025Article
- Characterization of the host specificity of the SH3 cell wall binding domain of the staphylococcal phage 88 endolysin.Archives of microbiology · 2025Article
- Piezoelectric biosensor with dissipation monitoring enables the analysis of bacterial lytic agent activity.Scientific reports · 2025Article
- Two-step localization driven by peptidoglycan hydrolase in interbacterial predation.The ISME journal · 2025Article
- Specifically targeted antimicrobial peptides synergize with bacterial-entrapping peptide against systemic MRSA infections.Journal of advanced research · 2025Article
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Characterization and bioinformatic analysis of a new chimeric endolysin against MRSA with great stability.AMB Express · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Engineering of chimeric enzymes with expanded tolerance to ionic strength.Microbiology spectrum · 2024Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Lysostaphin is a bacteriolytic enzyme targeting peptidoglycan, the essential component of the bacterial cell envelope. It displays a very potent and specific activity toward staphylococci, including methicillin-resistant Staphylococcus aureus. Lysostaphin causes rapid cell lysis and disrupts biofilms, and is therefore a therapeutic agent of choice to eradicate staphylococcal infections. The C-terminal SH3b domain of lysostaphin recognizes peptidoglycans containing a pentaglycine crossbridge and has been proposed to drive the preferential digestion of staphylococcal cell walls. Here we elucidate the molecular mechanism underpinning recognition of staphylococcal peptidoglycan by the lysostaphin SH3b domain. We show that the pentaglycine crossbridge and the peptide stem are recognized by two independent binding sites located on opposite sides of the SH3b domain, thereby inducing a clustering of SH3b domains. We propose that this unusual binding mechanism allows synergistic and structurally dynamic recognition of S. aureus peptidoglycan and underpins the potent bacteriolytic activity of this enzyme.
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Registered trials
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.