ArticleFEMS microbiology letters2015
Fusion with a cell wall binding domain renders autolysin LytM a potent anti-Staphylococcus aureus agent.
Article in FEMS microbiology letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Enhancing stability and safety of chimeric peptidoglycan hydrolases by linker engineering.Applied microbiology and biotechnology · 2026Article
- Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM.Biomolecular NMR assignments · 2024Article
- Influence of NaCl and pH on lysostaphin catalytic activity, cell binding, and bacteriolytic activity.Applied microbiology and biotechnology · 2022Article
- Molecular docking and proteomics reveals the synergistic antibacterial mechanism of theaflavin with β-lactam antibiotics against MRSA.Frontiers in microbiology · 2022Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Structural Investigations on the SH3b Domains ofMolecules (Basel, Switzerland) · 2021Article
- Structural Characterization of EnpA D,L-Endopeptidase fromInternational journal of molecular sciences · 2021Article
- Building blocks and blueprints for bacterial autolysins.PLoS computational biology · 2021Article
- Two New M23 Peptidoglycan Hydrolases With Distinct Net Charge.Frontiers in microbiology · 2021Article
- Surface display of p75, a Lactobacillus rhamnosus GG derived protein, on Bacillus subtilis spores and its antibacterial activity against Listeria monocytogenes.AMB Express · 2020Article
- LytU-SH3b fusion protein as a novel and efficient enzybiotic against methicillin-resistantMolecular biology research communications · 2019Article
- Interaction of host and Staphylococcus aureus protease-system regulates virulence and pathogenicity.Medical microbiology and immunology · 2019Review
- Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.Scientific reports · 2019Article
- ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain.Antimicrobial agents and chemotherapy · 2019Article
- Structural and Functional Insights Into Lysostaphin-Substrate Interaction.Frontiers in molecular biosciences · 2018Article
- Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.Scientific reports · 2017Article
- LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions.Microbial drug resistance (Larchmont, N.Y.) · 2016Article
- Discovery of novel S. aureus autolysins and molecular engineering to enhance bacteriolytic activity.Applied microbiology and biotechnology · 2015Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Despite intense efforts by the medical and pharmaceutical communities, Staphylococcus aureus continues to be a pervasive pathogen that causes a myriad of diseases and a high level of morbidity and mortality among infected patients. Thus, discovering or designing novel therapeutics able to kill both drug-resistant and drug-sensitive S. aureus remains a top priority. Bacteriolytic enzymes, mostly from phage, have shown great promise in preclinical studies, but little consideration has been given to cis-acting autolytic enzymes derived from the pathogen itself. Here, we use the S. aureus autolysin LytM as a proof of principal to demonstrate the antibacterial potential of endogenous peptidoglycan-degrading enzymes. While native LytM is only marginally bactericidal, fusion of LytM to the lysostaphin cell wall binding domain enhances its anti-staphylococcal activity approximately 540-fold, placing it on par with many phage lysins currently in preclinical development. The potential to therapeutically co-opt a pathogen's endogenous peptidoglycan recycling machinery opens the door to a previously untapped reservoir of antibacterial drug candidates.
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