ArticleApplied and environmental microbiology1995
The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus.
Article in Applied and environmental microbiology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.
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46 citing papers in PubMed, 105 citations in OpenAlex.
- Establishment of a human osteocyte model to reveal mechanisms of chronic Staphylococcus epidermidis bone and joint infections.Bone & joint research · 2026Article
- Turbid but accurate: automating lysostaphin quantification including uncertainty quantification.Microbial cell factories · 2026Article
- A bacteriolysin of Lactococcus carnosus is potentially involved in mediating contact-dependent antagonism against Listeria monocytogenes.Scientific reports · 2025Article
- Bactericidal activities and biochemical features of 16 antimicrobial peptides against bovine-mastitis causative pathogens.Veterinary research · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Article
- Staphylococcus aureus sacculus mediates activities of M23 hydrolases.Nature communications · 2023Article
- Treating Bacterial Infections with Bacteriophage-Based Enzybiotics: In Vitro, In Vivo and Clinical Application.Antibiotics (Basel, Switzerland) · 2021Review
- A Simple Protocol for the Determination of Lysostaphin Enzymatic Activity.Antibiotics (Basel, Switzerland) · 2020Article
- FmhA and FmhC ofThe Journal of biological chemistry · 2020Article
- Production of Lysostaphin by Nonproprietary Method Utilizing a Promoter from Toxin-Antitoxin System.Molecular biotechnology · 2019Article
- In Vitro Activity of the Bacteriophage Endolysin HY-133 againstInternational journal of molecular sciences · 2019Article
- Potential for Bacteriophage Endolysins to Supplement or Replace Antibiotics in Food Production and Clinical Care.Antibiotics (Basel, Switzerland) · 2018Review
- Corrected and Republished from: Identification of Peptidoglycan Hydrolase Constructs with Synergistic Staphylolytic Activity in Cow's Milk.Applied and environmental microbiology · 2018Article
- Identification of Peptidoglycan Hydrolase Constructs with Synergistic Staphylolytic Activity in Cow's Milk.Applied and environmental microbiology · 2017Article
- Teichoic Acid Polymers Affect Expression and Localization of dl-Endopeptidase LytE Required for Lateral Cell Wall Hydrolysis in Bacillus subtilis.Journal of bacteriology · 2016Article
- Bacteriocin protein BacL1 of Enterococcus faecalis targets cell division loci and specifically recognizes L-Ala2-cross-bridged peptidoglycan.Journal of bacteriology · 2015Article
- Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128: Comparison to recombinant lysostaphin.Bacteriophage · 2013Article
- Staphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'.Journal of biotechnology · 2012Article
- Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity.Probiotics and antimicrobial proteins · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus simulans biovar staphylolyticus produces an extracellular glycylglycine endopeptidase (lysostaphin) that lyses other staphylococci by hydrolyzing the cross bridges in their cell wall peptidoglycans. The genes for endopeptidase (end) and endopeptidase resistance (epr) reside on plasmid pACK1. An 8.4-kb fragment containing end was cloned into shuttle vector pL150 and was then introduced into Staphylococcus aureus RN4220. The recombinant S. aureus cells produced endopeptidase and were resistant to lysis by the enzyme, which indicated that the cloned fragment also contained epr. Treatments to remove accessory wall polymers (proteins, teichoic acids, and lipoteichoic acids) did not change the endopeptidase sensitivity of walls from strains of S. simulans biovar staphylolyticus or of S. aureus with and without epr. Immunological analyses of various wall fractions showed that there were epitopes associated with endopeptidase resistance and that these epitopes were found only on the peptidoglycans of epr+ strains of both species. Treatment of purified peptidoglycans with endopeptidase confirmed that resistance or susceptibility of both species was a property of the peptidoglycan itself. A comparison of the chemical compositions of these peptidoglycans revealed that cross bridges in the epr+ cells contained more serine and fewer glycine residues than those of cells without epr. The presence of the 8.4-kb fragment from pACK1 also increased the susceptibility of both species to methicillin.
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