ArticleBMC microbiology2012
Anti-staphylococcal activities of lysostaphin and LytM catalytic domain.
Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- The "Cins" of Our Fathers: Rejuvenated Interest in Colicins to Combat Drug Resistance.Journal of microbiology (Seoul, Korea) · 2023Review
- Influence of NaCl and pH on lysostaphin catalytic activity, cell binding, and bacteriolytic activity.Applied microbiology and biotechnology · 2022Article
- Electrostatic Interaction with the Bacterial Cell Envelope Tunes the Lytic Activity of Two Novel Peptidoglycan Hydrolases.Microbiology spectrum · 2022Article
- A LytM-Domain Factor, ActS, Functions in Two Distinctive Peptidoglycan Hydrolytic Pathways inFrontiers in microbiology · 2022Article
- Improved antimicrobial spectrum of the N-acetylmuramoyl-L-alanine amidase from Latilactobacillus sakei upon LysM domain deletion.World journal of microbiology & biotechnology · 2021Article
- Structural Characterization of EnpA D,L-Endopeptidase fromInternational journal of molecular sciences · 2021Article
- ActS activates peptidoglycan amidases during outer membrane stress in Escherichia coli.Molecular microbiology · 2021Article
- Article
- Electrostatic-Mediated Affinity Tuning of Lysostaphin Accelerates Bacterial Lysis Kinetics and EnhancesAntimicrobial agents and chemotherapy · 2021Article
- Two New M23 Peptidoglycan Hydrolases With Distinct Net Charge.Frontiers in microbiology · 2021Article
- Molecular Characterization of a Novel Lytic Enzyme LysC fromInternational journal of molecular sciences · 2020Article
- YycH and YycI Regulate Expression ofMicroorganisms · 2020Article
- Cell-Wall Hydrolases as Antimicrobials against Staphylococcus Species: Focus on Sle1.Microorganisms · 2019Article
- Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.Frontiers in microbiology · 2019Review
- Hydrogel delivery of lysostaphin eliminates orthopedic implant infection byProceedings of the National Academy of Sciences of the United States of America · 2018Article
- 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
- Fusion with a cell wall binding domain renders autolysin LytM a potent anti-Staphylococcus aureus agent.FEMS microbiology letters · 2015Article
- Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.The FEBS journal · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
Abstract
backgroundLysostaphin and the catalytic domain of LytM cleave pentaglycine crossbridges of Staphylococcus aureus peptidoglycan. The bacteriocin lysostaphin is secreted by Staphylococcus simulans biovar staphylolyticus and directed against the cell walls of competing S. aureus. LytM is produced by S. aureus as a latent autolysin and can be activated in vitro by the removal of an N-terminal domain and occluding region.
resultsWe compared the efficacies of the lysostaphin and LytM catalytic domains using a newly developed model of chronic S. aureus infected eczema. Lysostaphin was effective, like in other models. In contrast, LytM was not significantly better than control. The different treatment outcomes could be correlated with in vitro properties of the proteins, including proteolytic stability, affinity to cell wall components other than peptidoglycan, and sensitivity to the ionic milieu.
conclusionsAlthough lysostaphin and LytM cleave the same peptide bond in the peptidoglycan, the two enzymes have very different environmental requirements what is reflected in their contrasting performance in mouse eczema model.
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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.