LysK is the endolysin from the staphylococcal bacteriophage K, and can digest the cell wall of many staphylococci. Lysostaphin is a bacteriocin secreted by Staphylococcus simulans to kill Staphylococcus aureus. Both LysK and lysostaphin have been shown to lyse methicillin-resistant S. aureus (MRSA). This study describes optimal reaction conditions for the recombinant His-tagged LysK protein (pH range pH 6-10, and 0.3-0.5 M NaCl), and C-His-LysK MIC (32.85+/-4.87 mug mL(-1)). LysK and lysostaphin demonstrate antimicrobial synergy by the checkerboard assay.
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http://dx.doi.org/10.1111/j.1574-6968.2008.01308.x | DOI Listing |
Antibiotics (Basel)
June 2021
Department of Biological Sciences, Munster Technological University, Cork T12 P928, Ireland.
Bacteriophage endolysins and their derivatives have strong potential as antibacterial agents considering the increasing prevalence of antibiotic resistance in common bacterial pathogens. The peptidoglycan degrading peptidase CHAPk, a truncated derivate of staphylococcal phage K endolysin (LysK), has proven efficacy in preventing and disrupting staphylococcal biofilms. Nevertheless, the concentration of CHAPk required to eliminate populations of stationary-phase cells was previously found to be four-fold higher than that for log-phase cells.
View Article and Find Full Text PDFFront Microbiol
March 2019
Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.
Bacteriophage endolysins and bacterial exolysins are capable of enzymatic degradation of the cell wall peptidoglycan layer and thus show promise as a new class of antimicrobials. Both exolysins and endolysins often consist of different modules, which are responsible for enzymatic functions and cell wall binding, respectively. Individual modules from different endo- or exolysins with different binding and enzymatic activities, can via gene fusion technology be re-combined into novel variants for investigations of arrangements of potential clinical interest.
View Article and Find Full Text PDFAntimicrob Agents Chemother
October 2018
Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York, USA.
The cell wall of Gram-positive bacteria contains abundant surface-exposed carbohydrate structures that are highly conserved. While these properties make surface carbohydrates ideal targets for immunotherapy, carbohydrates elicit a poor immune response that results primarily in low-affinity IgM antibodies. In a previous publication, we introduced the lysibody approach to address this shortcoming.
View Article and Find Full Text PDFAppl Biochem Biotechnol
October 2016
Department of Chemical Enzymology, Faculty of Chemistry, M.V. Lomonosov Moscow State University, Moscow, Russia.
A staphylolytic fusion protein (chimeric enzyme K-L) was created, harboring three unique lytic activities composed of the LysK CHAP endopeptidase, and amidase domains, and the lysostaphin glycyl-glycine endopeptidase domain. To assess the potential of possible therapeutic applications, the kinetic behavior of chimeric enzyme K-L was investigated. As a protein antimicrobial, with potential antigenic properties, the biophysical effect of including chimeric enzyme K-L in anionic polymer matrices that might help reduce the immunogenicity of the enzyme was tested.
View Article and Find Full Text PDFAnalyst
January 2014
Department of Biomedical Engineering, McGill University, 3775 university Street, Montreal, Quebec H3A 2B4, Canada.
Rapid, specific detection of pathogenic bacteria remains a major challenge in infectious disease diagnostics. Bacteriophages can show genus- or even species-level specificity and have been developed for biosensing purposes, but the possibility of using individual phage proteins for detection has not been fully explored. This work exploits the ability of specific phage proteins, the endolysins LysK and Φ11, and the bacteriocin lysostaphin, fixed on silicon wafers to bind staphylococci.
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