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Modular Engineering of Lysostaphin with Significantly Improved Stability and Bioavailability for Treating MRSA Infections.
ACS Appl Mater Interfaces
January 2025
State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China.
Methicillin-resistant (MRSA) is a refractory pneumonia-causing pathogen due to the antibiotic resistance and the characteristics of persisting inside its host cell. Lysostaphin is a typical bacteriolytic enzyme for degrading bacterial cell walls via hydrolysis of pentaglycine cross-links, showing potential to combat multidrug-resistant bacteria. However, there are still grand challenges for native lysostaphin because of its poor shelf stability and limited bioavailability.
View Article and Find Full Text PDF[Effect of enzybiotics on the healing of Staphylococcus aureus-infected skin wounds in a pig model].
Klin Mikrobiol Infekc Lek
March 2024
Department of Infectious Diseases and Preventive Medicine, Research Institute of Veterinary Medicine, Brno, Czech Republic, e-mail:
Introduction: Staphylococcus aureus is a gram-positive, facultatively anaerobic coccus capable of causing infectious diseases in animals and humans. Especially dangerous are multidrug-resistant forms with poor or even no response to available treatments.
Objectives: The study aimed to verify the effect of enzybiotics on the healing of S.
Characterization and bioinformatic analysis of a new chimeric endolysin against MRSA with great stability.
AMB Express
December 2024
Department of Biotechnology, Iranian Research Organization for Science and Technology (IROST), Tehran, Iran.
Antibiotics become less effective in treating infectious diseases as resistance increases. Staphylococcus aureus is a global problem due to its ability to form biofilms and resistance mechanisms. Phage endolysin is one of the most promising methods for combating antibiotic resistance.
View Article and Find Full Text PDFReassessing the substrate specificities of the major peptidoglycan hydrolases lysostaphin and LytM.
Elife
November 2024
Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyväskylä, Finland.
Orchestrated action of peptidoglycan (PG) synthetases and hydrolases is vital for bacterial growth and viability. Although the function of several PG synthetases and hydrolases is well understood, the function, regulation, and mechanism of action of PG hydrolases characterised as lysostaphin-like endopeptidases have remained elusive. Many of these M23 family members can hydrolyse glycyl-glycine peptide bonds and show lytic activity against whose PG contains a pentaglycine bridge, but their exact substrate specificity and hydrolysed bonds are still vaguely determined.
View Article and Find Full Text PDFDeleterious Effects of Histidine Tagging to the SH3b Cell Wall-Binding Domain on Recombinant Endolysin Activity.
J Microbiol Biotechnol
November 2024
Laboratory of Poultry Medicine, Department of Farm Animal Medicine, College of Veterinary Medicine and BK21 PLUS for Veterinary Science, Seoul National University, Seoul 08826, Republic of Korea.
Natural and artificial endolysins exhibit bactericidal effects by destroying peptidoglycans in the cell wall of gram-positive bacteria and are usually composed of an N-terminal catalytic domain (CTD) and a C-terminal cell wall-binding domain (CBD). The structures and receptors of CBDs are variable, but bacterial Src homology 3 (SH3b) CBDs are prevalent among the natural endolysins of . Moreover, although recombinant endolysins with a C-terminal 6x histidine tag (His-tag) are often produced and convenient to purify, the deleterious effects of His-tags on antibacterial activity have not been evaluated thoroughly.
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