ArticleJournal of microbiology (Seoul, Korea)2021
Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition.
Article in Journal of microbiology (Seoul, Korea), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The trial behind it
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Bacteriophage lysins: a promising strategy for combating foodborne pathogens in food safety.Frontiers in microbiology · 2026Review
- Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025Review
- ZAM-CS, a novel chimeric endolysin with enhanced stability and rapid action against methicillin-resistant Staphylococcus aureus.BMC microbiology · 2025Article
- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Phage-Derived Endolysins Against Resistant Staphylococcus spp.: A Review of Features, Antibacterial Activities, and Recent Applications.Infectious diseases and therapy · 2025Review
- A Novel Truncated CHAP Modular Endolysin, CHAPJournal of microbiology and biotechnology · 2024Article
- Molecular Machinery of the Triad Holin, Endolysin, and Spanin: Key Players Orchestrating Bacteriophage-Induced Cell Lysis and their Therapeutic Applications.Protein and peptide letters · 2024Review
- Therapeutic potential of bacteriophage endolysins for infections caused by Gram-positive bacteria.Journal of biomedical science · 2023Review
- Endolysin, a Promising Solution against Antimicrobial Resistance.Antibiotics (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endolysin, a peptidoglycan hydrolase derived from bacteriophage, has been suggested as an alternative antimicrobial agent. Many endolysins on staphylococcal phages have been identified and applied extensively against Staphylococcus spp. Among them, LysK-like endolysin, a well-studied staphylococcal endolysin, accounts for most of the identified endolysins. However, relatively little interest has been paid to LysKunlike endolysin and a few of them has been characterized. An endolysin LysSAP33 encoded on bacteriophage SAP33 shared low homology with LysK-like endolysin in sequence by 41% and domain composition (CHAP-unknown CBD). A green fluorescence assay using a fusion protein for LysSAP33_CBD indicated that the CBD domain (157-251 aa) was bound to the peptidoglycan of S. aureus. The deletion of LysSAP33_CBD at the C-terminal region resulted in a significant decrease in lytic activity and efficacy. Compared to LysK-like endolysin, LysSAP33 retained its lytic activity in a broader range of temperature, pH, and NaCl concentrations. In addition, it showed a higher activity against biofilms than LysK-like endolysin. This study could be a helpful tool to develop our understanding of staphylococcal endolysins not belonging to LysK-like endolysins and a potential biocontrol agent against biofilms.
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