Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition

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...

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Bibliographic Details
Published in:The journal of microbiology 2021, 59(9), , pp.840-847
Main Authors: Yu, Jun-Hyeok, Park, Do-Won, Lim, Jeong-A, Park, Jong-Hyun
Format: Article
Language:English
Subjects:
Antiinfectives and antibacterials
Antimicrobial agents
Biofilms
Biological control
Biomedical and Life Sciences
Composition
Domains
Fluorescence
Fusion protein
Genomics and Molecular Biology
Homology
Hydrolase
Identification
Life Sciences
Microbial Genetics
Microbiology
Peptidoglycan hydrolase
Phages
Sodium chloride
Staphylococcus aureus
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Summary: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.
ISSN:1225-8873
1976-3794
DOI:10.1007/s12275-021-1242-1