Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition
- Authors
- Yu, Jun-Hyeok; Park, Do-Won; Lim, Jeong-A.; Park, Jong-Hyun
- Issue Date
- Sep-2021
- Publisher
- MICROBIOLOGICAL SOCIETY KOREA
- Keywords
- Staphylococcus aureus; bacteriophage; endolysin; LysK; biofilm
- Citation
- JOURNAL OF MICROBIOLOGY, v.59, no.9, pp.840 - 847
- Journal Title
- JOURNAL OF MICROBIOLOGY
- Volume
- 59
- Number
- 9
- Start Page
- 840
- End Page
- 847
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/81972
- DOI
- 10.1007/s12275-021-1242-1
- ISSN
- 1225-8873
- 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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