Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition
DC Field | Value | Language |
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dc.contributor.author | Yu, Jun-Hyeok | - |
dc.contributor.author | Park, Do-Won | - |
dc.contributor.author | Lim, Jeong-A. | - |
dc.contributor.author | Park, Jong-Hyun | - |
dc.date.accessioned | 2021-08-31T08:40:18Z | - |
dc.date.available | 2021-08-31T08:40:18Z | - |
dc.date.created | 2021-08-20 | - |
dc.date.issued | 2021-09 | - |
dc.identifier.issn | 1225-8873 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/81972 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | MICROBIOLOGICAL SOCIETY KOREA | - |
dc.relation.isPartOf | JOURNAL OF MICROBIOLOGY | - |
dc.title | Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000684464300001 | - |
dc.identifier.doi | 10.1007/s12275-021-1242-1 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY, v.59, no.9, pp.840 - 847 | - |
dc.identifier.kciid | ART002748672 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-85112383989 | - |
dc.citation.endPage | 847 | - |
dc.citation.startPage | 840 | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY | - |
dc.citation.volume | 59 | - |
dc.citation.number | 9 | - |
dc.contributor.affiliatedAuthor | Yu, Jun-Hyeok | - |
dc.contributor.affiliatedAuthor | Park, Do-Won | - |
dc.contributor.affiliatedAuthor | Park, Jong-Hyun | - |
dc.type.docType | Article; Early Access | - |
dc.subject.keywordAuthor | Staphylococcus aureus | - |
dc.subject.keywordAuthor | bacteriophage | - |
dc.subject.keywordAuthor | endolysin | - |
dc.subject.keywordAuthor | LysK | - |
dc.subject.keywordAuthor | biofilm | - |
dc.subject.keywordPlus | BACTERIOPHAGE ENDOLYSINS | - |
dc.subject.keywordPlus | BIOCONTROL AGENT | - |
dc.subject.keywordPlus | LYTIC ACTIVITY | - |
dc.subject.keywordPlus | AUREUS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | FOOD | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | LYSIS | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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