Detailed Information on Publication Record
2023
Antimicrobial effect of endolysins LYSDERM‐S and LYSDERM‐T1 and endolysin‐ubiquitin combination on methicillin‐resistant Staphylococcus aureus
VACEK, Lukáš, Michaela KOUŘILOVÁ, Šárka KOBZOVÁ and Lubomír JANDABasic information
Original name
Antimicrobial effect of endolysins LYSDERM‐S and LYSDERM‐T1 and endolysin‐ubiquitin combination on methicillin‐resistant Staphylococcus aureus
Authors
VACEK, Lukáš (203 Czech Republic, belonging to the institution), Michaela KOUŘILOVÁ (203 Czech Republic), Šárka KOBZOVÁ (203 Czech Republic) and Lubomír JANDA (203 Czech Republic, guarantor)
Edition
BIOLOGIA, NEW YORK, SPRINGER, 2023, 0006-3088
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10606 Microbiology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 1.500 in 2022
RIV identification code
RIV/00216224:14110/23:00134618
Organization unit
Faculty of Medicine
UT WoS
000894986000002
Keywords in English
Endolysin;Ubiquitin;LYSDERM-S;LYSDERM-T1;Staphylococcus aureus;MRSA
Tags
International impact, Reviewed
Změněno: 24/2/2023 08:14, Mgr. Tereza Miškechová
Abstract
V originále
Bacterial resistance is a major issue in the modern world, and Staphylococcus aureus is one of these well-known multi-resistant species. Staphylococcal infections are one of the leading causes of infection in humans and are becoming more challenging to treat by conventional methods. Endolysins, a novel class of antibacterial agents, are bacteriophage-encoded lytic enzymes capable of degrading peptidoglycan and thus able to kill bacteria. This study aimed to study endolysin LYSDERM-S (a variant of endolysin LysF1 optimized for heterologous expression in E. coli) and newly prepared thermally stabilized endolysin LYSDERM-T1 (with a mutation in the CHAP domain) both with (LYSDERM-US, LYSDERM-UT1) and without fused ubiquitin and determine its role in protein expression and antibacterial activity. The results showed that fused endolysin-ubiquitin proteins did not exceed the antimicrobial effect of endolysins alone, but cleaved endolysin-ubiquitin proteins possessed longer lasting antimicrobial effect than endolysin alone. The biobetter endolysin LYSDERM-T1 with higher thermal stability showed a prolonged antimicrobial effect. Further, we showed that ubiquitin alone possesses antimicrobial properties. Minimal inhibitory and bactericidal concentrations (MIC and MBC) were assessed and confirmed that ubiquitin is able to increase the antimicrobial potential of endolysins. Biobetter endolysins or endolysin-ubiquitin combinations could serve as an alternative to well-established antimicrobial therapy for methicillin-resistant S. aureus infections.
Links
NU22-05-00475, research and development project |
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