Antimicrobial effect of endolysins LYSDERM-S and LYSDERM-T1 and endolysin-ubiquitin combination on methicillin-resistant Staphylococcus aureus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F23%3A00078674" target="_blank" >RIV/00159816:_____/23:00078674 - isvavai.cz</a>

Alternative codes found

RIV/00027162:_____/23:N0000008 RIV/00216224:14110/23:00134618

Result on the web

<a href="https://link.springer.com/article/10.1007/s11756-022-01282-6" target="_blank" >https://link.springer.com/article/10.1007/s11756-022-01282-6</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11756-022-01282-6" target="_blank" >10.1007/s11756-022-01282-6</a>

Result language

angličtina

Original language name

Antimicrobial effect of endolysins LYSDERM-S and LYSDERM-T1 and endolysin-ubiquitin combination on methicillin-resistant Staphylococcus aureus

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10600 - Biological sciences

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2023

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biologia

ISSN

0006-3088

e-ISSN

1336-9563

Volume of the periodical

78

Issue of the periodical within the volume

2

Country of publishing house

SK - SLOVAKIA

Number of pages

8

Pages from-to

601-608

UT code for WoS article

000894986000002

EID of the result in the Scopus database

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