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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027162%3A_____%2F23%3AN0000008" target="_blank" >RIV/00027162:_____/23:N0000008 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00159816:_____/23:00078674 RIV/00216224:14110/23:00134618

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 LysF1 and newly prepared thermally stabilized endolysin LysT1 both with 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 endolysin LysT1 with higher thermal stability showed a better 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. Endolysin or endolysin-ubiquitin combination could serve as an alternative to well-established antimicrobial therapy for methicillin-resistant S. aureus infections.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 LysF1 and newly prepared thermally stabilized endolysin LysT1 both with 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 endolysin LysT1 with higher thermal stability showed a better 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. Endolysin or endolysin-ubiquitin combination could serve as an alternative to well-established antimicrobial therapy for methicillin-resistant S. aureus infections.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

Biologia

ISSN

0006-3088

e-ISSN

1336-9563

Svazek periodika

78

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

601-608

Kód UT WoS článku

000894986000002

EID výsledku v databázi Scopus

2-s2.0-85143397420