Antimicrobial susceptibility testing of thermally stabilized endolysins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027162%3A_____%2F21%3AN0000240" target="_blank" >RIV/00027162:_____/21:N0000240 - isvavai.cz</a>

Výsledek na webu

<a href="http://symma.cz/hojeniran/down/hojeniran2021_program.pdf" target="_blank" >http://symma.cz/hojeniran/down/hojeniran2021_program.pdf</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Antimicrobial susceptibility testing of thermally stabilized endolysins

Popis výsledku v původním jazyce

Endolysins are phage-encoded peptidoglycan hydrolases that play an essential role in the release of the phage progeny to the environment while destroying the bacterial cell. Endolysins display strong lytic activity, particularly in Gram-positive bacteria with no protective outer cell membrane. In our study, we aim to improve the thermal stability of these enzymes to achieve better antimicrobial properties. Existing endolysin F1 was altered employing protein engineering, and stabilizing mutations were introduced into the structure. An increase in the thermal stability of novel enzymes was verified by a thermal shift assay. Antimicrobial susceptibility testing was performed by recording bacterial growth curves over 24-hour cultivation of two methicillin-resistant Staphylococcus aureus strains for each enzyme variant in concentrations ranging from 0.78 to 50 µg/mL. These measurements confirmed that the introduction of stabilizing mutations improved antimicrobial properties. Modified endolysins proved to be more stable in time (the antimicrobial effect lasted longer, up to 20 hours), and lower concentrations were needed to reduce bacterial counts (3 µg/mL). These results will help the effort to use endolysins in the fields of medicine and biotechnology.

Název v anglickém jazyce

Antimicrobial susceptibility testing of thermally stabilized endolysins

Popis výsledku anglicky

Endolysins are phage-encoded peptidoglycan hydrolases that play an essential role in the release of the phage progeny to the environment while destroying the bacterial cell. Endolysins display strong lytic activity, particularly in Gram-positive bacteria with no protective outer cell membrane. In our study, we aim to improve the thermal stability of these enzymes to achieve better antimicrobial properties. Existing endolysin F1 was altered employing protein engineering, and stabilizing mutations were introduced into the structure. An increase in the thermal stability of novel enzymes was verified by a thermal shift assay. Antimicrobial susceptibility testing was performed by recording bacterial growth curves over 24-hour cultivation of two methicillin-resistant Staphylococcus aureus strains for each enzyme variant in concentrations ranging from 0.78 to 50 µg/mL. These measurements confirmed that the introduction of stabilizing mutations improved antimicrobial properties. Modified endolysins proved to be more stable in time (the antimicrobial effect lasted longer, up to 20 hours), and lower concentrations were needed to reduce bacterial counts (3 µg/mL). These results will help the effort to use endolysins in the fields of medicine and biotechnology.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10606 - Microbiology

Projekt

<a href="/cs/project/NV19-05-00214" target="_blank" >NV19-05-00214: Studium terapeutické aplikace antibakteriálního krytí rány pro infekce kůže a měkkých tkání u epidemiologicky relevantních kmenů S. aureus - rezistentních na meticilin.</a><br>

Návaznosti

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

Rok uplatnění

2021

Kód důvěrnosti údajů

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