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How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides
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SYSNO ASEP 0482244 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides Tvůrce(i) Nešuta, Ondřej (UOCHB-X) RID, ORCID
Buděšínský, Miloš (UOCHB-X) RID, ORCID
Hadravová, Romana (UOCHB-X) RID, ORCID
Monincová, Lenka (UOCHB-X)
Humpolíčková, Jana (UOCHB-X) ORCID
Čeřovský, Václav (UOCHB-X) RID, ORCIDČíslo článku ftx091 Zdroj.dok. Pathogens and Disease - ISSN 2049-632X
Roč. 75, č. 7 (2017)Poč.str. 12 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova antimicrobial peptides ; biofilm ; C-terminal deamidation ; gelatinase ; protease Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP TA04010638 GA TA ČR - Technologická agentura ČR NV16-27726A GA MZd - Ministerstvo zdravotnictví Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000414395500012 EID SCOPUS 85037057931 DOI 10.1093/femspd/ftx091 Anotace HYL-20 (GILSSLWKKLKKIIAK-NH2) is an analogue of a natural antimicrobial peptide (AMP) previously isolated from the venom of wild bee. We examined its antimicrobial activity against three strains of Enterococcus faecalis while focusing on its susceptibility to proteolytic degradation by two known proteases-gelatinase (GelE) and serine protease (SprE)-which are secreted by these bacterial strains. We found that HYL-20 was primarily deamidated at its C-terminal which made the peptide susceptible to consecutive intramolecular cleavage by GelE. Further study utilising 1,10-phenanthroline, a specific GelE inhibitor and analogous peptide with D-Lys at its C-terminus (HYL-20k) revealed that the C-terminal deamidation of HYL-20 is attributed to not yet unidentified protease which also cleaves internal peptide bonds of AMPs. In contrast to published data, participation of SprE in the protective mechanism of E. faecalis against AMPs was not proved. The resistance of HYL-20k to C-terminal deamidation and subsequent intramolecular cleavage has resulted in increased antimicrobial activity against E. faecalis grown in planktonic and biofilm form when compared to HYL-20. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2018
Počet záznamů: 1