How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides

0482244 - ÚOCHB 2018 RIV GB eng J - Článek v odborném periodiku
Nešuta, Ondřej - Buděšínský, Miloš - Hadravová, Romana - Monincová, Lenka - Humpolíčková, Jana - Čeřovský, Václav
How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides.
Pathogens and Disease. Roč. 75, č. 7 (2017), č. článku ftx091. ISSN 2049-632X. E-ISSN 2049-632X
Grant CEP: GA TA ČR(CZ) TA04010638; GA MZd(CZ) NV16-27726A
Institucionální podpora: RVO:61388963
Klíčová slova: antimicrobial peptides * biofilm * C-terminal deamidation * gelatinase * protease
Obor OECD: Microbiology
Impakt faktor: 2.337, rok: 2017

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.
Trvalý link: http://hdl.handle.net/11104/0277623