How proteases from Enterococcus faecalis contribute to its resistance to short α-helical antimicrobial peptides
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
28830077
DOI
10.1093/femspd/ftx091
PII: 4056144
Knihovny.cz E-resources
- Keywords
- C-terminal deamidation, antimicrobial peptides, biofilm, gelatinase, protease,
- MeSH
- Anti-Bacterial Agents chemical synthesis metabolism pharmacology MeSH
- Bacterial Proteins antagonists & inhibitors chemistry metabolism MeSH
- Biofilms drug effects growth & development MeSH
- Enterococcus faecalis drug effects enzymology growth & development ultrastructure MeSH
- Phenanthrolines pharmacology MeSH
- Enzyme Inhibitors pharmacology MeSH
- Antimicrobial Cationic Peptides chemical synthesis metabolism pharmacology MeSH
- Microbial Sensitivity Tests MeSH
- Plankton drug effects enzymology growth & development ultrastructure MeSH
- Proteolysis MeSH
- Amino Acid Sequence MeSH
- Serine Endopeptidases chemistry metabolism MeSH
- Amino Acid Substitution MeSH
- Bees chemistry physiology MeSH
- Structure-Activity Relationship MeSH
- Gelatinases antagonists & inhibitors chemistry metabolism MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 1,10-phenanthroline MeSH Browser
- Anti-Bacterial Agents MeSH
- Bacterial Proteins MeSH
- Phenanthrolines MeSH
- Enzyme Inhibitors MeSH
- Antimicrobial Cationic Peptides MeSH
- Serine Endopeptidases MeSH
- Gelatinases MeSH
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.
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