5MMK

HYL-20

5MMK の概要

• エントリーDOI: 10.2210/pdb5mmk/pdb
• NMR情報: BMRB: 34074
• 分子名称: GLY-ILE-LEU-SER-SER-LEU-TRP-LYS-LYS-LEU-LYS-LYS-ILE-ILE-ALA-LYS (1 entity in total)
• 機能のキーワード: antimicrobial peptide, antimicrobial protein
• 由来する生物種: Hylaeus signatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1829.36

構造登録者

Hexnerova, R. (登録日: 2016-12-10, 公開日: 2017-09-06, 最終更新日: 2024-11-20)

主引用文献

Nesuta, O.,Budesinsky, M.,Hadravova, R.,Monincova, L.,Humpolickova, J.,Cerovsky, V.
How proteases from Enterococcus faecalis contribute to its resistance to short alpha-helical antimicrobial peptides.
Pathog Dis, 75:-, 2017

PubMed Abstract: 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.

PubMed: 28830077
DOI: 10.1093/femspd/ftx091

実験手法

SOLUTION NMR