A Novel High-Molecular-Mass Bacteriocin Produced by Enterococcus faecium : Biochemical Features and Mode of Action
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A Novel High-Molecular-Mass Bacteriocin Produced by Enterococcus faecium: Biochemical Features and Mode of Action A. S. Vasilchenko 1
&
A.V. Vasilchenko 1 & A.V. Valyshev 2 & E.A. Rogozhin 3,4
# Springer Science+Business Media, LLC, part of Springer Nature 2018
Abstract Discovery of a novel bacteriocin is always an event in sciences, since cultivation of most bacterial species is a general problem in microbiology. This statement is reflected by the fact that number of bacteriocins is smaller for tenfold comparing to known antimicrobial peptides. We cultivated Enterococcus faecium on simplified medium to reduce amount of purification steps. This approach allows to purify the novel heavy weight bacteriocin produced by E. faecium ICIS 7. The novelty of this bacteriocin, named enterocin-7, was confirmed by N-terminal sequencing and by comparing the structural-functional properties with available data. Purified enterocin-7 is characterized by a sequence of amino acid residues having no homology in UniProt/SwissProt/TrEMBL databases: NH2 - Asp - Ala - His - Leu - Ser - Glu - Val - Ala - Glu - Arg - Phe - Glu - Asp - Leu - Gly. Isolated thermostable protein has a molecular mass of 65 kDa, which allows it to be classified into class III in bacteriocin classification schemes. Enterocin-7 displayed a broad spectrum of activity against some Gram-positive and Gram-negative microorganisms. Fluorescent microscopy and spectroscopy showed the permeabilizing mechanism of the action of enterocin-7, which is realized within a few minutes. Keywords Bacteriocin . Enterocin . Enterococcus . Class III . Antimicrobial peptides . Liquid chromatography
Introduction During evolution, microorganisms acquire an effective chemical arsenal that regulates inter-microbial relationships in communities. Bacteriocins are biologically active protein moieties, which determine antagonistic activity of bacteria and play a significant role in the ability to widespread [1]. According to their structural and functional characteristics, bacteriocins can be related to antimicrobial peptides (AMPs) produced by eukaryotes. Meanwhile bacteriocins are a relatively small group compared to other AMPs, since they are included in about 10% of the total known * A. S. Vasilchenko [email protected] 1
Tyumen State University, Volodarsky st, 6, Tyumen, Russian Federation 625003
2
Institute of Cellular and Intracellular Symbiosis, RAS, Pionerskaya st, 11, Orenburg, Russian Federation 460000
3
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, RAS, Miklukho-Maklaya st, 16/10, Moscow, Russian Federation 117997
4
Gause Institute of New Antibiotics, Bolshaya Pirogovskaya st, 11, Moscow, Russian Federation 119021
AMPss [2]. This disparity is due to the fact that most bacterial species are uncultivated in laboratory conditions [3]; in addition, separation of bacteriocins from microbial metabolites is an another problem [4]. Partial solution of stated problems is provided by searching for new bacteriocins using genome database mining approach [5, 6]. N
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