Production of enterolysin A by rumen Enterococcus faecalis strain and occurrence of enlA homologues among ruminal Gram-positive cocci

Nigutová, Katarína; Morovský, Marcel; Pristaš, Peter; Teather, R. M.; Holo, Helge; Javorský, P.

doi:10.1111/j.1365-2672.2006.03068.x

Cited by 31 publications

(24 citation statements)

References 25 publications

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“…44,45 Our results indicate that the incidence of entA and also entL50A/B are frequently found in enterococcal isolates from dairy origin and are in line with these findings. Additionally, according to our previous study, same genes of bacteriocin have been found in human blood and fecal derived enterococci; it is rational to believe that because of the extensive distribution of enterococcal contamination in nature they are likely derived from the same environment and most probably from intestine of various animals.…”

Section: Screening Of Structural Bacteriocin Encoding Genes In Enterosupporting

confidence: 88%

Evaluation of Bacteriocin Activities among Enterococcal Poultry Isolates from East Azarbaijan Iran

Javaherzadeh¹,

Jamshidian²,

Zahraei³

et al. 2015

Pharm Sci

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Section: Screening Of Structural Bacteriocin Encoding Genes In Enterosupporting

confidence: 88%

Evaluation of Bacteriocin Activities among Enterococcal Poultry Isolates from East Azarbaijan Iran

Javaherzadeh¹,

Jamshidian²,

Zahraei³

et al. 2015

Pharm Sci

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“…Nigutova et al (56) first detected the presence of enterolysin homologues in 5 of the 33 isolates of E. faecalis isolated from the bovine rumen using primers designed to amplify the structural gene encoding enterolysin A.…”

Section: Discussionmentioning

confidence: 99%

Distribution and Genetic Diversity of Bacteriocin Gene Clusters in Rumen Microbial Genomes

Azevedo

Bento

Ruiz

et al. 2015

Appl Environ Microbiol

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b Some species of ruminal bacteria are known to produce antimicrobial peptides, but the screening procedures have mostly been based on in vitro assays using standardized methods. Recent sequencing efforts have made available the genome sequences of hundreds of ruminal microorganisms. In this work, we performed genome mining of the complete and partial genome sequences of 224 ruminal bacteria and 5 ruminal archaea to determine the distribution and diversity of bacteriocin gene clusters. A total of 46 bacteriocin gene clusters were identified in 33 strains of ruminal bacteria. Twenty gene clusters were related to lanthipeptide biosynthesis, while 11 gene clusters were associated with sactipeptide production, 7 gene clusters were associated with class II bacteriocin production, and 8 gene clusters were associated with class III bacteriocin production. The frequency of strains whose genomes encode putative antimicrobial peptide precursors was 14.4%. Clusters related to the production of sactipeptides were identified for the first time among ruminal bacteria. BLAST analysis indicated that the majority of the gene clusters (88%) encoding putative lanthipeptides contained all the essential genes required for lanthipeptide biosynthesis. Most strains of Streptococcus (66.6%) harbored complete lanthipeptide gene clusters, in addition to an open reading frame encoding a putative class II bacteriocin. Albusin B-like proteins were found in 100% of the Ruminococcus albus strains screened in this study. The in silico analysis provided evidence of novel biosynthetic gene clusters in bacterial species not previously related to bacteriocin production, suggesting that the rumen microbiota represents an underexplored source of antimicrobial peptides.T he production of low-molecular-weight antimicrobial peptides is a trait widely distributed among species of bacteria and archaea (1). Although a variety of functions has been assigned to these compounds (e.g., toxins, virulence factors, bacterial hormones), the bacteriocins have mainly been investigated due to their potential as alternatives to antibiotics and food preservatives (2-4). With the rise in antibiotic resistance among commensal and pathogenic strains of bacteria, there is an urgent need to identify and develop novel therapeutic strategies for clinical applications in human and animal health (5).Bacteriocins are often defined as ribosomally synthesized antimicrobial peptides produced by bacteria or archaea (6). Bacteriocins show great diversity in their chemical structures and mechanisms of action, and at least four main groups have been proposed to classify these antimicrobial agents (7). Class I contains posttranslationally modified antimicrobial peptides, such as lanthipeptides, sactipeptides, and lasso peptides, which differ in their molecular structures, their mechanisms of action, and the enzymatic apparatuses involved in modifying the precursor peptides (7,8). Class II bacteriocins consist of antimicrobial peptides without posttranslationally modified residues and ca...

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“…Afterwards, an EnlA homologue was found to be produced by Gram-positive ruminal cocci and enlA structural gene homologues were identified in several enterococcal and streptococcal bacterial species including Streptococcus bovis and Enterococcus malodoratus strains [18]. Enterolysin A belongs to group of PGHs with typical modular structure.…”

Section: Enterolysin Amentioning

confidence: 99%

“…The strain Enterococcus faecalis II/1 was used as the source of enterolysin A gene [18]. Most of enterococcal and streptococcal strains used in this study were described previously [18,19], all other bacterial strains were obtained from collection of microorganisms of our institute.…”

Section: Bacterial Strains and Growth Conditionsmentioning

confidence: 99%

Peptidoglycan Hydrolase Enterolysin A Recognizes Lipoteichoic Acid Chains in the Cell Walls of Sensitive Bacteria

Maliničová

Dubikova²,

Piknová³

et al. 2012

PPL

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C-terminal domain of peptidoglycan hydrolase enterolysin A (EnlA) is involved in specific recognition and binding to the target cell envelopes and represents true cell wall binding (CWB) domain. Sensitivity/resistance to EnlA is dependent on binding ability/disability of its CWB domain. We assume that main mechanism of resistance against EnlA is absence of the specific receptor on the cell surface, which is necessary for binding of the enzyme molecule. Using competitive and enzymatic assays we have uncovered the chemical nature of the EnlA receptor, which is a lipoteichoic acid.

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Production of enterolysin A by rumen Enterococcus faecalis strain and occurrence of enlA homologues among ruminal Gram-positive cocci

Cited by 31 publications

References 25 publications

Evaluation of Bacteriocin Activities among Enterococcal Poultry Isolates from East Azarbaijan Iran

Evaluation of Bacteriocin Activities among Enterococcal Poultry Isolates from East Azarbaijan Iran

Distribution and Genetic Diversity of Bacteriocin Gene Clusters in Rumen Microbial Genomes

Peptidoglycan Hydrolase Enterolysin A Recognizes Lipoteichoic Acid Chains in the Cell Walls of Sensitive Bacteria

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