ArticleApplied and environmental microbiology2015
Enterocin F4-9, a Novel O-Linked Glycosylated Bacteriocin.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Structural Modification and Conjugation Strategies of Antimicrobial Peptides for Topical Anti-Infective Applications.Antibiotics (Basel, Switzerland) · 2026Review
- Characterization and antimicrobial potential of bacteriocin-producing lactic acid bacteria isolated from the gut ofMicrobiology spectrum · 2025Article
- Antimicrobial Activity of Carboxymethyl Cellulose Films Containing Plantaricin W and Enterocin F4-9 for Meat Preservation.International journal of molecular sciences · 2025Article
- Characterization of a novel glycocin from a thermophile.bioRxiv : the preprint server for biology · 2025Article
- The natural symbiotic bacterium Enterococcus faecalis LX10 drives Bombyx mori refractoriness to Nosema bombycis infection via the secretion of enterococcin.BMC microbiology · 2025Article
- Design and Biosynthesis of Ornithine 8-Containing Semaglutide Variants with a Click Chemistry-Modifiable Position 26.ACS synthetic biology · 2025Article
- Current status and potential of bacteriocin-producing lactic acid bacteria applied in the food industry.Current research in food science · 2025Review
- Characterization of S-glycosylated glycocins containing three disulfides.Journal of industrial microbiology & biotechnology · 2024Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Glycosylation and Lipidation Strategies: Approaches for Improving Antimicrobial Peptide Efficacy.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Enterocins: Classification, Synthesis, Antibacterial Mechanisms and Food Applications.Molecules (Basel, Switzerland) · 2022Review
- Strategies for Biocontrol ofFoods (Basel, Switzerland) · 2022Review
- Bacteriocins: Properties and potential use as antimicrobials.Journal of clinical laboratory analysis · 2022Review
- Structural and mechanistic investigations of protein S-glycosyltransferases.Cell chemical biology · 2021Article
- Characterization of the Biosynthetic Gene Cluster of Enterocin F4-9, a Glycosylated Bacteriocin.Microorganisms · 2021Article
- Review
- The Antimicrobial Activity of the Glycocin Sublancin Is Dependent on an Active Phosphoenolpyruvate-Sugar Phosphotransferase System.ACS infectious diseases · 2021Article
- SELECT-GLYCOCIN: a recombinant microbial system for expression and high-throughput screening of glycocins.Glycoconjugate journal · 2021Article
- Optimized Genetic Tools Allow the Biosynthesis of Glycocin F and Analogues Designed To Test the Roles ofJournal of bacteriology · 2021Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enterococcus faecalis F4-9 isolated from Egyptian salted-fermented fish produces a novel bacteriocin, termed enterocin F4-9. Enterocin F4-9 was purified from the culture supernatant by three steps, and its molecular mass was determined to be 5,516.6 Da by mass spectrometry. Amino acid and DNA sequencing showed that the propeptide consists of 67 amino acid residues, with a leader peptide containing a double glycine cleavage site to produce a 47-amino-acid mature peptide. Enterocin F4-9 is modified by two molecules of N-acetylglucosamine β-O-linked to Ser37 and Thr46. The O-linked N-acetylglucosamine moieties are essential for the antimicrobial activity of enterocin F4-9. Further analysis of the enterocin F4-9 gene cluster identified enfC, which has high sequence similarity to a glycosyltransferase. The antimicrobial activity of enterocin F4-9 covered a limited range of bacteria, including, interestingly, a Gram-negative strain, Escherichia coli JM109. Enterocin F4-9 is sensitive to protease, active at a wide pH range, and moderately resistant to heat.
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