The Potential of Antimicrobial Activity and Antibiofilm Activity of Bacteriocins

A special issue of Microorganisms (ISSN 2076-2607). This special issue belongs to the section "Antimicrobial Agents and Resistance".

Deadline for manuscript submissions: 15 May 2024 | Viewed by 1649

Special Issue Editor

Institute of Animal Physiology, Centre of Biosciences of the Slovak Academy of Sciences, Košice, Slovakia
Interests: beneficial bacteria; bacteriocins; enterococcus
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The world is facing various contamination incidents and infections caused by microbiota. Many strategies have been explored to treat/eliminate them. The traditional treatments for these cases include using different classes of antibiotics. This leads to a great increase in antibiotic-resistant bacteria. Therefore, preventing and controlling the spread of antibiotic-resistance bacteria is necessary. Bacteriocins are a group of antimicrobial substances of proteinaceous character produced by various bacteria, capable of controlling more or less (clinically) relevant drug-resistant bacteria. Bacteriocins can act against pathogens and improve host health. Although bacteriocin has been investigated for many years, it is still a hot topic due to its application potentials. Recently, bacteriocins have been used in veterinary medicine, animal husbandry, and agriculture as biocontrol agents. This Special Issue will welcome original contributions on bacteriocins, with special reference to work relevant to their antimicrobial potential and antibiofilm activity, and how they can contribute to further benefiting human and veterinary health.

Dr. Andrea Lauková
Guest Editor

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Keywords

  • bacteriocins
  • antimicrobial
  • antibiofilm

Published Papers (2 papers)

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Research

12 pages, 3166 KiB  
Article
Human Milk-Derived Enterococcus faecalis HM20: A Potential Alternative Agent of Antimicrobial Effect against Methicillin-Resistant Staphylococcus aureus (MRSA)
Microorganisms 2024, 12(2), 306; https://doi.org/10.3390/microorganisms12020306 - 31 Jan 2024
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Abstract
The increasing global impact of skin diseases, fueled by methicillin-resistant Staphylococcus aureus (MRSA), emphasizes the necessity for alternative therapies with lower toxicity, such as lactic acid bacteria (LAB). This study aims to isolate potential LAB from human milk and evaluate their efficacy against [...] Read more.
The increasing global impact of skin diseases, fueled by methicillin-resistant Staphylococcus aureus (MRSA), emphasizes the necessity for alternative therapies with lower toxicity, such as lactic acid bacteria (LAB). This study aims to isolate potential LAB from human milk and evaluate their efficacy against MRSA using various methods, including well diffusion, microdilution, crystal violet assay, enzymatic characterization, SDS-PAGE, and scanning electron microscopy (SEM). Among the 26 LAB screened, the human milk-derived strain HM20 exhibited significant antimicrobial activity against S. aureus CCARM 3089 (MRSA), which is a highly resistant skin pathogen. Through 16S rRNA sequencing, strain HM20 was identified as closely related to Enterococcus faecalis ATCC 19433T, which was subsequently designated as Enterococcus faecalis HM20. The minimum inhibitory concentration (MIC) of the cell-free supernatant (CFS) of HM20 against S. aureus KCTC 3881 and S. aureus CCARM 3089 was determined to be 6.25% and 12.5%, respectively. Furthermore, the effective inhibition of biofilm formation in S. aureus KCTC 3881 and S. aureus CCARM 3089 was observed at concentrations of 12.5% and 25% or higher, respectively. The antibacterial effect of the CFS was attributed to the presence of organic acids, hydrogen peroxide, and bacteriocins. Additionally, the antimicrobial peptides produced by HM20 were found to be stable under heat treatment and analyzed to have a size below 5 kDa. SEM image observations confirmed that the CFS of HM20 caused damage to the cell wall, forming pores and wrinkles on S. aureus KCTC 3881 and S. aureus CCARM 3089. This comprehensive investigation on strain HM20 conducted in this study provides foundational data for potential developments in functional materials aimed at addressing skin infections and antibiotic-resistant strains in the future. Full article
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16 pages, 4837 KiB  
Article
A Novel Deoxyribonuclease Low-Molecular-Weight Bacteriocin, Carocin S4, from Pectobacterium carotovorum subsp. carotovorum
Microorganisms 2023, 11(7), 1854; https://doi.org/10.3390/microorganisms11071854 - 22 Jul 2023
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Abstract
Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, [...] Read more.
Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc. A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc. CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg2+, Ca2+, and Zn2+ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc, with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively. Full article
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