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Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4

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2017
2539.pdf (1.696Mb)
Authors
Lozo, Jelena
Mirković, Nemanja
O'Connor, Paula M.
Malešević, Milka
Miljković, Marija
Polović, Natalija
Jovčić, Branko
Cotter, Paul D.
Kojić, Milan O.
Article (Published version)
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Abstract
Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited ...similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.

Keywords:
bacteriocin / lactolisterin BU / antilisterial activity
Source:
Applied and Environmental Microbiology, 2017, 83, 21
Publisher:
  • Amer Soc Microbiology, Washington
Funding / projects:
  • Genes and molecular mechanisms promoting probiotic activity of lactic acid bacteria from Western Balkan (RS-173019)
Note:
  • Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/2999

DOI: 10.1128/AEM.01519-17

ISSN: 0099-2240

PubMed: 28842543

WoS: 000413104500013

Scopus: 2-s2.0-85031687597
[ Google Scholar ]
20
16
URI
https://cherry.chem.bg.ac.rs/handle/123456789/2541
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - JOUR
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2541
AB  - Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4
VL  - 83
IS  - 21
DO  - 10.1128/AEM.01519-17
UR  - Kon_3357
ER  - 
@article{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
abstract = "Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4",
volume = "83",
number = "21",
doi = "10.1128/AEM.01519-17",
url = "Kon_3357"
}
Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 83(21).
https://doi.org/10.1128/AEM.01519-17
Kon_3357
Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology. 2017;83(21).
doi:10.1128/AEM.01519-17
Kon_3357 .
Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4" in Applied and Environmental Microbiology, 83, no. 21 (2017),
https://doi.org/10.1128/AEM.01519-17 .,
Kon_3357 .

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