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

Lozo, Jelena; Mirković, Nemanja; O’Connor, Paula M.; Malešević, Milka; Miljković, Marija; Polović, Natalija; Jovčić, Branko; Cotter, Paul D.; Kojić, Milan

doi:10.1128/aem.01519-17

Cited by 31 publications

(27 citation statements)

References 42 publications

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“…Additionally, the structure genes and the genes encoding the putative biosynthetic enzymes of weissellicin Y and M and enterocin MR10 (MR10A and B) seem to be encoded in the chromosomal DNA of its producer strains Weissella hellenica QU 13 ( Masuda et al, 2012a ) and Enterococcus faecalis MRR10-3 ( Martín-Platero et al, 2006 ), respectively. Whereas the plasmid-encoded genetic determinants for the leaderless bacteriocins enterocin EJ97 ( Sánchez-Hidalgo et al, 2003 ), lactolisterin BU ( Lozo et al, 2017 ), garvicin KS ( Ovchinnikov et al, 2016 ), cereucin H, V, and X ( Ovchinnikov et al, 2016 ), and epidermicin NI01 ( Sandiford and Upton, 2012 ) have also been described. Although, the specific functions of the gene products encoded in these putative biosynthetic genes have remained unconfirmed.…”

Section: Leaderless Bacteriocinsmentioning

confidence: 99%

Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects

2018

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Bacteriocins are a huge family of ribosomally synthesized peptides known to exhibit a range of bioactivities, most predominantly antibacterial activities. Bacteriocins from lactic acid bacteria are of particular interest due to the latter’s association to food fermentation and the general notion of them to be safe. Among the family of bacteriocins, the groups known as circular bacteriocins and leaderless bacteriocins are gaining more attention due to their enormous potential for industrial application. Circular bacteriocins and leaderless bacteriocins, arguably the least understood groups of bacteriocins, possess distinctively peculiar characteristics in their structures and biosynthetic mechanisms. Circular bacteriocins have N-to-C- terminal covalent linkage forming a structurally distinct circular peptide backbone. The circular nature of their structures provides them superior stability against various stresses compared to most linear bacteriocins. The molecular mechanism of their biosynthesis, albeit has remained poorly understood, is believed to possesses huge application prospect as it can serve as scaffold in bioengineering other biologically important peptides. On the other hand, while most bacteriocins are synthesized as inactive precursor peptides, which possess an N-terminal leader peptide attached to a C-terminal propeptide, leaderless bacteriocins are atypical as they do not have an N-terminal leader peptide, hence the name. Leaderless bacteriocins are active right after translation as they do not undergo any post-translational processing common to other groups of bacteriocins. This “simplicity” in the biosynthesis of leaderless bacteriocins offers a huge commercial potential as scale-up production systems are considerably easier to assemble. In this review, we summarize the current studies of both circular and leaderless bacteriocins, highlighting the progress in understanding their biosynthesis, mode of action, application and their prospects.

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Section: Leaderless Bacteriocinsmentioning

confidence: 99%

Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects

2018

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“…In a previous study, it was reported that Lactococcus lactis subsp. lactis BGBU1-4 contains a plasmid, pBU6, carrying the structural lactolisterin BU operon ( Lozo et al, 2017 ). Based on comparisons with known bacteriocin clusters, it was hypothesized that the lactolisterin BU bacteriocin operon was organized into a four gene operon-like structure consisting of ( lliBU ) the structural gene; ( abcT ) an ABC transporter; and hyp1 and hyp2 genes to which the exact function has not been attributed.…”

Section: Resultsmentioning

confidence: 99%

“…and streptococci. The production of lactolisterin BU is related to the smallest plasmid pBU6 of 6.2 kb, which contains nine open reading frames (ORFs): repB , lliBU , abcT , hyp1 , hyp2 , hyp3 , mobC , relM , and rnaY ( Lozo et al, 2017 ). An identity (BLAST) search within the lactolisterin BU operon recognized the product of the abcT gene as a sugar transporter, while other genes were designated as hypothetical.…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4

et al. 2018

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The gene cluster responsible for the production of the aureocin A53-like bacteriocin, lactolisterin BU, is located on plasmid pBU6 in Lactococcus lactis subsp. lactis BGBU1-4. Heterologous expression of pBU6 confirmed that production and limited immunity to lactolisterin BU were provided by the plasmid. Comparative analysis of aureocin A53-like operons revealed that the structural genes shared a low level of identity, while other genes were without homology, indicating a different origin. Subcloning and expression of genes located downstream of the structural gene, lliBU, revealed that the lactolisterin BU cluster consists of four genes: the structural gene lliBU, the abcT gene encoding an ABC transporter, the accL gene encoding an accessory protein and the immL gene which provides limited immunity to lactolisterin BU. Reverse transcription analysis revealed that all genes were transcribed as one polycistronic mRNA. Attempts to split the lactolisterin BU operon, even when both parts were under control of the PlliBU promoter, were unsuccessful indicating that expression of lactolisterin BU is probably precisely regulated at the translational level by translational coupling and is possible only when all genes of the operon are in cis constellation. Two ρ-independent transcription terminators were detected in the lactolisterin BU operon: the first in the intergenic region of the lliBU and abcT genes and the second at the end of operon. Deletion of the second transcription terminator did not influence production of the bacteriocin in lactococci.

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“…A key emerging group of antimicrobial peptides include the bacteriocins which are produced by Lactic Acid Bacteria (LAB). Bacteriocins are ribosomally synthesized hydrophobic peptides which usually display activity towards bacteria closely related to the producer (Lozo et al 2017) and may be subdivided based on whether or not they have undergone post translational modifications (Class I) or not (Class II). This group of antimicrobial peptides exhibit enhanced potency, are biocompatible and stable and can have a narrow or broad range spectrum of activity .…”

Section: Introductionmentioning

confidence: 99%

“…This bacteriocin has a very narrow spectrum of activity and could be used specifically to treat C. difficile infections of the gut. (Acedo et al 2017, Ahn et al 2017, Lozo et al 2017. Enterocin NKR-5-3, a class IIa bacteriocin, shows potent activity against Listeria spp.…”

Section: Introductionmentioning

confidence: 99%

Protecting bactofencin A to enable its antimicrobial activity using mesoporous matrices

Durack

Mallen

O’Connor

et al. 2019

International Journal of Pharmaceutics

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There is huge global concern surrounding the emergence of antimicrobial resistant bacteria and this is resulting in an inability to treat infectious diseases. This is due to a lack of new antimicrobials coming to the market and irresponsible use of traditional antibiotics. Bactofencin A, a novel antimicrobial peptide which shows potential as an antibiotic, is susceptible to enzyme degradation. To improve its solution stability and inherent activity, bactofencin A was loaded onto a traditional silica mesoporous matrix, SBA-15, and a periodic mesoporous organosilane, MSE. The loading of bactofencin A was considerably higher onto SBA-15 than MSE due to the hydrophilic nature of SBA-15. While there was no detectable peptide released from SBA-15 into phosphate buffered saline and only 20 % of the peptide loaded onto MSE was released, the loaded matrices showed enhanced activity compared to the free peptide during in vitro antimicrobial assays. In addition, the mesoporous matrices were found to protect bactofencin A against enzymatic degradation where results showed that the SBA-15 and MSE with loaded bactofencin A exposed to trypsin inhibited the growth of S. aureus while a large decrease in activity was observed for free bactofencin upon exposure to trypsin. Thus, the activity and stability of bactofencin A can be enhanced using mesoporous matrices and these matrices may enable its potential development as a novel antibiotic. This work also shows that in silico studies looking at surface functional group and size complementarity between the peptide and the protective matrix could enable the systemic selection of a mesoporous matrix for individual bacteriocins with potential antimicrobial therapeutic properties.

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

Cited by 31 publications

References 42 publications

Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects

Circular and Leaderless Bacteriocins: Biosynthesis, Mode of Action, Applications, and Prospects

Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4

Protecting bactofencin A to enable its antimicrobial activity using mesoporous matrices

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