The potential of lacticin 3147, enterocin AS-48, lacticin 481, variacin and sakacin P for food biopreservation

ABSTRACT Mersacidin binds to lipid II and thus blocks the transglycosylation step of the cell wall biosynthesis. Binding of lipid II involves a special motif, the so-called mersacidin-lipid II binding motif, which is conserved in a major subgroup of lantibiotics. We analyzed the role of Ca2+ ions in the mode of action of mersacidin and some related peptides containing a mersacidin-like lipid II binding motif. We found that the stimulating effect of Ca2+ ions on the antimicrobial activity known for mersacidin also applies to plantaricin C and lacticin 3147. Ca2+ ions appear to facilitate the interaction of the lantibiotics with the bacterial membrane and with lipid II rather than being an essential part of a peptide-lipid II complex. In the case of lacticin 481, both the interaction with lipid II and the antimicrobial activity were Ca2+ independent.

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Generation of Food-Grade Lactococcal Starters Which Produce the Lantibiotics Lacticin 3147 and Lacticin 481

Applied and Environmental Microbiology ◽

10.1128/aem.69.6.3681-3685.2003 ◽

2003 ◽

Vol 69 (6) ◽

pp. 3681-3685 ◽

Cited By ~ 31

Author(s):

Lisa O'Sullivan ◽

Maire P. Ryan ◽

R. Paul Ross ◽

Colin Hill

Keyword(s):

Listeria Monocytogenes ◽

Food Safety ◽

Lactobacillus Fermentum ◽

Food Grade ◽

Lacticin 3147 ◽

Lacticin 481 ◽

Safety Applications

ABSTRACT Transconjugant lactococcal starters which produce both lantibiotics lacticin 3147 and lacticin 481 were generated via conjugation of large bacteriocin-encoding plasmids. A representative of one of the resultant strains proved more effective at killing Lactobacillus fermentum and inhibiting the growth of Listeria monocytogenes LO28H than either of the single bacteriocin-producing parental strains, demonstrating the potential of these transconjugants as protection cultures for food safety applications.

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A comparison of the activities of lacticin 3147 and nisin against drug-resistant Staphylococcus aureus and Enterococcus species

Journal of Antimicrobial Chemotherapy ◽

10.1093/jac/dkp221 ◽

2009 ◽

Vol 64 (3) ◽

pp. 546-551 ◽

Cited By ~ 87

Author(s):

C. Piper ◽

L. A. Draper ◽

P. D. Cotter ◽

R. P. Ross ◽

C. Hill

Keyword(s):

Staphylococcus Aureus ◽

Drug Resistant ◽

Enterococcus Species ◽

Lacticin 3147

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Continuous production of lacticin 3147 and nisin using cells immobilized in calcium alginate

Journal of Applied Microbiology ◽

10.1046/j.1365-2672.2000.01149.x ◽

2000 ◽

Vol 89 (4) ◽

pp. 573-579 ◽

Cited By ~ 24

Author(s):

A.G.M. Scannell ◽

C. Hill ◽

R.P. Ross ◽

S. Marx ◽

W. Hartmeier ◽

...

Keyword(s):

Calcium Alginate ◽

Continuous Production ◽

Lacticin 3147

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The Leader Peptide Is Not Required for Post-Translational Modification by Lacticin 481 Synthetase

Journal of the American Chemical Society ◽

10.1021/ja072967+ ◽

2007 ◽

Vol 129 (34) ◽

pp. 10314-10315 ◽

Cited By ~ 36

Author(s):

Matthew R. Levengood ◽

Gregory C. Patton ◽

Wilfred A. van der Donk

Keyword(s):

Leader Peptide ◽

Post Translational Modification ◽

Lacticin 481 ◽

Lacticin 481 Synthetase

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Lantibiotic Reductase LtnJ Substrate Selectivity Assessed with a Collection of Nisin Derivatives as Substrates

Applied and Environmental Microbiology ◽

10.1128/aem.00475-15 ◽

2015 ◽

Vol 81 (11) ◽

pp. 3679-3687 ◽

Cited By ~ 11

Author(s):

Dongdong Mu ◽

Manuel Montalbán-López ◽

Jingjing Deng ◽

Oscar P. Kuipers

Keyword(s):

Amino Acids ◽

Posttranslational Modifications ◽

Substrate Selectivity ◽

Biosynthesis Gene Cluster ◽

Content Type ◽

Hydrophobic Residues ◽

Lacticin 3147 ◽

Biosynthesis Gene ◽

Biosynthetic Machinery

ABSTRACTLantibiotics are potent antimicrobial peptides characterized by the presence of dehydrated amino acids, dehydroalanine and dehydrobutyrine, and (methyl)lanthionine rings. In addition to these posttranslational modifications, some lantibiotics exhibit additional modifications that usually confer increased biological activity or stability on the peptide. LtnJ is a reductase responsible for the introduction ofd-alanine in the lantibiotic lacticin 3147. The conversion ofl-serine intod-alanine requires dehydroalanine as the substrate, which is producedin vivoby the dehydration of serine by a lantibiotic dehydratase, i.e., LanB or LanM. In this work, we probe the substrate specificity of LtnJ using a system that combines the nisin modification machinery (dehydratase, cyclase, and transporter) and the stereospecific reductase LtnJ inLactococcus lactis. We also describe an improvement in the production yield of this system by inserting a putative attenuator from the nisin biosynthesis gene cluster in front of theltnJgene. In order to clarify the sequence selectivity of LtnJ, peptides composed of truncated nisin and different mutated C-terminal tails were designed and coexpressed with LtnJ and the nisin biosynthetic machinery. In these tails, serine was flanked by diverse amino acids to determine the influence of the surrounding residues in the reaction. LtnJ successfully hydrogenated peptides when hydrophobic residues (Leu, Ile, Phe, and Ala) were flanking the intermediate dehydroalanine, while those in which dehydroalanine was flanked by one or two polar residues (Ser, Thr, Glu, Lys, and Asn) or Gly were either less prone to be modified by LtnJ or not modified at all. Moreover, our results showed that dehydrobutyrine cannot serve as a substrate for LtnJ.

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Mutants of the Zinc Ligands of Lacticin 481 Synthetase Retain Dehydration Activity but Have Impaired Cyclization Activity†

Biochemistry ◽

10.1021/bi7000104 ◽

2007 ◽

Vol 46 (21) ◽

pp. 6268-6276 ◽

Cited By ~ 48

Author(s):

Moushumi Paul ◽

Gregory C. Patton ◽

Wilfred A. van der Donk

Keyword(s):

Lacticin 481 ◽

Lacticin 481 Synthetase

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Mechanistic Dissection of the Enzyme Complexes Involved in Biosynthesis of Lacticin 3147 and Nisin

Applied and Environmental Microbiology ◽

10.1128/aem.01334-08 ◽

2008 ◽

Vol 74 (21) ◽

pp. 6591-6597 ◽

Cited By ~ 30

Author(s):

Anneke Kuipers ◽

Jenny Meijer-Wierenga ◽

Rick Rink ◽

Leon D. Kluskens ◽

Gert N. Moll

Keyword(s):

Lactococcus Lactis ◽

Bifunctional Enzyme ◽

Bifunctional Enzymes ◽

Lacticin 3147 ◽

Two Component ◽

Modified Peptides ◽

Enzyme Complexes ◽

Insight Into ◽

Design And Production

ABSTRACT The thioether rings in the lantibiotics lacticin 3147 and nisin are posttranslationally introduced by dehydration of serines and threonines, followed by coupling of these dehydrated residues to cysteines. The prepeptides of the two-component lantibiotic lacticin 3147, LtnA1 and LtnA2, are dehydrated and cyclized by two corresponding bifunctional enzymes, LtnM1 and LtnM2, and are subsequently processed and exported via one bifunctional enzyme, LtnT. In the nisin synthetase complex, the enzymes NisB, NisC, NisT, and NisP dehydrate, cyclize, export, and process prenisin, respectively. Here, we demonstrate that the combination of LtnM2 and LtnT can modify, process, and transport peptides entirely different from LtnA2 and that LtnT can process and transport unmodified LtnA2 and unrelated peptides. Furthermore, we demonstrate a higher extent of NisB-mediated dehydration in the absence of thioether rings. Thioether rings apparently inhibited dehydration, which implies alternating actions of NisB and NisC. Furthermore, certain (but not all) NisC-cyclized peptides were exported with higher efficiency as a result of their conformation. Taken together, these data provide further insight into the applicability of Lactococcus lactis strains containing lantibiotic enzymes for the design and production of modified peptides.

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