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Journal articles on the topic 'Two-peptide lantibiotics'

Author: Grafiati

Published: 7 September 2021

Last updated: 29 July 2025

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1

Begley, Mï¿½ire, Paul D. Cotter, Colin Hill, and R. Paul Ross. "Identification of a Novel Two-Peptide Lantibiotic, Lichenicidin, following Rational Genome Mining for LanM Proteins." Applied and Environmental Microbiology 75, no. 17 (2009): 5451–60. http://dx.doi.org/10.1128/aem.00730-09.

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ABSTRACT Lantibiotics are ribosomally synthesized peptide antimicrobials which contain considerable posttranslational modifications. Given their usually broad host range and their highly stable structures, there have been renewed attempts to identify and characterize novel members of the lantibiotic family in recent years. The increasing availability of bacterial genome sequences means that in addition to traditional microbiological approaches, in silico screening strategies may now be employed to the same end. Taking advantage of the highly conserved nature of lantibiotic biosynthetic enzymes

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2

Birri, Dagim Jirata, Dag Anders Brede, and Ingolf F. Nes. "Salivaricin D, a Novel Intrinsically Trypsin-Resistant Lantibiotic from Streptococcus salivarius 5M6c Isolated from a Healthy Infant." Applied and Environmental Microbiology 78, no. 2 (2011): 402–10. http://dx.doi.org/10.1128/aem.06588-11.

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ABSTRACTIn this work, we purified and characterized a newly identified lantibiotic (salivaricin D) fromStreptococcus salivarius5M6c. Salivaricin D is a 34-amino-acid-residue peptide (3,467.55 Da); the locus of the gene encoding this peptide is a 16.5-kb DNA segment which contains genes encoding the precursor of two lantibiotics, two modification enzymes (dehydratase and cyclase), an ABC transporter, a serine-like protease, immunity proteins (lipoprotein and ABC transporters), a response regulator, and a sensor histidine kinase. The immunity gene (salI) was heterologously expressed in a sensiti

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3

Antoshina, D. V., S. V. Balandin, A. A. Tagaev, A. A. Potemkina, and T. V. Ovchinnikova. "Biotechnological Production of the Recombinant Two-Component Lantibiotic Lichenicidin in a Bacterial Expression System." Russian Journal of Bioorganic Chemistry 50, no. 4 (2024): 1150–61. http://dx.doi.org/10.1134/s1068162024040459.

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Abstract Objective: Lantibiotics are a family of bacterial antimicrobial peptides synthesized by ribosomes, that undergo post-translational modification to form lanthionine (Lan) and methyllanthionine (MeLan) residues. Lantibiotics are currently considered promising agents for combating antibiotic-resistant bacterial infections. This paper presents a biotechnological method for obtaining two components of the lantibiotic lichenicidin from Bacillus licheniformis B-511, Lchα and Lchβ. Such a system has the potential to facilitate the production of not only lichenicidin, but also other lantibioti

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4

Lawton, Elaine, R. Ross, Colin Hill, and Paul Cotter. "Two-Peptide Lantibiotics: A Medical Perspective." Mini-Reviews in Medicinal Chemistry 7, no. 12 (2007): 1236–47. http://dx.doi.org/10.2174/138955707782795638.

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Antoshina, D. V., S. V. Balandin, A. A. Tagaev, A. A. Potemkina, and T. V. Ovchinnikova. "Biotechnological Production of the Recombinant Two-Component Lantibiotic Lichenicidin in the Bacterial Expression System." Биоорганическая химия 50, no. 4 (2024): 485–97. http://dx.doi.org/10.31857/s0132342324040081.

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Lantibiotics are a family of bacterial antimicrobial peptides synthesized by ribosomes that undergo post-translational modification to form lanthionine (Lan) and methyllanthionine (MeLan) residues. Lantibiotics are considered promising agents for combating antibiotic-resistant bacterial infections. This paper presents a biotechnological method for obtaining two components of the lantibiotic lichenicidin from Bacillus licheniformis B-511 – Lchα and Lchβ. A system has been developed that allows co-expression of the lchA1 or lchA2 genes, encoding the precursors of the α- or β-components, respecti

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Navaratna, Maduwe A. D. B., Hans-Georg Sahl, and John R. Tagg. "Identification of Genes Encoding Two-Component Lantibiotic Production in Staphylococcus aureus C55 and Other Phage Group II S. aureus Strains and Demonstration of an Association with the Exfoliative Toxin B Gene." Infection and Immunity 67, no. 8 (1999): 4268–71. http://dx.doi.org/10.1128/iai.67.8.4268-4271.1999.

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ABSTRACT The production of exfoliative toxin B (ET-B), but not ET-A, was shown to be specifically associated with production of a highly conserved two-component lantibiotic peptide system in phage group IIStaphylococcus aureus. Two previously studied but incompletely characterized S. aureus bacteriocins, staphylococcins C55 and BacR1, were found to be members of this lantibiotic system, and considerable homology was also found with the two-component Lactococcus lactis bacteriocin, lacticin 3147. sacαA and sacβA, the structural genes of the lantibiotics staphylococcins C55α and C55β and two put

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Goldbeck, Oliver, Dominik Weixler, Bernhard J. Eikmanns, and Christian U. Riedel. "In Silico Prediction and Analysis of Unusual Lantibiotic Resistance Operons in the Genus Corynebacterium." Microorganisms 9, no. 3 (2021): 646. http://dx.doi.org/10.3390/microorganisms9030646.

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Post-translationally modified, (methyl-)lanthionine-containing peptides are produced by several Gram-positive bacteria. These so-called lantibiotics have potent activity against various bacterial pathogens including multidrug-resistant strains and are thus discussed as alternatives to antibiotics. Several naturally occurring mechanisms of resistance against lantibiotics have been described for bacteria, including cell envelope modifications, ABC-transporters, lipoproteins and peptidases. Corynebacterium species are widespread in nature and comprise important pathogens, commensals as well as en

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Upton, M., J. R. Tagg, P. Wescombe, and H. F. Jenkinson. "Intra- and Interspecies Signaling betweenStreptococcus salivarius and Streptococcus pyogenes Mediated by SalA and SalA1 Lantibiotic Peptides." Journal of Bacteriology 183, no. 13 (2001): 3931–38. http://dx.doi.org/10.1128/jb.183.13.3931-3938.2001.

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ABSTRACT Streptococcus salivarius 20P3 produces a 22-amino-acid residue lantibiotic, designated salivaricin A (SalA), that inhibits the growth of a range of streptococci, including all strains ofStreptococcus pyogenes. Lantibiotic production is associated with the sal genetic locus comprisingsalA, the lantibiotic structural gene; salBCTXgenes encoding peptide modification and export machinery proteins; andsalYKR genes encoding a putative immunity protein and two-component sensor-regulator system. Insertional inactivation ofsalB in S. salivarius 20P3 resulted in abrogation of SalA peptide produ

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Kalmokoff, M. L., D. Lu, M. F. Whitford, and R. M. Teather. "Evidence for Production of a New Lantibiotic (Butyrivibriocin OR79A) by the Ruminal Anaerobe Butyrivibrio fibrisolvensOR79: Characterization of the Structural Gene Encoding Butyrivibriocin OR79A." Applied and Environmental Microbiology 65, no. 5 (1999): 2128–35. http://dx.doi.org/10.1128/aem.65.5.2128-2135.1999.

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ABSTRACT The ruminal anaerobe Butyrivibrio fibrisolvens OR79 produces a bacteriocin-like activity demonstrating a very broad spectrum of activity. An inhibitor was isolated from spent culture fluid by a combination of ammonium sulfate and acidic precipitations, reverse-phase chromatography, and high-resolution gel filtration. N-terminal analysis of the isolated inhibitor yielded a 15-amino-acid sequence (G-N/Q-G/P-V-I-L-X-I-X-H-E-X-S-M-N). Two different amino acid residues were detected in the second and third positions from the N terminus, indicating the presence of two distinct peptides. A g

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10

Majchrzykiewicz, Joanna A., Jacek Lubelski, Gert N. Moll, et al. "Production of a Class II Two-Component Lantibiotic of Streptococcus pneumoniae Using the Class I Nisin Synthetic Machinery and Leader Sequence." Antimicrobial Agents and Chemotherapy 54, no. 4 (2010): 1498–505. http://dx.doi.org/10.1128/aac.00883-09.

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ABSTRACT Recent studies showed that the nisin modification machinery can successfully dehydrate serines and threonines and introduce lanthionine rings in small peptides that are fused to the nisin leader sequence. This opens up exciting possibilities to produce and engineer larger antimicrobial peptides in vivo. Here we demonstrate the exploitation of the class I nisin production machinery to generate, modify, and secrete biologically active, previously not-yet-isolated and -characterized class II two-component lantibiotics that have no sequence homology to nisin. The nisin synthesis machinery

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Mota-Meira, Marilaine, Gisèle Lapointe, Christophe Lacroix, and Marc C. Lavoie. "MICs of Mutacin B-Ny266, Nisin A, Vancomycin, and Oxacillin against Bacterial Pathogens." Antimicrobial Agents and Chemotherapy 44, no. 1 (2000): 24–29. http://dx.doi.org/10.1128/aac.44.1.24-29.2000.

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ABSTRACT Peptide antibiotics, particularly lantibiotics, are good candidates for replacing antibiotics to which bacteria have become resistant. In order to compare two such lantibiotics with two antibiotics, the MICs of nisin A, mutacin B-Ny266, vancomycin, and oxacillin against various bacterial pathogens were determined. The results indicate that nisin A and mutacin B-Ny266 are as active as vancomycin and oxacillin against most of the strains tested. Furthermore, mutacin B-Ny266 remains active against strains that are resistant to nisin A, oxacillin, or vancomycin. The wide spectrum of activ

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12

Hindré, Thomas, Sandrine Didelot, Jean-Paul Le Pennec, Dominique Haras, Alain Dufour, and Karine Vallée-Réhel. "Bacteriocin Detection from Whole Bacteria by Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry." Applied and Environmental Microbiology 69, no. 2 (2003): 1051–58. http://dx.doi.org/10.1128/aem.69.2.1051-1058.2003.

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ABSTRACT Class I bacteriocins (lantibiotics) and class II bacteriocins are antimicrobial peptides secreted by gram-positive bacteria. Using two lantibiotics, lacticin 481 and nisin, and the class II bacteriocin coagulin, we showed that bacteriocins can be detected without any purification from whole producer bacteria grown on plates by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS). When we compared the results of MALDI-TOF-MS performed with samples of whole cells and with samples of crude supernatants of liquid cultures, the former samples led to m

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Holtsmark, I., D. Mantzilas, V. G. H. Eijsink, and M. B. Brurberg. "Purification, Characterization, and Gene Sequence of Michiganin A, an Actagardine-Like Lantibiotic Produced by the Tomato Pathogen Clavibacter michiganensis subsp. michiganensis." Applied and Environmental Microbiology 72, no. 9 (2006): 5814–21. http://dx.doi.org/10.1128/aem.00639-06.

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ABSTRACT Members of the actinomycete genus Clavibacter are known to produce antimicrobial compounds, but so far none of these compounds has been purified and characterized. We have isolated an antimicrobial peptide, michiganin A, from the tomato pathogen Clavibacter michiganensis subsp. michiganensis, using ammonium sulfate precipitation followed by cation-exchange and reversed-phase chromatography steps. Upon chemical derivatization of putative dehydrated amino acids and lanthionine bridges by alkaline ethanethiol, Edman degradation yielded sequence information that proved to be sufficient fo

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Cintas, L. M., M. P. Casaus, C. Herranz, I. F. Nes, and P. E. Hernández. "Review: Bacteriocins of Lactic Acid Bacteria." Food Science and Technology International 7, no. 4 (2001): 281–305. http://dx.doi.org/10.1106/r8de-p6hu-clxp-5ryt.

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During the last few years, a large number of new bacteriocins produced by lactic acid bacteria (LAB) have been identified and characterized. LAB-bacteriocins comprise a heterogeneous group of physicochemically diverse ribosomally-synthesized peptides or proteins showing a narrow or broad antimicrobial activity spectrum against Gram-positive bacteria. Bacteriocins are classified into separate groups such as the lantibiotics (Class I); the small (<10 kDa) heat-stable postranslationally unmodified non-lantibiotics (Class II), further subdivided in the pediocin-like and anti Listeria bacterioci

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15

Wescombe, Philip A., and John R. Tagg. "Purification and Characterization of Streptin, a Type A1 Lantibiotic Produced by Streptococcus pyogenes." Applied and Environmental Microbiology 69, no. 5 (2003): 2737–47. http://dx.doi.org/10.1128/aem.69.5.2737-2747.2003.

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ABSTRACT Approximately 10% of Streptococcus pyogenes strains inhibit the growth of all nine indicators in a standardized streptococcal bacteriocin typing scheme. The present study has shown that this inhibitory profile, referred to as bacteriocin producer (P)-type 777 activity, is due to the type A1 lantibiotic streptin. Two major forms of streptin were purified to homogeneity from 95% acidified (pH 2) methanol extracts of S. pyogenes M25 cells by using a series of reversed-phase chromatographic separations. The fully processed form of streptin (streptin 1) is a 23-amino-acid peptide with a ma

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16

Mu, Dongdong, Manuel Montalbán-López, Jingjing Deng, and Oscar P. Kuipers. "Lantibiotic Reductase LtnJ Substrate Selectivity Assessed with a Collection of Nisin Derivatives as Substrates." Applied and Environmental Microbiology 81, no. 11 (2015): 3679–87. http://dx.doi.org/10.1128/aem.00475-15.

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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

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Staroń, Anna, Dora Elisabeth Finkeisen, and Thorsten Mascher. "Peptide Antibiotic Sensing and Detoxification Modules ofBacillus subtilis." Antimicrobial Agents and Chemotherapy 55, no. 2 (2010): 515–25. http://dx.doi.org/10.1128/aac.00352-10.

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ABSTRACTPeptide antibiotics are produced by a wide range of microorganisms. Most of them target the cell envelope, often by inhibiting cell wall synthesis. One of the resistance mechanisms against antimicrobial peptides is a detoxification module consisting of a two-component system and an ABC transporter. Upon the detection of such a compound, the two-component system induces the expression of the ABC transporter, which in turn removes the antibiotic from its site of action, mediating the resistance of the cell. Three such peptide antibiotic-sensing and detoxification modules are present inBa

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18

Wilson-Stanford, Shawanda, Anastasia Kalli, Kristina Håkansson, James Kastrantas, Ravi S. Orugunty, and Leif Smith. "Oxidation of Lanthionines Renders the Lantibiotic Nisin Inactive." Applied and Environmental Microbiology 75, no. 5 (2008): 1381–87. http://dx.doi.org/10.1128/aem.01864-08.

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ABSTRACT The peptide antibiotic nisin A belongs to the group of antibiotics called lantibiotics. They are classified as lantibiotics because they contain the structural group lanthionine. Lanthionines are composed of a single sulfur atom that is linked to the β-carbons of two alanine moieties. These sulfur atoms are vulnerable to environmental oxidation. A mild oxidation reaction was performed on nisin A to determine the relative effects it would have on bioactivity. High-mass-accuracy Fourier transform ion cyclotron resonance mass spectrometry data revealed the addition of seven, eight, and n

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Blake, Katy L., Chris P. Randall, and Alex J. O'Neill. "In VitroStudies Indicate a High Resistance Potential for the Lantibiotic Nisin in Staphylococcus aureus and Define a Genetic Basis for Nisin Resistance." Antimicrobial Agents and Chemotherapy 55, no. 5 (2011): 2362–68. http://dx.doi.org/10.1128/aac.01077-10.

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ABSTRACTLantibiotics such as nisin (NIS) are peptide antibiotics that may have a role in the chemotherapy of bacterial infections. A perceived benefit of lantibiotics for clinical use is their low propensity to select resistance, although detailed resistance studies with relevant bacterial pathogens are lacking. Here we examined the development of resistance to NIS inStaphylococcus aureus, establishing that mutants, including small-colony variants, exhibiting substantial (4- to 32-fold) reductions in NIS susceptibility could be selected readily. Comparative genome sequencing of a single NISrmu

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Holo, Helge, Zoran Jeknic, Mark Daeschel, Stefan Stevanovic, and Ingolf F. Nes. "Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics The GenBank accession number for the sequence reported in this paper is AY007251." Microbiology 147, no. 3 (2001): 643–51. http://dx.doi.org/10.1099/00221287-147-3-643.

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Qi, Fengxia, Ping Chen, and Page W. Caufield. "The Group I Strain of Streptococcus mutans, UA140, Produces Both the Lantibiotic Mutacin I and a Nonlantibiotic Bacteriocin, Mutacin IV." Applied and Environmental Microbiology 67, no. 1 (2001): 15–21. http://dx.doi.org/10.1128/aem.67.1.15-21.2001.

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ABSTRACT Strains of Streptococcus mutans produce at least three mutacins, I, II, and III. Mutacin II is a member of subgroup AII in the lantibiotic family of bacteriocins, and mutacins I and III belong to subgroup AI in the lantibiotic family. In this report, we characterize two mutacins produced by UA140, a group I strain of S. mutans. One is identical to the lantibiotic mutacin I produced by strain CH43 (F. Qi et al., Appl. Environ. Microbiol. 66:3221–3229, 2000); the other is a nonlantibiotic bacteriocin, which we named mutacin IV. Mutacin IV belongs to the two-peptide, nonlantibiotic famil

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Cotter, Paul D., Lorraine A. Draper, Elaine M. Lawton, Olivia McAuliffe, Colin Hill, and R. Paul Ross. "Overproduction of Wild-Type and Bioengineered Derivatives of the Lantibiotic Lacticin 3147." Applied and Environmental Microbiology 72, no. 6 (2006): 4492–96. http://dx.doi.org/10.1128/aem.02543-05.

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ABSTRACT Lacticin 3147 is a broad-spectrum two-peptide lantibiotic whose genetic determinants are located on two divergent operons on the lactococcal plasmid pMRC01. Here we introduce each of 14 subclones, containing different combinations of lacticin 3147 genes, into MG1363 (pMRC01) and determine that a number of them can facilitate overproduction of the lantibiotic. Based on these studies it is apparent that while the provision of additional copies of genes encoding the biosynthetic/production machinery and the regulator LtnR is a requirement for high-level overproduction, the presence of ad

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Sawa, Naruhiko, Pongtep Wilaipun, Seisuke Kinoshita, et al. "Isolation and Characterization of Enterocin W, a Novel Two-Peptide Lantibiotic Produced by Enterococcus faecalis NKR-4-1." Applied and Environmental Microbiology 78, no. 3 (2011): 900–903. http://dx.doi.org/10.1128/aem.06497-11.

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ABSTRACTEnterococcus faecalisNKR-4-1 isolated from pla-ra produces a novel two-peptide lantibiotic, termed enterocin W, comprising Wα and Wβ. The structure of enterocin W exhibited similarity with that of plantaricin W. The two peptides acted synergistically, and their order of binding to the cell membrane was important for their inhibitory activity.

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Deegan, Lucy H., Srinivas Suda, Elaine M. Lawton, et al. "Manipulation of charged residues within the two-peptide lantibiotic lacticin 3147." Microbial Biotechnology 3, no. 2 (2009): 222–34. http://dx.doi.org/10.1111/j.1751-7915.2009.00145.x.

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Altena, Karsten, André Guder, Claudia Cramer, and Gabriele Bierbaum. "Biosynthesis of the Lantibiotic Mersacidin: Organization of a Type B Lantibiotic Gene Cluster." Applied and Environmental Microbiology 66, no. 6 (2000): 2565–71. http://dx.doi.org/10.1128/aem.66.6.2565-2571.2000.

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ABSTRACT The biosynthetic gene cluster (12.3 kb) of mersacidin, a lanthionine-containing antimicrobial peptide, is located on the chromosome of the producer, Bacillus sp. strain HIL Y-85,54728 in a region that corresponds to 348° on the chromosome ofBacillus subtilis 168. It consists of 10 open reading frames and contains, in addition to the previously described mersacidin structural gene mrsA (G. Bierbaum, H. Brötz, K.-P. Koller, and H.-G. Sahl, FEMS Microbiol. Lett. 127:121–126, 1995), two genes, mrsM and mrsD, coding for enzymes involved in posttranslational modification of the prepeptide;

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Barbosa, Joana C., Sónia Gonçalves, Marcin Makowski, et al. "Insights into the mode of action of the two-peptide lantibiotic lichenicidin." Colloids and Surfaces B: Biointerfaces 211 (March 2022): 112308. http://dx.doi.org/10.1016/j.colsurfb.2021.112308.

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Martin, Nathaniel I., Tara Sprules, Michael R. Carpenter, et al. "Structural Characterization of Lacticin 3147, a Two-Peptide Lantibiotic with Synergistic Activity†." Biochemistry 43, no. 11 (2004): 3049–56. http://dx.doi.org/10.1021/bi0362065.

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Oman, Trent J., and Wilfred A. van der Donk. "Insights into the Mode of Action of the Two-Peptide Lantibiotic Haloduracin." ACS Chemical Biology 4, no. 10 (2009): 865–74. http://dx.doi.org/10.1021/cb900194x.

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Mirkovic, Nemanja, Natalija Polovic, Goran Vukotic, et al. "Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic." Applied and Environmental Microbiology 82, no. 8 (2016): 2555–62. http://dx.doi.org/10.1128/aem.03988-15.

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ABSTRACTBacteriocin producers normally possess dedicated immunity systems to protect themselves from their own bacteriocins.Lactococcus lactisstrains LMG2081 and BGBM50 are known as lactococcin G producers. However, BGBM50 was sensitive to LMG2081, which indicated that LMG2081 might produce additional bacteriocins that are not present in BGBM50. Therefore, whole-genome sequencing of the two strains was performed, and a lantibiotic operon (calledlctLMG) was identified in LMG2081 but not in BGBM50. ThelctLMGoperon contains six open reading frames; the first three genes,lmgA,lmgM, andlmgT, are in

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Kuipers, Anneke, Jenny Wierenga, Rick Rink, et al. "Sec-Mediated Transport of Posttranslationally Dehydrated Peptides in Lactococcus lactis." Applied and Environmental Microbiology 72, no. 12 (2006): 7626–33. http://dx.doi.org/10.1128/aem.01802-06.

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ABSTRACT Nisin is a lanthionine-containing antimicrobial peptide produced by Lactococcus lactis. Its (methyl)lanthionines are introduced by two posttranslational enzymatic steps involving the dehydratase NisB, which dehydrates serine and threonine residues, and the cyclase NisC, which couples these dehydrated residues to cysteines, yielding thioether-bridged amino acids called lanthionines. The prenisin is subsequently exported by the ABC transporter NisT and extracellularly processed by the peptidase NisP. L. lactis expressing the nisBTC genes can modify and secrete a wide range of nonlantibi

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Bakhtiary, Alireza, Stephen A. Cochrane, Pascal Mercier, et al. "Insights into the Mechanism of Action of the Two-Peptide Lantibiotic Lacticin 3147." Journal of the American Chemical Society 139, no. 49 (2017): 17803–10. http://dx.doi.org/10.1021/jacs.7b04728.

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Dischinger, Jasmin, Michaele Josten, Christiane Szekat, Hans-Georg Sahl, and Gabriele Bierbaum. "Production of the Novel Two-Peptide Lantibiotic Lichenicidin by Bacillus licheniformis DSM 13." PLoS ONE 4, no. 8 (2009): e6788. http://dx.doi.org/10.1371/journal.pone.0006788.

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Stein, Torsten, Stefan Heinzmann, Stefanie Düsterhus, Stefan Borchert, and Karl-Dieter Entian. "Expression and Functional Analysis of the Subtilin Immunity Genes spaIFEG in the Subtilin-Sensitive Host Bacillus subtilis MO1099." Journal of Bacteriology 187, no. 3 (2005): 822–28. http://dx.doi.org/10.1128/jb.187.3.822-828.2005.

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ABSTRACT Bacillus subtilis ATCC 6633 produces the cationic pore-forming lantibiotic subtilin, which preferentially acts on gram-positive microorganisms; self protection of the producer cells is mediated by the four genes spaIFEG. To elucidate the mechanism of subtilin autoimmunity, we transferred different combinations of subtilin immunity genes under the control of an inducible promoter into the genome of subtilin-sensitive host strain B. subtilis MO1099. Recipient cells acquired subtilin tolerance through expression of either spaI or spaFEG, which shows that subtilin immunity is based on two

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Masuda, Y., T. Zendo, and K. Sonomoto. "New type non-lantibiotic bacteriocins: circular and leaderless bacteriocins." Beneficial Microbes 3, no. 1 (2012): 3–12. http://dx.doi.org/10.3920/bm2011.0047.

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Bacteriocins are antimicrobial peptides that are ribosomally synthesised by bacteria. Bacteriocins produced by Gram-positive bacteria, including lactic acid bacteria, are under focus as the next generation of safe natural biopreservatives and as therapeutic alternatives to antibiotics. Recently, two novel types of non-lantibiotic class II bacteriocins have been reported with unique characteristics in their structure and biosynthesis mechanism. One is a circular bacteriocin that contains a head-to-tail structure in the mature form, and the other is a leaderless bacteriocin without an N-terminal

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Guder, André, Tim Schmitter, Imke Wiedemann, Hans-Georg Sahl, and Gabriele Bierbaum. "Role of the Single Regulator MrsR1 and the Two-Component System MrsR2/K2 in the Regulation of Mersacidin Production and Immunity." Applied and Environmental Microbiology 68, no. 1 (2002): 106–13. http://dx.doi.org/10.1128/aem.68.1.106-113.2002.

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ABSTRACT The lantibiotic mersacidin is an antimicrobial peptide of 20 amino acids which inhibits bacterial cell wall biosynthesis by binding to the precursor molecule lipid II and which is produced by Bacillus sp. strain HIL Y-85,54728. The structural gene of mersacidin as well as accessory genes is organized in a biosynthetic gene cluster which is located on the chromosome and contains three open reading frames with similarities to regulatory proteins: mrsR2 and mrsK2 encode two proteins with homology to bacterial two-component systems, and mrsR1 shows similarity to a response regulator. Both

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Lawton, Elaine M., Paul D. Cotter, Colin Hill, and R. Paul Ross. "Identification of a novel two-peptide lantibiotic, Haloduracin, produced by the alkaliphileBacillus haloduransC-125." FEMS Microbiology Letters 267, no. 1 (2007): 64–71. http://dx.doi.org/10.1111/j.1574-6968.2006.00539.x.

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Martinez-Cuesta, M. C., G. Buist, J. Kok, et al. "Biological and molecular characterization of a two-peptide lantibiotic produced by Lactococcus lactis IFPL105." Journal of Applied Microbiology 89, no. 2 (2000): 249–60. http://dx.doi.org/10.1046/j.1365-2672.2000.01103.x.

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He, Zengguo, Duygu Kisla, Liwen Zhang, Chunhua Yuan, Kari B. Green-Church, and Ahmed E. Yousef. "Isolation and Identification of a Paenibacillus polymyxa Strain That Coproduces a Novel Lantibiotic and Polymyxin." Applied and Environmental Microbiology 73, no. 1 (2006): 168–78. http://dx.doi.org/10.1128/aem.02023-06.

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ABSTRACT A new bacterial strain, displaying potent antimicrobial properties against gram-negative and gram-positive pathogenic bacteria, was isolated from food. Based on its phenotypical and biochemical properties as well as its 16S rRNA gene sequence, the bacterium was identified as Paenibacillus polymyxa and it was designated as strain OSY-DF. The antimicrobials produced by this strain were isolated from the fermentation broth and subsequently analyzed by liquid chromatography-mass spectrometry. Two antimicrobials were found: a known antibiotic, polymyxin E1, which is active against gram-neg

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Draper, Lorraine A., Paul D. Cotter, Colin Hill, and R. Ross. "The two peptide lantibiotic lacticin 3147 acts synergistically with polymyxin to inhibit Gram negative bacteria." BMC Microbiology 13, no. 1 (2013): 212. http://dx.doi.org/10.1186/1471-2180-13-212.

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Morgan, Sheila M., Paula M. O'Connor, Paul D. Cotter, R. Paul Ross, and Colin Hill. "Sequential Actions of the Two Component Peptides of the Lantibiotic Lacticin 3147 Explain Its Antimicrobial Activity at Nanomolar Concentrations." Antimicrobial Agents and Chemotherapy 49, no. 7 (2005): 2606–11. http://dx.doi.org/10.1128/aac.49.7.2606-2611.2005.

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ABSTRACT Lacticin 3147 is a two-peptide (LtnA1 and LtnA2) lantibiotic produced by Lactococcus lactis subsp. lactis DPC3147 and has inhibitory activity against all gram-positive microorganisms tested. In this study the specific activities of the component peptides (alone or in combination) were determined by using L. lactis subsp. cremoris HP as the target strain. Lacticin 3147 exhibited an MIC50 of 7 nM for each component peptide (in combination), suggesting a peptide stoichiometry of 1:1. Interestingly, the LtnA1 peptide demonstrated independent inhibitory activity, with an MIC50 of 200 nM ag

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McAuliffe, Olivia, Colin Hill, and R. Paul Ross. "Each peptide of the two-component lantibiotic lacticin 3147 requires a separate modification enzyme for activity." Microbiology 146, no. 9 (2000): 2147–54. http://dx.doi.org/10.1099/00221287-146-9-2147.

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Valsesia, G., G. Medaglia, M. Held, W. Minas, and S. Panke. "Circumventing the Effect of Product Toxicity: Development of a Novel Two-Stage Production Process for the Lantibiotic Gallidermin." Applied and Environmental Microbiology 73, no. 5 (2006): 1635–45. http://dx.doi.org/10.1128/aem.01969-06.

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ABSTRACT Lantibiotics such as gallidermin are lanthionine-containing polypeptide antibiotics produced by gram-positive bacteria that might become relevant for the treatment of various infectious diseases. So far, self-toxicity has prevented the isolation of efficient overproducing strains, thus hampering their thorough investigation and preventing their exploitation in fields other than the food area. We wanted to investigate the effect of lantibiotic precursor peptides on the producing strains in order to evaluate novel strategies for the overproduction of these promising peptides. In this st

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Nguyen, Trang, Zhijun Zhang, I.-Hsiu Huang, et al. "Genes involved in the repression of mutacin I production in Streptococcus mutans." Microbiology 155, no. 2 (2009): 551–56. http://dx.doi.org/10.1099/mic.0.021303-0.

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Streptococcus mutans is considered a primary pathogen for human dental caries. Its ability to produce a variety of peptide antibiotics called mutacins may play an important role in its invasion and establishment in the dental biofilm. S. mutans strain UA140 produces two types of mutacins, the lantibiotic mutacin I and the non-lantibiotic mutacin IV. In a previous study, we constructed a random insertional-mutation library to screen for genes involved in regulating mutacin I production, and found 25 genes/operons that have a positive effect on mutacin I production. In this study, we continued o

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Sugrue, Ivan, Daragh Hill, Paula M. O’Connor, et al. "Nisin E Is a Novel Nisin Variant Produced by Multiple Streptococcus equinus Strains." Microorganisms 11, no. 2 (2023): 427. http://dx.doi.org/10.3390/microorganisms11020427.

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Nisin A, the prototypical lantibiotic, is an antimicrobial peptide currently utilised as a food preservative, with potential for therapeutic applications. Here, we describe nisin E, a novel nisin variant produced by two Streptococcus equinus strains, APC4007 and APC4008, isolated from sheep milk. Shotgun whole genome sequencing and analysis revealed biosynthetic gene clusters similar to nisin U, with a unique rearrangement of the core peptide encoding gene within the cluster. The 3100.8 Da peptide by MALDI-TOF mass spectrometry, is 75% identical to nisin A, with 10 differences, including 2 del

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Field, Des, Barry Collins, Paul D. Cotter, Colin Hill, and R. Paul Ross. "A System for the Random Mutagenesis of the Two-Peptide Lantibiotic Lacticin 3147: Analysis of Mutants Producing Reduced Antibacterial Activities." Journal of Molecular Microbiology and Biotechnology 13, no. 4 (2007): 226–34. http://dx.doi.org/10.1159/000104747.

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Zheng, Guolu, Liang Z. Yan, John C. Vederas, and Peter Zuber. "Genes of the sbo-alb Locus ofBacillus subtilis Are Required for Production of the Antilisterial Bacteriocin Subtilosin." Journal of Bacteriology 181, no. 23 (1999): 7346–55. http://dx.doi.org/10.1128/jb.181.23.7346-7355.1999.

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ABSTRACT Bacillus subtilis JH642 and a wild strain of B. subtilis called 22a both produce an antilisterial peptide that can be purified by anion-exchange and gel filtration chromatography. Amino acid analysis confirmed that the substance was the cyclic bacteriocin subtilosin. A mutant defective in production of the substance was isolated from a plasmid gene disruption library. The plasmid insertion conferring the antilisterial-peptide-negative phenotype was located in a seven-gene operon (alb, for antilisterial bacteriocin) residing immediately downstream from thesbo gene, which encodes the pr

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Ni, Jianqiang, Kunling Teng, Gang Liu, Caixia Qiao, Liandong Huan, and Jin Zhong. "Autoregulation of Lantibiotic Bovicin HJ50 Biosynthesis by the BovK-BovR Two-Component Signal Transduction System inStreptococcus bovisHJ50." Applied and Environmental Microbiology 77, no. 2 (2010): 407–15. http://dx.doi.org/10.1128/aem.01278-10.

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ABSTRACTStreptococcus bovisHJ50 produces a lacticin 481-like 33-amino-acid-residue lantibiotic, designated bovicin HJ50.bovK-bovRin the bovicin HJ50 biosynthetic gene cluster is predicted to be a two-component signal transduction system involved in sensing signals and regulating gene expression. Disruption ofbovKorbovRresulted in the abrogation of bovicin HJ50 production, suggesting both genes play important roles in bovicin HJ50 biosynthesis. Addition of exogenous bovicin HJ50 peptide to cultures of abovMmutant that lost the capability for bovicin HJ50 production and structural genebovAtransc

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Richard, Audrey Stéphanie, Adam Zhang, Sun-Jin Park, Michael Farzan, Min Zong, and Hyeryun Choe. "Virion-associated phosphatidylethanolamine promotes TIM1-mediated infection by Ebola, dengue, and West Nile viruses." Proceedings of the National Academy of Sciences 112, no. 47 (2015): 14682–87. http://dx.doi.org/10.1073/pnas.1508095112.

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Phosphatidylserine (PS) receptors contribute to two crucial biological processes: apoptotic clearance and entry of many enveloped viruses. In both cases, they recognize PS exposed on the plasma membrane. Here we demonstrate that phosphatidylethanolamine (PE) is also a ligand for PS receptors and that this phospholipid mediates phagocytosis and viral entry. We show that a subset of PS receptors, including T-cell immunoglobulin (Ig) mucin domain protein 1 (TIM1), efficiently bind PE. We further show that PE is present in the virions of flaviviruses and filoviruses, and that the PE-specific cycli

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Christophers, Meg, Lauren Heng, and Nicholas Heng. "Nisin E, a New Nisin Variant Produced by Streptococcus equinus MDC1." Applied Sciences 13, no. 2 (2023): 1186. http://dx.doi.org/10.3390/app13021186.

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Members of the genus Streptococcus inhabit a variety of sites in humans and other animals and some species are prolific producers of proteinaceous antibiotics (bacteriocins). As little is known about (i) streptococci inhabiting domestic pets, and (ii) whether novel bacteriocin-producing streptococci can be isolated from domestic pets, the aim of this study is to address these gaps in the research literature. In this study, Streptococcus equinus MDC1, isolated from a healthy dog, was found to exhibit potent antibacterial activity against Micrococcus luteus in a simultaneous antagonism assay, su

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Lim, Kong Boon, Marilen P. Balolong, Sang Hoon Kim, Ju Kyoung Oh, Ji Yoon Lee, and Dae-Kyung Kang. "Isolation and Characterization of a Broad Spectrum Bacteriocin fromBacillus amyloliquefaciensRX7." BioMed Research International 2016 (2016): 1–7. http://dx.doi.org/10.1155/2016/8521476.

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We isolated aBacillusstrain, RX7, with inhibitory activity againstListeria monocytogenesfrom soil and identified it asBacillus amyloliquefaciensbased on 16S rRNA gene sequencing. The inhibitory activity was stable over a wide range of pH and was fully retained after 30 min at 80°C, after which it decreased gradually at higher temperatures. The activity was sensitive to the proteolytic action ofα-chymotrypsin, proteinase-K, and trypsin, indicating its proteinaceous nature. This bacteriocin was active against a broad spectrum of bacteria and the fungusCandida albicans. Direct detection of antimi

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