Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product

Kaletta, Cortina; Entian, Karl‐Dieter

doi:10.1128/jb.171.3.1597-1601.1989

Cited by 257 publications

(166 citation statements)

References 32 publications

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“…Amino acid sequences of representative bacteriocins from different classes: (a) nisin from class I [72]; (b) pediocin PA-1 from class IIa; (c) plantaricins EF and JK from class IIb [73]; (d) garvicin ML from class IIc [74]; and (e) enterocin Q from class IId [75]. The sequences of the peptides that form plantaricins EF and JK have been shown in the order of plantaricin E, plantaricin F, plantaricin J and plantaricin K. The red, blue and yellow amino acids represent acidic amino acids, basic amino acids and uncommon amino acids (Dhb, didehydroaminobutyric acid; Dha, didehydroalanine; Abu, 2-aminobutyric acid), respectively.…”

Section: Bacteriocinsmentioning

confidence: 99%

Modulation of the gut microbiota by prebiotic fibres and bacteriocins

Umu

Rudi

Diep

2017

Microbial Ecology in Health and Disease

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The gut microbiota is considered an organ that co-develops with the host throughout its life. The composition and metabolic activities of the gut microbiota are subject to a complex interplay between the host genetics and environmental factors, such as lifestyle, diet, stress and antimicrobials. It is evident that certain prebiotics, and antimicrobials produced by lactic acid bacteria (LAB), can shape the composition of the gut microbiota and its metabolic activities to promote host health and/or prevent diseases. In this review, we aim to give an overview of the impact of prebiotic fibres, and bacteriocins from LAB, on the gut microbiota and its activities, which affect the physiology and health of the host. These represent two different mechanisms in modulating the gut microbiota, the first involving exploitative competition by which the growth of beneficial bacteria is promoted and the latter involving interference competition by which the growth of pathogens and other unwanted bacteria is prevented. For interference competition in the gut, bacteriocins offer special advantages over traditional antibiotics, in that they can be designed to act towards specific unwanted bacteria and other pathogens, without any remarkable collateral effects on beneficial microbes sharing the same niche.

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Section: Bacteriocinsmentioning

confidence: 99%

Modulation of the gut microbiota by prebiotic fibres and bacteriocins

Umu

Rudi

Diep

2017

Microbial Ecology in Health and Disease

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“…The first lan-!ibiotic to be characterised was nisin, produced by strains of Lactococcus lactis carrying a transposon containing genes coding for the nisin precursor and for proteins involved in aisin biosynthesis and resistance [2][3][4][5]. Nisin has been quite videly used as a food preservative, notably in cheese and ,~ther dairy products and in canned vegetables, for some 30 .,ears [6,7].…”

Section: ~ Introductionmentioning

confidence: 99%

Structure‐activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin

Chan¹,

Leyland²,

Clark³

et al. 1996

FEBS Letters

122

160

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The post-translationally modified peptide antibiotic nisin has been cleaved by a number of proteases and the fragments produced purified, characterised chemically, and assayed for activity in inhibiting the growth of Lactococcus lactis MG1614 and Micrococcus luteus NCDO8166. These results provide information on the importance of different parts of the nisin molecule for its growth-inhibition activity. Removal of the C-terminal five residues leads to approximately a 10-fold decrease in potency, while removal of a further nine residues, encompassing two of the lanthionine rings, leads to a 100-fold decrease. There are some differences between analogous fragments of nisin and subtilin, suggesting possible subtle differences in mode of action. Cleavage within, or removal of, lanthionine ring C essentially abolishes the activity of nisin. The fragment ulsin t-12 is inactive itself, and specifically antagonises the growth-inhibitory action of nisin. These results are discussed in lerms of current models for the mechanism of action of nisin.Key words: Nisin; Lantibiotic; Peptide antibiotic; I'roteolysis; Structure-activity relationships mation of voltage-dependent pores in biological membranes [8][9][10], although recent evidence indicates that the inhibition of the outgrowth of spores by nisin and subtilin takes place by a different mechanism [11,12]. We have been studying the structure-activity relationships in nisin and subtilin, by both genetic and chemical modification of the structure [12][13][14][15][16][17][18][19][20], with a view to understanding their mechanism of action and to developing new derivatives with desirable properties. We now report the preparation, characterisation and anti-bacterial activity of a number of proteolytic fragments of nisin and subtilin, which allow us to define the parts of the molecule most important for biological activity. Materials and methodsNisin and subtilin were prepared as previously described [14,15]; [Ser33]-nisin, in which the serine residue at position 33 has escaped processing to a dehydroalanine residue, was isolated as a minor component of commercial nisin. All proteases were obtained from Sigma Chemical Co., Poole, Dorset, UK. ~. IntroductionThe post-translationally modified peptide antibiotics known :ts 'lantibiotics' contain cyclic structures formed by lanthioaine or 3-methyl-lanthionine residues, and often also dehydroalanine and/or dehydrobutyrine residues [1]. The first lan-!ibiotic to be characterised was nisin, produced by strains of Lactococcus lactis carrying a transposon containing genes coding for the nisin precursor and for proteins involved in aisin biosynthesis and resistance [2][3][4][5]. Nisin has been quite videly used as a food preservative, notably in cheese and ,~ther dairy products and in canned vegetables, for some 30 .,ears [6,7]. It inhibits the growth of a wide range of Gram~ositive organisms, and also inhibits the germination and/or mtgrowth of spores of Bacillus and Clostridium species [6]. Fhe growth-inhibitory activity of nisi...

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“…To avoid possible anchoring and export of NisI in E. coli, the NisI lipoprotein signal sequence and the anchoring Cys residue (amino acids [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] were substituted by the sequence MRSGSHHHHHH, resulting in the protein His 6 -NisI. Recombinant His 6 -NisI from E. coli (Fig.…”

Section: Fusion Of Nisi To Nisfeg and Transfer To The Chromosome Of Bmentioning

confidence: 99%

Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis

Stein

Heinzmann

Solovieva

et al. 2003

Journal of Biological Chemistry

162

240

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Nisin-producing Lactococcus lactis strains show a high degree of resistance to the action of nisin, which is based upon expression of the self-protection (immunity) genes nisI, nisF, nisE, and nisG. Different combinations of nisin immunity genes were integrated into the chromosome of a nisin-sensitive Bacillus subtilis host strain under the control of an inducible promoter. For the recipient strain, the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes. But either the lipoprotein NisI or the ABC transporter-homologous system Nis-FEG, respectively, were also able to protect the Bacillus host cells. The acquired immunity was specific to nisin and provided no tolerance to subtilin, a closely related lantibiotic. Quantitative in vivo peptide release assays demonstrated that NisFEG diminished the quantity of cell-associated nisin, providing evidence that one role of NisFEG is to transport nisin from the membrane into the extracellular space. NisI solubilized from B. subtilis membrane vesicles and recombinant hexahistidinetagged NisI from Escherichia coli interacted specifically with nisin and not with subtilin. This suggests a function of NisI as a nisin-intercepting protein.In recent years peptide antibiotics have gained increasing attention as therapeutics (1, 2) and food preservatives (3). Nisin represents the most prominent member of lantibiotics, peptide antibiotics with intramolecular lanthionine bridges (4 -9). The nisin producer Lactococcus lactis 6F3 contains a gene cluster encoding proteins for the biosynthesis and transport (10 -14), immunity (15), and regulation (16 -18) of nisin. Subtilin (19,20) and ericin S (21) produced by Bacillus subtilis ATCC 6633 and A1/3, respectively, are closely related lantibiotics. Lantibiotics form voltage-dependent pores in the bacterial cytoplasmic membrane that are lethal for the target cells but also for the producer. For nisin, the mode of action was investigated in several model systems such as black lipid bilayers and membrane vesicles (22)(23)(24)(25). Recent findings demonstrated that specific binding of nisin to the cell wall precursor lipid II coincides with pore formation (26, 27). Specific selfprotection (immunity) mechanisms are necessary to protect the lantibiotic-producing organisms from the action of their own lantibiotics. For nisin and subtilin (28) Although numerous genes involved in lantibiotic immunity are known, the mechanism by which the encoded proteins confer immunity remain unclear. For full nisin or subtilin immunity, both are required, i.e. the lipoprotein as well as the immunity transporter. The lack of each component diminished the tolerance to nisin (35) or subtilin (28) significantly. Here we report for the first time on the establishment of nisin immunity in the heterologous host B. subtilis. Functional analyses of its different components provided evidence that NisI acts as a nisin-sequestering protein and that NisFEG acts as a nisin exporter that expels nisin molecules fro...

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Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product

Cited by 257 publications

References 32 publications

Modulation of the gut microbiota by prebiotic fibres and bacteriocins

Modulation of the gut microbiota by prebiotic fibres and bacteriocins

Structure‐activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin

Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis

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