Lantibiotics: How do producers become self-protected?

Alkhatib, Zainab; Abts, André; Mavaro, Antonino; Schmitt, Lutz; Smits, Sander H. J.

doi:10.1016/j.jbiotec.2012.01.032

Cited by 64 publications

(63 citation statements)

References 77 publications

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“…The lack of an equivalent to the immunity protein, NisI, can have negative implications for bacteriocin production by the producing cell (41,42). The yield of nisin H from the culture supernatant is low relative to that of nisin A, a finding initially attributed to the lack of a nisI immunity gene.…”

Section: Discussionmentioning

confidence: 99%

Nisin H Is a New Nisin Variant Produced by the Gut-Derived Strain Streptococcus hyointestinalis DPC6484

O’Connor

O’Shea

Guinane

et al. 2015

Appl Environ Microbiol

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dAccumulating evidence suggests that bacteriocin production represents a probiotic trait for intestinal strains to promote dominance, fight infection, and even signal the immune system. In this respect, in a previous study, we isolated from the porcine intestine a strain of Streptococcus hyointestinalis DPC6484 that displays antimicrobial activity against a wide range of Grampositive bacteria and produces a bacteriocin with a mass of 3,453 Da. Interestingly, the strain was also found to be immune to a nisin-producing strain. Genome sequencing revealed the genetic determinants responsible for a novel version of nisin, designated nisin H, consisting of the nshABTCPRKGEF genes, with transposases encoded between nshP and nshR and between nshK and nshG. A similar gene cluster is also found in S. hyointestinalis LMG14581. Notably, the cluster lacks an equivalent of the nisin immunity gene, nisI. Nisin H is proposed to have the same structure as the prototypical nisin A but differs at 5 amino acid positions-Ile1Phe (i.e., at position 1, nisin A has Ile while nisin H has Phe), Leu6Met, Gly18Dhb (threonine dehydrated to dehydrobutyrine), Met21Tyr, and His31Lys--and appears to represent an intermediate between the lactococcal nisin A and the streptococcal nisin U variant of nisin. Purified nisin H inhibits a wide range of Gram-positive bacteria, including staphylococci, streptococci, Listeria spp., bacilli, and enterococci. It represents the first example of a natural nisin variant produced by an intestinal isolate of streptococcal origin.

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Section: Discussionmentioning

confidence: 99%

Nisin H Is a New Nisin Variant Produced by the Gut-Derived Strain Streptococcus hyointestinalis DPC6484

O’Connor

O’Shea

Guinane

et al. 2015

Appl Environ Microbiol

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“…NMR spectra were acquired at 25°C on Bruker AVANCE 600, 700, 800, 900, and 950 MHz spectrometers equipped with cryogenic triple resonance probes. The proton chemical shifts were internally referenced to 2.2-dimethyl-2-silapentane-5-sulfonic acid and the heteronuclear 13 C and 15 N chemical shifts were indirectly referenced with the appropriate conversion factors (29). All spectra were processed using Bruker TopSpin TM 2.1/3.2 and analyzed using the programs CARA (30) and CcpNmr Analysis (31).…”

Section: Methodsmentioning

confidence: 99%

“…Structure Calculation-Distance restraints based on nuclear Overhauser effect (NOE) were obtained from 15 N-NOESY-HSQC, 13 C-NOESY-HSQC (aliphatic carbons), and 13 C-NOESY-HSQC (aromatic carbons) experiments in H 2 O with mixing times of 120 ms. Torsion angle restraints were calculated using TALOS-N (37) based on backbone H, N, C␣, C␤, and CO chemical shifts and used for all residues with { 1 H}, 15 NhetNOE values Ͼ0.5.…”

Section: Methodsmentioning

confidence: 99%

“…Thus, lantibiotic producer strains possess a so-called immunity system. The immunity system of many lantibiotic producers consists of an ABC transporter LanFEG and an immunity protein LanI (11)(12)(13). Its expression is regulated by the extracellular concentration of the lantibiotic through a twocomponent system with a sensor histidine kinase LanK and a response regulator LanR (14,15).…”

mentioning

confidence: 99%

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The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin

Hacker

Christ

Duchardt‐Ferner

et al. 2015

Journal of Biological Chemistry

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Background:The lipoprotein NisI confers immunity to Lactococcus lactis against its own lantibiotic nisin. Results: NisI contains a membrane and a nisin binding domain both with the same fold as SpaI from Bacillus subtilis. Conclusion: The C-terminal domain of NisI interacts directly and specifically with nisin. Significance: Our results help to understand the mechanism of the NisI mediated immunity against nisin on a structural level.

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“…For example, lantibiotics such as nisin or mersacidin bind to lipid II directly (1)(2)(3), whereas the non-ribosomally synthesized bacitracin prevents the dephosphorylation and recycling of the lipid carrier undecaprenyl-pyrophosphate (4). For self-protection, producer strains of antimicrobial peptides express so-called immunity proteins, summarily referred to as LanI, as well as ATP-binding cassette (ABC) transporters of the LanFEG or BcrAB type (5)(6)(7)(8).…”

mentioning

confidence: 99%

Identification of Regions Important for Resistance and Signalling within the Antimicrobial Peptide Transporter BceAB of Bacillus subtilis

Kallenberg

Dintner

Schmitz

et al. 2013

Journal of Bacteriology

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In the low-G؉C-content Gram-positive bacteria, resistance to antimicrobial peptides is often mediated by so-called resistance modules. These consist of a two-component system and an ATP-binding cassette transporter and are characterized by an unusual mode of signal transduction where the transporter acts as a sensor of antimicrobial peptides, because the histidine kinase alone cannot detect the substrates directly. Thus, the transporters fulfill a dual function as sensors and detoxification systems to confer resistance, but the mechanistic details of these processes are unknown. The paradigm and best-understood example for this is the BceRS-BceAB module of Bacillus subtilis, which mediates resistance to bacitracin, mersacidin, and actagardine. Using a random mutagenesis approach, we here show that mutations that affect specific functions of the transporter BceAB are primarily found in the C-terminal region of the permease, BceB, particularly in the eighth transmembrane helix. Further, we show that while signaling and resistance are functionally interconnected, several mutations could be identified that strongly affected one activity of the transporter but had only minor effects on the other. Thus, a partial genetic separation of the two properties could be achieved by single amino acid replacements, providing first insights into the signaling mechanism of these unusual modules.

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Lantibiotics: How do producers become self-protected?

Cited by 64 publications

References 77 publications

Nisin H Is a New Nisin Variant Produced by the Gut-Derived Strain Streptococcus hyointestinalis DPC6484

Nisin H Is a New Nisin Variant Produced by the Gut-Derived Strain Streptococcus hyointestinalis DPC6484

The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin

Identification of Regions Important for Resistance and Signalling within the Antimicrobial Peptide Transporter BceAB of Bacillus subtilis

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