Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci

Brumfitt, W.; Saltón, M. R. J.; Hamilton‐Miller, J. M. T.

doi:10.1093/jac/dkf190

Cited by 143 publications

(102 citation statements)

References 12 publications

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“…After centrifugation at room temperature for 20 min at 10,000 rpm, the culture supernatants were diluted with equal amounts of methanol and were loaded onto StrataX solid-phase extraction (SPE) cartridges (particle size, 33 m; Phenomenex, Aschaffenburg, Germany). After a wash with 70% methanol-0.1% trifluoroacetic acid (TFA), which led to elution of the truncated S-entianin fragment comprising amino acids 1 to 19 (fragment [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19], intact entianin, succinylated entianin (S-entianin), and succinylated subtilin (S-subtilin) were eluted with 99.9% methanol-0.1% TFA, dried, and stored at Ϫ20°C.…”

Section: Methodsmentioning

confidence: 99%

“…The protein concentrations of these stock solutions were determined by the micro-bicinchoninic acid (micro-BCA) method (35) using a bovine albumin standard of known concentration for quantification. Additionally, solutions of S-entianin and S-entianin [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] were quantified without previous dilution to identical HPLC peak integrals. The concentrations in the stock solutions were determined to be 3.7 M S-subtilin and 3.2 M S-entianin; 3.4 M S-entianin and 3.5 M entianin; and 2.9 M S-entianin and 15.3 M S-entianin [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] .…”

Section: Methodsmentioning

confidence: 99%

“…Whereas B. subtilis DSM 15029 T produced a considerable amount of free entianin, the B. subtilis laboratory strain ATCC 6633 produced succinylated subtilin almost exclusively (data not shown). In addition to entianin and Sentianin, two peptide fragments without antibiotic activity, corresponding to the N-terminal fragment entianin [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] and the C-terminal fragment entianin [20][21][22][23][24][25][26][27][28][29][30][31][32] , were eluted as distinct peaks from the C 18 column (Fig. 1, right).…”

Section: Entianin a New Lantibiotic From B Subtilis Dsm 15029mentioning

confidence: 99%

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Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 ^T with High Antimicrobial Activity

Fuchs

Jaskolla

Bochmann

et al. 2011

Appl Environ Microbiol

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Lantibiotics, such as nisin and subtilin, are lanthionine-containing peptides that exhibit antimicrobial as well as pheromone-like autoinducing activity. Autoinduction is specific for each lantibiotic, and reporter systems for nisin and subtilin autoinduction are available. In this report, we used the previously reported subtilin autoinduction bioassay in combination with mass spectrometric analyses to identify the novel subtilin-like lantibiotic entianin from Bacillus subtilis subsp. spizizenii DSM 15029T . Linearization of entianin using Raney nickel-catalyzed reductive cleavage enabled, for the first time, the use of tandem mass spectrometry for the fast and efficient determination of an entire lantibiotic primary structure, including posttranslational modifications. The amino acid sequence determined was verified by DNA sequencing of the etnS structural gene, which confirmed that entianin differs from subtilin at 3 amino acid positions. In contrast to B. subtilis ATCC 6633, which produces only small amounts of unsuccinylated subtilin, B. subtilis DSM 15029 T secretes considerable amounts of unsuccinylated entianin. Entianin was very active against several Gram-positive pathogens, such as Staphylococcus aureus and Enterococcus faecalis. The growth-inhibiting activity of succinylated entianin (S-entianin) was much lower than that of unsuccinylated entianin: a 40-fold higher concentration was required for inhibition. For succinylated subtilin (S-subtilin), a concentration 100-fold higher than that of unsuccinylated entianin was required to inhibit the growth of a B. subtilis test strain. This finding was in accordance with a strongly reduced sensing of cellular envelope stress provided by S-entianin relative to that of entianin. Remarkably, S-entianin and S-subtilin showed considerable autoinduction activity, clearly demonstrating that autoinduction and antibiotic activity underlie different molecular mechanisms.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Entianin a New Lantibiotic From B Subtilis Dsm 15029mentioning

confidence: 99%

See 1 more Smart Citation

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 ^T with High Antimicrobial Activity

Fuchs

Jaskolla

Bochmann

et al. 2011

Appl Environ Microbiol

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show abstract

“…Nevertheless, we also expect more applications of class IIa bacteriocins in the medical area as antibiotic complements, since encouraging examples have been reported for nisin (a class I bacteriocin) in the treatment of infections caused by Pseudomonas aeruginosa (71) and methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci (21 …”

Section: Concluding Remarks and Future Prospectsmentioning

confidence: 99%

The Continuing Story of Class IIa Bacteriocins

Drider

Fimland

Héchard

et al. 2006

Microbiol Mol Biol Rev

637

543

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SUMMARY Many bacteria produce antimicrobial peptides, which are also referred to as peptide bacteriocins. The class IIa bacteriocins, often designated pediocin-like bacteriocins, constitute the most dominant group of antimicrobial peptides produced by lactic acid bacteria. The bacteriocins that belong to this class are structurally related and kill target cells by membrane permeabilization. Despite their structural similarity, class IIa bacteriocins display different target cell specificities. In the search for new antibiotic substances, the class IIa bacteriocins have been identified as promising new candidates and have thus received much attention. They kill some pathogenic bacteria (e.g., Listeria) with high efficiency, and they constitute a good model system for structure-function analyses of antimicrobial peptides in general. This review focuses on class IIa bacteriocins, especially on their structure, function, mode of action, biosynthesis, bacteriocin immunity, and current food applications. The genetics and biosynthesis of class IIa bacteriocins are well understood. The bacteriocins are ribosomally synthesized with an N-terminal leader sequence, which is cleaved off upon secretion. After externalization, the class IIa bacteriocins attach to potential target cells and, through electrostatic and hydrophobic interactions, subsequently permeabilize the cell membrane of sensitive cells. Recent observations suggest that a chiral interaction and possibly the presence of a mannose permease protein on the target cell surface are required for a bacteria to be sensitive to class IIa bacteriocins. There is also substantial evidence that the C-terminal half penetrates into the target cell membrane, and it plays an important role in determining the target cell specificity of these bacteriocins. Immunity proteins protect the bacteriocin producer from the bacteriocin it secretes. The three-dimensional structures of two class IIa immunity proteins have been determined, and it has been shown that the C-terminal halves of these cytosolic four-helix bundle proteins specify which class IIa bacteriocin they protect against.

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“…Over the past 20 years there has been an increasing interest in such compounds as possible preservative agents for food and as potential supplements or replacements for currently used antibiotics. Many lantibiotics show promising activity towards a variety of pathogenic bacteria including methicillinresistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococcus (VRE) [43].…”

Section: Lantibioticsmentioning

confidence: 99%

The Expanding Role of Lipid II as a Target for Lantibiotics

Martin

Breukink

2007

Future Microbiol.

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Lipid II is an essential cell-wall precursor required for the growth and replication of both Gram-positive and Gram-negative bacteria. Compounds that use lipid II to selectively target bacterial cells for destruction represent an important class of antibiotics. Clinically, vancomycin is the most important example of an antibiotic that operates in this manner. Despite being considered the ‘antibiotic drug of last resort’, significant bacterial resistance to vancomycin now manifests itself worldwide. In this paper we review recent progress made in understanding the lipid II-associated antibacterial characteristics of various naturally occurring compounds, with particular focus on the lantibiotic peptides.

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Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci

Abstract: Observations of synergy between nisin and ramoplanin against MRSA and VRE offer a promising approach to the concept of combining nisin with inhibitors of cell wall peptidoglycan. Further investigations are needed in order to develop this approach as a clinical possibility.

Cited by 143 publications

References 12 publications

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 ^T with High Antimicrobial Activity

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 ^T with High Antimicrobial Activity

The Continuing Story of Class IIa Bacteriocins

The Expanding Role of Lipid II as a Target for Lantibiotics

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Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci

Abstract: Observations of synergy between nisin and ramoplanin against MRSA and VRE offer a promising approach to the concept of combining nisin with inhibitors of cell wall peptidoglycan. Further investigations are needed in order to develop this approach as a clinical possibility.

Cited by 143 publications

References 12 publications

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 T with High Antimicrobial Activity

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 T with High Antimicrobial Activity

The Continuing Story of Class IIa Bacteriocins

The Expanding Role of Lipid II as a Target for Lantibiotics

Contact Info

Product

Resources

About

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 ^T with High Antimicrobial Activity

Entianin, a Novel Subtilin-Like Lantibiotic from Bacillus subtilis subsp. spizizenii DSM 15029 ^T with High Antimicrobial Activity