Amylocyclicin, a Novel Circular Bacteriocin Produced by Bacillus amyloliquefaciens FZB42

Scholz, Romy; Vater, Joachim; Budiharjo, Anto; Wang, Zhiyuan; He, Yueqiu; Dietel, Kristin; Schwecke, Torsten; Herfort, Stefanie; Lasch, Peter; Borriss, Rainer

doi:10.1128/jb.01474-14

Cited by 190 publications

(130 citation statements)

References 42 publications

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“…A number of circular bacteriocins that are composed of 58 to 70 amino acid residues have been identified to date, including enterocin AS-48 (4), gassericin A (5), circularin A (6), butyrivibriocin AR10 (7), uberolysin (8), carnocyclin A (9), lactocyclicin Q (10), garvicin ML (11), leucocyclicin Q (12), amylocyclicin (13), and aureocyclicin 4185 (14). Another peptide exhibiting Nto C-terminal cyclization is subtilosin A (15).…”

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confidence: 99%

Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46

Acedo

Belkum

Lohans

et al. 2015

Appl Environ Microbiol

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Acidocin B, a bacteriocin produced by Lactobacillus acidophilus M46, was originally reported to be a linear peptide composed of 59 amino acid residues. However, its high sequence similarity to gassericin A, a circular bacteriocin from Lactobacillus gasseri LA39, suggested that acidocin B might be circular as well. Acidocin B was purified from culture supernatant by a series of hydrophobic interaction chromatographic steps. Its circular nature was ascertained by matrix-assisted laser desorption ionizationtime of flight (MALDI-TOF) mass spectrometry and tandem mass spectrometry (MS/MS) sequencing. The peptide sequence was found to consist of 58 amino acids with a molecular mass of 5,621.5 Da. The sequence of the acidocin B biosynthetic gene cluster was also determined and showed high nucleotide sequence similarity to that of gassericin A. The nuclear magnetic resonance (NMR) solution structure of acidocin B in sodium dodecyl sulfate micelles was elucidated, revealing that it is composed of four ␣-helices of similar length that are folded to form a compact, globular bundle with a central pore. This is a three-dimensional structure for a member of subgroup II circular bacteriocins, which are classified based on their isoelectric points of ϳ7 or lower.Comparison of acidocin B with carnocyclin A, a subgroup I circular bacteriocin with four ␣-helices and a pI of 10, revealed differences in the overall folding. The observed variations could be attributed to inherent diversity in their physical properties, which also required the use of different solvent systems for three-dimensional structural elucidation. C ircular bacteriocins are antimicrobial peptides that are ribosomally synthesized by bacteria and are posttranslationally modified to release a leader peptide and form a peptide bond between the N and C termini. These peptides exhibit antimicrobial activity against a broad range of Gram-positive bacteria, including Listeria spp. and Clostridium spp., which are common pathogens causing food-borne diseases (1). In addition, the circular nature of these bacteriocins imparts enhanced stability against proteolytic degradation and denaturation due to extreme temperature and pH conditions relative to linear forms (2). They thus serve as promising alternatives to traditional antimicrobial agents for food, medical, and industrial applications (3).A number of circular bacteriocins that are composed of 58 to 70 amino acid residues have been identified to date, including enterocin AS-48 (4), gassericin A (5), circularin A (6), butyrivibriocin AR10 (7), uberolysin (8), carnocyclin A (9), lactocyclicin Q (10), garvicin ML (11), leucocyclicin Q (12), amylocyclicin (13), and aureocyclicin 4185 (14). Another peptide exhibiting Nto C-terminal cyclization is subtilosin A (15). It is, however, considered a member of the sactipeptides, which represent a class of peptides containing cross-links between cysteine sulfurs and ␣-carbons (16). The structure and genetics of circular bacteriocins were reviewed previously (2). More recently, a re...

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confidence: 99%

Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46

Acedo

Belkum

Lohans

et al. 2015

Appl Environ Microbiol

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“…In the context of phytopathogen biocontrol, the antiSMASH analysis allowed to identify gene clusters encoding the enzymatic machinery for synthesis of nonribosomal peptides (surfactins, iturins, fengycins, bacillibactin, and bacilysin) and polyketides (bacillaene, difficidin, and macrolactin, Table 3). The antiSMASH analysis identified additional genes related to the production of other antimicrobials, such as the lantibiotic amylolysin (Arguelles-Arias et al, 2013), the bacteriocin amylocyclicin (Scholz et al, 2014), and the aminoglycoside antibiotic butirosin (Llewellyn et al, 2007), which have not been detected using chemical analysis in culture media of the strain to date (Debois et al, 2014). The genomic features of S499 thus clearly reflect its rootassociated lifestyle and its biocontrol potential.…”

Section: Resultsmentioning

confidence: 99%

Complete genome sequence of Bacillus amyloliquefaciens subsp. plantarum S499, a rhizobacterium that triggers plant defences and inhibits fungal phytopathogens

Molinatto

Puopolo

Sonego

et al. 2016

Journal of Biotechnology

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a b s t r a c tBacillus amyloliquefaciens subsp. plantarum S499 is a plant beneficial rhizobacterium with a good antagonistic potential against phytopathogens through the release of active secondary metabolites. Moreover, it can induce systemic resistance in plants by producing considerable amounts of surfactins. The complete genome sequence of B. amyloliquefaciens subsp. plantarum S499 includes a circular chromosome of 3,927,922 bp and a plasmid of 8,008 bp. A remarkable abundance in genomic regions of putative horizontal origin emerged from the analysis. Furthermore, we highlighted the presence of genes involved in the establishment of interactions with the host plants at the root level and in the competition with other soilborne microorganisms. More specifically, genes related to the synthesis of amylolysin, amylocyclicin, and butirosin were identified. These antimicrobials were not known before to be part of the antibiotic arsenal of the strain. The information embedded in the genome will support the upcoming studies regarding the application of B. amyloliquefaciens isolates as plant-growth promoters and biocontrol agents.

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“…A number of glycosylated bacteriocins and circular bacteriocins have recently been isolated from other Bacillus spp. 47,48 In addition to bacteriocins, Bacillus and Paenibacillus spp. are noted producers of a great number of antibacterial nonribosomal peptides.…”

Section: Antimicrobial Peptides Active Against C Jejuni From Bacillumentioning

confidence: 99%

Characterization of bacterial antimicrobial peptides active against Campylobacter jejuni

Lohans

Belkum

et al. 2015

Can. J. Chem.

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Abstract:Campylobacter jejuni is one of the major causes of food poisoning, often resulting from the consumption of improperly cooked poultry products. The emergence of C. jejuni strains resistant to conventional antibiotics necessitates the evaluation of other possible treatments or preventative measures to minimize the impact and prevalence of infections. Antimicrobial peptides produced by bacteria have begun to emerge as a potential means of decreasing the levels of C. jejuni in poultry, thereby limiting Campylobacter contamination in associated food products. A number of bacteriocins produced by Gram-positive bacteria have unexpectedly been described as having antimicrobial activity against the Gram-negative C. jejuni. Additionally, some nonribosomal lipopeptides produced by Bacillus and Paenibacillus spp. show efficacy against this pathogen. This review will describe the bacterial antimicrobial peptides reported to be active against C. jejuni, with an emphasis on the characterization of their primary structures. However, for many of these peptides, little is known about their amino acid sequences and structures. Furthermore, there are unusual inconsistencies associated with the reported amino acid sequences for several of the more well-studied bacteriocins. Clarifying the chemical nature of these promising antimicrobial peptides is necessary before their potential utility for livestock protection from C. jejuni can be fully explored. Once these peptides are better characterized, they may prove to be strong candidates for minimizing the impact of Campylobacter on human health.Key words: Campylobacter, bacteriocin, antimicrobial, lipopeptide, tridecaptin. Résumé :Campylobacter jejuni est l'un des agents les plus importants à l'origine de l'empoisonnement alimentaire, souvent dû à la consommation de produits de volaille cuits de manière inadéquate. L'émergence de souches de C. jejuni résistantes aux antibiotiques habituels exige d'évaluer les autres possibilités de traitements ou mesures préventives afin de réduire la préva-lence et les conséquences des infections. La possibilité d'utiliser les peptides antimicrobiens d'origine bactérienne pour diminuer les taux de C. jejuni dans la volaille et limiter ainsi la contamination des produits alimentaires dérivés par le Campylobacter est apparue récemment. De façon inattendue, un certain nombre de bactériocines produites par des bactéries à Gram positif ont été décrites comme ayant une activité antimicrobienne contre la bactérie à Gram négatif C. jejuni. De plus, certains lipopeptides d'origine non ribosomique produits par des espèces de Bacillus et Paenibacillus montrent une efficacité contre cet agent pathogène. Cet exposé de synthèse décrira les peptides antimicrobiens d'origine bactérienne dont l'activité contre C. jejuni est connue, et mettra l'accent sur la caractérisation de leur structure primaire. Cependant, on sait peu de choses de la séquence d'acides aminés et de la structure de plusieurs de ces peptides. En outre, les séquences d'acides aminés de plusi...

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Amylocyclicin, a Novel Circular Bacteriocin Produced by Bacillus amyloliquefaciens FZB42

Cited by 190 publications

References 42 publications

Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46

Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46

Complete genome sequence of Bacillus amyloliquefaciens subsp. plantarum S499, a rhizobacterium that triggers plant defences and inhibits fungal phytopathogens

Characterization of bacterial antimicrobial peptides active against Campylobacter jejuni

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