Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to α-Carbons of Phenylalanine and Threonine

Kawulka, Karen E.; Sprules, Tara; McKay, Roy T.; Mercier, Pascal; Diaper, C. M.; Zuber, Peter; Vederas, John C.

doi:10.1021/ja029654t

Cited by 118 publications

(103 citation statements)

References 8 publications

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“…In recent years, a new class of bacteriocins has been proposed, the circular bacteriocins, which are characterized by a covalent linkage between the N and C termini (26,31,36). To date, only seven circular bacteriocins from a diverse group of gram-positive organisms have been reported (36): AS-48 (37,43), butyrivibriocin AR10 (23), circularin A (32), gassericin A, and reutericin 6 (which are diastereomers) (25,27,28) and subtilosin A (29,30,53) and uberolysin (50). Acidocin B, which shows 98% sequence homology to gassericin A, is considered a putative circular protein (34).…”

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confidence: 99%

Isolation and Characterization of Carnocyclin A, a Novel Circular Bacteriocin Produced by Carnobacterium maltaromaticum UAL307

Martin‐Visscher¹,

Belkum²,

Garneau‐Tsodikova³

et al. 2008

Appl Environ Microbiol

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143

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Carnobacterium maltaromaticum UAL307, isolated from fresh pork, exhibits potent activity against a number of gram-positive organisms, including numerous Listeria species. Three bacteriocins were isolated from culture supernatant, and using matrix-assisted laser desorption ionization-time of flight mass spectrometry and Edman sequencing, two of these bacteriocins were identified as piscicolin 126 and carnobacteriocin BM1, both of which have previously been described. The remaining bacteriocin, with a molecular mass of 5,862 Da, could not be sequenced by traditional methods, suggesting that the peptide was either cyclic or N-terminally blocked. This bacteriocin showed remarkable stability over a wide temperature and pH range and was unaffected by a variety of proteases. After digestion with trypsin and ␣-chymotrypsin, the peptide was de novo sequenced by tandem mass spectrometry and a linear sequence deduced, consisting of 60 amino acids. Based on this sequence, the molecular mass was predicted to be 5,880 Da, 18 units higher than the observed molecular mass, which suggested that the peptide has a cyclic structure. Identification of the genetic sequence revealed that this peptide is circular, formed by a covalent linkage between the N and C termini following cleavage of a 4-residue peptide leader sequence. The results of structural studies suggest that the peptide is highly structured in aqueous conditions. This bacteriocin, named carnocyclin A, is the first reported example of a circular bacteriocin produced by Carnobacterium spp.

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confidence: 99%

Isolation and Characterization of Carnocyclin A, a Novel Circular Bacteriocin Produced by Carnobacterium maltaromaticum UAL307

Martin‐Visscher¹,

Belkum²,

Garneau‐Tsodikova³

et al. 2008

Appl Environ Microbiol

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143

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“…For example, a well-established bioindicator strain for sterilization control, ATCC 6633 (11), was investigated with respect to biosynthesis of the lantibiotic subtilin (4,8,16,27) and its regulation (26,28). In a series of B. subtilis strains production of the nonribosomally synthesized cyclic lipopeptides surfactin, fengycin, and the iturins, including mycosubtilin, with different compositions has been observed (9,18,20,31).Subtilosin is a macrocyclic bacteriocin with three intramolecular bridges (14,19). An acidic isoelectric point differentiates subtilosin from the basic lantibiotics (13, 24).…”

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confidence: 99%

“…Subtilosin is a macrocyclic bacteriocin with three intramolecular bridges (14,19). An acidic isoelectric point differentiates subtilosin from the basic lantibiotics (13,24).…”

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confidence: 99%

Subtilosin Production by Two Bacillus subtilis Subspecies and Variance of the sbo-alb Cluster

Stein

Düsterhus

Stroh

et al. 2004

Appl Environ Microbiol

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Eight different Bacillus subtilis strains and Bacillus atrophaeus were found to produce the bacteriocin subtilosin A. On the basis of the subtilosin gene (sbo) sequences two distinct classes of B. subtilis strains were distinguished, and they fell into the two B. subtilis subspecies (B. subtilis subsp. subtilis and B. subtilis subsp. spizizenii). The entire sequence of the subtilosin gene cluster of a B. subtilis subsp. spizizenii strain, B. subtilis ATCC 6633, was determined. This sequence exhibited a high level of homology to the sequence of the sbo-alb gene locus of B. subtilis 168. By using primer extension analysis the transcriptional start sites of sbo in B. subtilis strains ATCC 6633 and 168 were found to be 47 and 45 bp upstream of the sbo start codon, respectively. Our results provide insight into the incipient evolutionary divergence of the two B. subtilis subspecies.Almost 4% of the 4.2-Mbp Bacillus subtilis 168 genome codes for proteins similar to the proteins involved in the biosynthesis of antimicrobial metabolites (17). However, B. subtilis 168 produces only a few antibiotics because several of the biosynthetic pathways are not functional, most likely because of the X-ray mutation of the original Marburg strain (6). In contrast, various other B. subtilis wild-type strains produce characteristic cocktails of numerous peptide antibiotics (1, 18). For example, a well-established bioindicator strain for sterilization control, ATCC 6633 (11), was investigated with respect to biosynthesis of the lantibiotic subtilin (4,8,16,27) and its regulation (26,28). In a series of B. subtilis strains production of the nonribosomally synthesized cyclic lipopeptides surfactin, fengycin, and the iturins, including mycosubtilin, with different compositions has been observed (9,18,20,31).Subtilosin is a macrocyclic bacteriocin with three intramolecular bridges (14,19). An acidic isoelectric point differentiates subtilosin from the basic lantibiotics (13, 24). Subtilosin transcription is increased under oxygen-limited and anaerobic conditions (22; T. Stein, S. Düsterhus, A. Stroh, and K.-D. Entian, 10th Int. Conf. Bacilli, abstr. P103, p. 65, 1999). The production of mature subtilosin is based on the expression of the sbo-alb gene cluster encompassing the subtilosin structural gene sbo and genes involved in posttranslational modification and processing of presubtilosin and in immunity (34, 35).Here we describe subtilosin production by eight different B. subtilis wild-type strains and Bacillus atrophaeus. The sbo genes of these organisms, as well as the entire subtilosin gene cluster of B. subtilis ATCC 6633, were sequenced in order to analyze the genetic variation between B. subtilis wild-type strains. MATERIALS AND METHODSStrains and plasmids. Strains used in this work are listed in Table 1. Recombinant plasmids were amplified in Escherichia coli DH5␣ or TG1 grown in Luria-Bertani medium (GIBCO, Neu-Isenburg, Germany). B. subtilis was grown either on TY (0.8% tryptone, 0.5% yeast extract [Difco, Detroit, Mich.], 0.5% N...

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“…29,42,43 The sactibiot-ics (or sactipeptides), characterized by the presence of thioether bridges between cysteine thiols and ␣-carbons of other residues, have thus far exclusively been isolated from Bacillus spp. Sactibiotics such as subtilosin A, 44 thuricin CD, 45 and thurincin H 46 have been fully structurally characterized. A number of glycosylated bacteriocins and circular bacteriocins have recently been isolated from other Bacillus spp.…”

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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Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to α-Carbons of Phenylalanine and Threonine

Cited by 118 publications

References 8 publications

Isolation and Characterization of Carnocyclin A, a Novel Circular Bacteriocin Produced by Carnobacterium maltaromaticum UAL307

Isolation and Characterization of Carnocyclin A, a Novel Circular Bacteriocin Produced by Carnobacterium maltaromaticum UAL307

Subtilosin Production by Two Bacillus subtilis Subspecies and Variance of the sbo-alb Cluster

Characterization of bacterial antimicrobial peptides active against Campylobacter jejuni

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