Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2

Tulini, Fabrício Luiz; Lohans, Christopher T.; Bordon, Karla de Castro Figueiredo; Zheng, Jun; Arantes, Eliane Candiani; Vederas, John C.; Martinis, Elaine Cristina Pereira De

doi:10.1016/j.ijfoodmicro.2013.12.019

Cited by 35 publications

(27 citation statements)

References 32 publications

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“…The class II bacteriocins are subdivided into five sub-classes by Cotter et al (2013). Class IIa bacteriocins are Listeria -active peptides with a consensus amino acid sequence of YGNGVXaaC in the N-terminal, and include pediocin PA-1 (Henderson et al, 1992) and carnobacteriocin X (Tulini et al, 2014). Class IIb bacteriocins require two different unmodified peptides for forming a fully active poration complex, such as lactacin F (Allison et al, 1994) and ABP-118 (Flynn et al, 2002).…”

Section: Classification Of Bacteriocinsmentioning

confidence: 99%

Antibacterial activities of bacteriocins: application in foods and pharmaceuticals

et al. 2014

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Bacteriocins are a kind of ribosomal synthesized antimicrobial peptides produced by bacteria, which can kill or inhibit bacterial strains closely-related or non-related to produced bacteria, but will not harm the bacteria themselves by specific immunity proteins. Bacteriocins become one of the weapons against microorganisms due to the specific characteristics of large diversity of structure and function, natural resource, and being stable to heat. Many recent studies have purified and identified bacteriocins for application in food technology, which aims to extend food preservation time, treat pathogen disease and cancer therapy, and maintain human health. Therefore, bacteriocins may become a potential drug candidate for replacing antibiotics in order to treat multiple drugs resistance pathogens in the future. This review article summarizes different types of bacteriocins from bacteria. The latter half of this review focuses on the potential applications in food science and pharmaceutical industry.

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Section: Classification Of Bacteriocinsmentioning

confidence: 99%

Antibacterial activities of bacteriocins: application in foods and pharmaceuticals

et al. 2014

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“…P. claussenii DSM 14800 was also shown to encode pediocin PD-1, however, this strain failed to display bacteriocin production. The Carnobacterium maltaromaticum strains DSM 20722 and DSM 20730 were also both found to encode the two-component lantibiotic carnolysin, however the in vitro production of this bacteriocin was not seen in either strain 25 .…”

Section: Resultsmentioning

confidence: 99%

“…13 . Numerous bacteriocins have been attributed to this genus previously 25, 36 . While the source of antimicrobial activity from C. maltaromaticum DSM20342 is unclear, C .…”

Section: Resultsmentioning

confidence: 99%

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Bacteriocin Gene-Trait matching across the complete Lactobacillus Pan-genome

Collins

O’Connor

O’Sullivan

et al. 2017

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Lactobacilli constitute a large genus of Gram-positive lactic acid bacteria which have widespread roles ranging from gut commensals to starters in fermented foods. A combination of in silico and laboratory-based screening allowed us to determine the overall bacteriocin producing potential of representative strains of each species of the genus. The genomes of 175 lactobacilli and 38 associated species were screened for the presence of antimicrobial producing genes and combined with screening for antimicrobial activity against a range of indicators. There also appears to be a link between the strains’ environment and bacteriocin production, with those from the animal and human microbiota encoding over twice as many bacteriocins as those from other sources. Five novel bacteriocins were identified belonging to differing bacteriocin classes, including two-peptide bacteriocins (muricidin and acidocin X) and circular bacteriocins (paracyclicin). In addition, there was a clear clustering of helveticin type bacteriolysins in the Lactobacillus acidophilus group of species. This combined in silico and in vitro approach to screening has demonstrated the true diversity and complexity of bacteriocins across the genus. It also highlights their biological importance in terms of communication and competition between closely related strains in diverse complex microbial environments.

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“…). It is likely that the previously observed activity of CbnX toward C. maltaromaticum A9b− was due to the presence of undetected CbnY or minute amounts of another bacteriocin from the producer organism .…”

Section: Discussionmentioning

confidence: 99%

Identification and three‐dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria

et al. 2017

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In this study, we report that CbnX (33 residues) and CbnY (29 residues) comprise a class IIb (two-component) bacteriocin in Carnobacteria. Individually, CbnX and CbnY are inactive, but together act synergistically to exert a narrow spectrum of activity. The structures of CbnX and CbnY in structure-inducing conditions were determined and strongly resemble other class IIb bacteriocins (i.e., LcnG, PlnEF, PlnJK). CbnX has an extended, amphipathic α-helix and a flexible C terminus. CbnY has two α-helices (one hydrophobic, one amphipathic) connected by a short loop and a cationic C terminus. CbnX and CbnY do not appear to interact directly and likely require a membrane-bound receptor to facilitate formation of the bacteriocin complex. This is the first class IIb bacteriocin reported for Carnobacteria.

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Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2

Cited by 35 publications

References 32 publications

Antibacterial activities of bacteriocins: application in foods and pharmaceuticals

Antibacterial activities of bacteriocins: application in foods and pharmaceuticals

Bacteriocin Gene-Trait matching across the complete Lactobacillus Pan-genome

Identification and three‐dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria

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