Functions and emerging applications of bacteriocins

Chikindas, Michael L.; Weeks, Richard; Drider, Djamel; Chistyakov, V. A.; Dicks, Leon M. T.

doi:10.1016/j.copbio.2017.07.011

Cited by 396 publications

(249 citation statements)

References 45 publications

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“…Since ancient times, LAB-fermentation process has been used as a preservation technique due to the production of antimicrobial metabolites such as organic acids, diacetyl, H 2 O 2 , and bacteriocins (Leroy & De Vuyst, 2004). In a general approach, Chikindas, Weeks, Drider, Chistyakov, & Dicks (2018) describe bacteriocins as multifunctional peptides produced in the ribosome, which exhibit antimicrobial activity at a given concentration. Klaenhammer (1988) stated that 99% of all bacteria have the genetic possibility to produce bacteriocins; based on the fact that bacteriocin genes are distributed in a large number of bacteria even when in many cases, the genes are not active (Walsh et al, 2015).…”

Section: Lab: a Cell Factorymentioning

confidence: 99%

Production of Bioactive Peptides from Lactic Acid Bacteria: A Sustainable Approach for Healthier Foods

Venegas-Ortega

Flores‐Gallegos

Martínez-Hernández

et al. 2019

Comp Rev Food Sci Food Safe

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Traditional fermented foods where lactic acid bacteria (LAB) are present have been associated with beneficial effects on human health, and some of those benefits are related to protein‐derived products. Peptides produced by LAB have attracted the interest of food industries because of their diverse applications. These peptides include ribosomally produced (bacteriocins) and protein hydrolysates by‐products (bioactive peptides), which can participate as natural preservatives and nutraceuticals, respectively. It is essential to understand the biochemical pathways and the effect of growth conditions for the production of bioactive peptides and bacteriocins by LAB, in order to suggest strategies for optimization. LAB is an important food‐grade expression system that can be used in the simultaneous production of peptide‐based products for the food, animal, cosmetic, and pharmaceutical industries. This review describes the multifunctional proteinaceous compounds generated by LAB metabolism and discusses a strategy to use a single‐step production process, using an alternative protein‐based media. This strategy will provide economic advantages in fermentation processes and will also provide an environmental alternative to industrial waste valorization. New technologies that can be used to improve production and bioactivity of LAB‐derived peptides are also analyzed.

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Section: Lab: a Cell Factorymentioning

confidence: 99%

Production of Bioactive Peptides from Lactic Acid Bacteria: A Sustainable Approach for Healthier Foods

Venegas-Ortega

Flores‐Gallegos

Martínez-Hernández

et al. 2019

Comp Rev Food Sci Food Safe

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“…In addition, we demonstrated the involvement of small secreted proteins characterized by double-glycine (GG) secretion motifs in biofilm development (Parnasa et al, 2016). GG-motifs are N-terminal secretion signals that allow secretion of multiple families of natural products including microcins (van Belkum et al, 1997;Riley and Wertz, 2002;Dirix et al, 2004;Arnison et al, 2013;Yang et al, 2014;Chikindas et al, 2018). Data mining indicated that genes encoding small proteins with GG-motifs and their putative related transporters are prevalent in cyanobacteria (Haft et al, 2010;Wang et al, 2011;Micallef et al, 2015); however, the roles of these cyanobacterial components are largely unknown.…”

Section: Introductionmentioning

confidence: 99%

A microcin processing peptidase‐like protein of the cyanobacterium Synechococcus elongatus is essential for secretion of biofilm‐promoting proteins

Parnasa

Sendersky

Simkovsky

et al. 2019

Environ Microbiol Rep

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Summary Small secreted compounds, e.g. microcins, are characterized by a double‐glycine (GG) secretion motif that is cleaved off upon maturation. Genomic analysis suggests that small proteins that possess a GG motif are widespread in cyanobacteria; however, the roles of these proteins are largely unknown. Using a biofilm‐proficient mutant of the cyanobacterium Synechococcus elongatus PCC 7942 in which the constitutive biofilm self‐suppression mechanism is inactivated, we previously demonstrated that four small proteins, Enable biofilm formation with a GG motif (EbfG1‐4), each with a GG motif, enable biofilm formation. Furthermore, a peptidase belonging to the C39 family, Peptidase transporter enabling Biofilm (PteB), is required for secretion of these proteins. Here, we show that the microcin processing peptidase‐like protein encoded by gene Synpcc7942_1127 is also required for biofilm development – inactivation of this gene in the biofilm‐proficient mutant abrogates biofilm development. Additionally, this peptidase‐like protein (denoted EbfE – enables biofilm formation peptidase) is required for secretion of the EbfG biofilm‐promoting small proteins. Given their protein‐domain characteristics, we suggest that PteB and EbfE take part in a maturation‐secretion system, with PteB being located to the cell membrane while EbfE is directed to the periplasmic space via its secretion signal.

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“…Lactic acid bacteria (LAB) produce a diverse array of bacteriocins. Bacteriocins are ribosomally synthesized peptides with bactericidal activity and are frequently most active against species that are highly related to the producer strains (Chikindas, Weeks, Drider, Chistyakov, & Dicks, ). Bacteriocins, and LAB bacteriocins in particular, have received considerable interest for their potential use in food preservation and pathogen inhibition (Cotter, Hill, & Ross, ).…”

Section: Introductionmentioning

confidence: 99%

Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein

2019

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Lactic acid bacteria produce a variety of antimicrobial peptides known as bacteriocins. Most bacteriocins are understood to kill sensitive bacteria through receptor‐mediated disruptions. Here, we report on the identification of the Lactobacillus plantarum plantaricin EF (PlnEF) receptor. Spontaneous PlnEF‐resistant mutants of the PlnEF‐indicator strain L. plantarum NCIMB 700965 (LP965) were isolated and confirmed to maintain cellular ATP levels in the presence of PlnEF. Genome comparisons resulted in the identification of a single mutated gene annotated as the membrane‐bound, magnesium/cobalt efflux protein CorC. All isolates contained a valine (V) at position 334 instead of a glycine (G) in a cysteine‐β‐synthase domain at the C‐terminal region of CorC. In silico template‐based modeling of this domain indicated that the mutation resides in a loop between two β‐strands. The relationship between PlnEF, CorC, and metal homeostasis was supported by the finding that PlnEF‐resistance was lost when PlnEF was applied together with high concentrations of Mg2+, Co2+, Zn2+, or Cu2+. Lastly, PlnEF sensitivity was increased upon heterologous expression of LP965 corC but not the G334V CorC mutant in the PlnEF‐resistant strain Lactobacillus casei BL23. These results show that PlnEF kills sensitive bacteria by targeting CorC.

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Functions and emerging applications of bacteriocins

Cited by 396 publications

References 45 publications

Production of Bioactive Peptides from Lactic Acid Bacteria: A Sustainable Approach for Healthier Foods

Production of Bioactive Peptides from Lactic Acid Bacteria: A Sustainable Approach for Healthier Foods

A microcin processing peptidase‐like protein of the cyanobacterium Synechococcus elongatus is essential for secretion of biofilm‐promoting proteins

Sensitivity to the two peptide bacteriocin plantaricin EF is dependent on CorC, a membrane‐bound, magnesium/cobalt efflux protein

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