Bacteriocins of gram-positive bacteria
Open accessAbstract
In recent years, a group of antibacterial proteins produced by gram-positive bacteria have attracted great interest in their potential use as food preservatives and as antibacterial agents to combat certain infections due to gram-positive pathogenic bacteria. They are ribosomally synthesized peptides of 30 to less than 60 amino acids, with a narrow to wide antibacterial spectrum against gram-positive bacteria; the antibacterial property is heat stable, and a producer strain displays a degree of specific self-protection against its own antibacterial peptide. In many respects, these proteins are quite different from the colicins and other bacteriocins produced by gram-negative bacteria, yet customarily they also are grouped as bacteriocins. Although a large number of these bacteriocins (or bacteriocin-like inhibitory substances) have been reported, only a few have been studied in detail for their mode of action, amino acid sequence, genetic characteristics, and biosynthesis mechanisms. Nevertheless, in general, they appear to be translated as inactive prepeptides containing an N-terminal leader sequence and a C-terminal propeptide component. During posttranslational modifications, the leader peptide is removed. In addition, depending on the particular type, some amino acids in the propeptide components may undergo either dehydration and thioether ring formation to produce lanthionine and beta-methyl lanthionine (as in lantibiotics) or thio ester ring formation to form cystine (as in thiolbiotics). Some of these steps, as well as the translocation of the molecules through the cytoplasmic membrane and producer self-protection against the homologous bacteriocin, are mediated through specific proteins (enzymes). Limited genetic studies have shown that the structural gene for such a bacteriocin and the genes encoding proteins associated with immunity, translocation, and processing are present in a cluster in either a plasmid, the chromosome, or a transposon. Following posttranslational modification and depending on the pH, the molecules may either be released into the environment or remain bound to the cell wall. The antibacterial action against a sensitive cell of a gram-positive strain is produced principally by destabilization of membrane functions. Under certain conditions, gram-negative bacterial cells can also be sensitive to some of these molecules. By application of site-specific mutagenesis, bacteriocin variants which may differ in their antimicrobial spectrum and physicochemical characteristics can be produced. Research activity in this field has grown remarkably but sometimes with an undisciplined regard for conformity in the definition, naming, and categorization of these molecules and their genetic effectors. Some suggestions for improved standardization of nomenclature are offered.
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Many lactic acid and propionic acid bacteria produce antibacterial substances such as peroxides and bacteriocins.
“Many lactic acid and propionic acid bacteria produce substances with antibacterial activity such as peroxides and bacteriocins (Jack et al., 1995;Meile et al., 1999).”
From Control of Escherichia coli O157:H7 in corn silage with or without various inoculants: Efficacy and mode of action (2010) · cites this paper as Jack et al., 1995
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Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391 · see citing works
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Extension of Tosèla cheese shelf-life using non-starter lactic acid bacteria
Settanni, L., Franciosi, E., Cavazza, A., Cocconcelli, P. S., & Poznanski, E. (2011) · Food Microbiology · doi:10.1016/j.fm.2010.12.003 · Cited by 33 · see citing works
Zhang, C., Zhang, Y., Ma, K., Wang, G., Tang, M., Wang, R., Xia, Z., Xu, Z., Sun, M., Bao, X., et al. (2022) · Annals of Translational Medicine · doi:10.21037/atm-22-458 · Cited by 25 · see citing works
- Authors
- Jack, R. W., Tagg, J. R., & Ray, B.
- Affiliations
- The University of Melbourne (AU)
- ORCID
- Tagg, J R
- Venue
- Microbiological Reviews
- Publisher
- American Society for Microbiology
- Published
- 1995-06
- Volume
- 59
- Issue
- 2
- Pages
- 171-200
- ISSN
- 0146-0749 (ISSN-L)
- PMC
- PMC239359
- OpenAlex
- W2159401663
- Cited by
- 2,711
- References
- 299
- Citations by year
- 2026: 13 · 2025: 23 · 2024: 32 · 2023: 44 · 2022: 39 · 2021: 49 · 2020: 67 · 2019: 57 · 2018: 60 · 2017: 69 · 2016: 72 · 2015: 109 · 2014: 118 · 2013: 102 · 2012: 97
- FWCI
- 62.59
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Microbiological Reviews (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- bacteriocins, Gram-positive bacteria, bacteriocin-like inhibitory substances, lantibiotics, ribosomally synthesized peptides, post-translational modification, leader peptide, propeptide, self-protection, immunity genes, biosynthesis genes, membrane perturbation, food preservatives, antibacterial agents, terminology standardization, colicins
- MeSH terms
- Amino Acid Sequence, Bacteriocins, Gram-Positive Bacteria, Models, Genetic, Molecular Sequence Data
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