Bacteriocins of lactic acid bacteria: Extending the family
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Lactic acid bacteria (LAB) constitute a heterogeneous group of microorganisms that produce lactic acid as the major product during the fermentation process. LAB are Gram-positive bacteria with great biotechnological potential in the food industry. They can produce bacteriocins, which are proteinaceous antimicrobial molecules with a diverse genetic origin, posttranslationally modified or not, that can help the producer organism to outcompete other bacterial species. In this review, we focus on the various types of bacteriocins that can be found in LAB and the organization and regulation of the gene clusters responsible for their production and biosynthesis, and consider the food applications of the prototype bacteriocins from LAB. Furthermore, we propose a revised classification of bacteriocins that can accommodate the increasing number of classes reported over the last years.
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The anti-infective effect of bacteriocins produced by LAB represents a promising alternative to the use of antibiotics, especially in special cases where other methods are not allowed (e.g., pregnancy).
“Therefore, the anti-infective effect of bacteriocins produced by LAB represents a promising alternative to the use of antibiotics, especially in special cases where other methods are not allowed (e.g., pregnancy) [246].”
From Lactic Acid Bacteria in Raw-Milk Cheeses: From Starter Cultures to Probiotic Functions (2022) · cites this paper as [246]
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1 retracted
Ni, J., Teng, K., Liu, G., et al. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.01278-10 · Cited by 13 · see citing works
RetractedBacteriocins: Developing innate immunity for food
Cotter, P. D., Hill, C., & Ross, R. P. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1273 · Cited by 2,380 · see citing works
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G. W., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2012) · Natural Product Reports · doi:10.1039/c2np20085f · Cited by 2,065 · see citing works
Self-citationGenetics of bacteriocins produced by lactic acid bacteria
Klaenhammer, T. R. (1993) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1993.tb00012.x · Cited by 1,835 · see citing works
Bacteriocins—A viable alternative to antibiotics?
Cotter, P. D., Ross, R. P., & Hill, C. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro2937 · Cited by 1,793 · see citing works
Discovery of microbial natural products by activation of silent biosynthetic gene clusters
Rutledge, P. J., & Challis, G. L. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3496 · Cited by 997 · see citing works
Minimum Information about a Biosynthetic Gene cluster
Medema, M. H., Kottmann, R., Yilmaz, P., Cummings, M., Biggins, J. B., Blin, K., de Bruijn, I., Chooi, Y., Claesen, J., Coates, R. C., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1890 · Cited by 876 · see citing works
Self-citationCorr, S. C., Li, Y., Riedel, C. U., O'Toole, P. W., Hill, C., & Gahan, C. G. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700440104 · Cited by 853 · see citing works
Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic
Breukink, E. J., Wiedemann, I., van Kraaij, C., Kuipers, O. P., Sahl, H., & KRUIJFF, B. D. (1999) · Science · doi:10.1126/science.286.5448.2361 · Cited by 815 · see citing works
Self-citationantiSMASH 2.0—a versatile platform for genome mining of secondary metabolite producers
Blin, K., Medema, M. H., Kazempour, D., Fischbach, M. A., Rainer Breitling, A., Eriko Takano, A., & Weber, T. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt449 · Cited by 798 · see citing works
The lactic acid bacteria: A literature survey
Carr, F. J., Chill, D., & Maida, N. (2002) · Critical Reviews in Microbiology · doi:10.1080/1040-840291046759 · Cited by 724 · see citing works
Bacteriocin Production: a Probiotic Trait?
Dobson, A., Cotter, P. D., Ross, R. P., & Hill, C. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.05576-11 · Cited by 690 · see citing works
Functional meat starter cultures for improved sausage fermentation
Leroy, F., Verluyten, J., & Vuyst, L. D. (2005) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2005.06.027 · Cited by 614 · see citing works
Rea, M. C., Sit, C. S., Clayton, E., O'Connor, P. M., Whittal, R. M., Zheng, J., Vederas, J. C., Ross, R. P., & Hill, C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913554107 · Cited by 530 · see citing works
An Alternative Bactericidal Mechanism of Action for Lantibiotic Peptides That Target Lipid II
Hasper, H. E., Kramer, N. E., Smith, L., Hillman, J. D., Zachariah, C., Kuipers, O. P., KRUIJFF, B. D., & Breukink, E. J. (2006) · Science · doi:10.1126/science.1129818 · Cited by 502 · see citing works
Self-citationvan Heel, A. J., de Jong, A., Montalbán‐López, M., Kok, J., & Kuipers, O. P. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt391 · Cited by 477 · see citing works
Self-citationKommineni, S., Bretl, D. J., Lam, V., Chakraborty, R., Hayward, M., Simpson, P., Cao, Y., Bousounis, P., Kristich, C. J., & Salzman, N. H. (2015) · Nature · doi:10.1038/nature15524 · Cited by 458 · see citing works
Diversity of enterococcal bacteriocins and their grouping in a new classification scheme
Franz, C. M. A. P., van Belkum, M. J., Holzapfel, W. H., Abriouel, H., & Gálvez, A. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00064.x · Cited by 443 · see citing works
Gavrish, E., Sit, C. S., Cao, S., Kandror, O., Spoering, A. L., Peoples, A. J., Ling, L. L., Fetterman, A., Hughes, D. E., Bissell, A., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.01.014 · Cited by 426 · see citing works
Holo, H., Nilssen, O., & Nes, I. F. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.12.3879-3887.1991 · Cited by 402 · see citing works
Lasso Peptides: An Intriguing Class of Bacterial Natural Products
Hegemann, J. D., Zimmermann, M., Xie, X., & Marahiel, M. A. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00156 · Cited by 395 · see citing works
Common mechanisms of target cell recognition and immunity for class II bacteriocins
Diep, D. B., Skaugen, M., Salehian, Z., Holo, H., & Nes, I. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608775104 · Cited by 374 · see citing works
Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin
Lubelski, J., Rink, R., Khusainov, R., Moll, G. N., & Kuipers, O. P. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7171-2 · Cited by 349 · see citing works
Self-citationA novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
Nissen-Meyer, J., Holo, H., Håvarstein, L. S., Sletten, K., & Nes, I. F. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.17.5686-5692.1992 · Cited by 346 · see citing works
Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB
Ortega, M. A., Hao, Y., Zhang, Q., Walker, M. C., van der Donk, W. A., & Nair, S. K. (2014) · Nature · doi:10.1038/nature13888 · Cited by 318 · see citing works
Discovery, Biosynthesis, and Engineering of Lantipeptides
Knerr, P. J., & van der Donk, W. A. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060110-113521 · Cited by 315 · see citing works
Enterolysin A, a Cell Wall-Degrading Bacteriocin from Enterococcus faecalis LMG 2333
Nilsen, T., Nes, I. F., & Holo, H. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.5.2975-2984.2003 · Cited by 308 · see citing works
Pediocin PA-1, a Wide-Spectrum Bacteriocin from Lactic Acid Bacteria
Rodríguez, J. M., Martínez, M., & Kok, J. (2002) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408690290825475 · Cited by 301 · see citing works
Cintas, L. M., Casaus, P., Holo, H., Hernández, P. E., Nes, I. F., & Håvarstein, L. S. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.8.1988-1994.1998 · Cited by 301 · see citing works
Lasso peptides: structure, function, biosynthesis, and engineering
Maksimov, M. O., Pan, S. J., & Link, A. J. (2012) · Natural Product Reports · doi:10.1039/c2np20070h · Cited by 277 · see citing works
Nissen-Meyer, J., Rogne, P., Oppegård, C., Haugen, H., & Kristiansen, P. E. (2009) · Current Pharmaceutical Biotechnology · doi:10.2174/138920109787048661 · Cited by 256 · see citing works
Amylocyclicin, a Novel Circular Bacteriocin Produced by Bacillus amyloliquefaciens FZB42
Scholz, R., Vater, J., Budiharjo, A., et al. (2014) · Journal of Bacteriology · doi:10.1128/jb.01474-14 · Cited by 241 · see citing works
Genetic Locus for Streptolysin S Production by Group A Streptococcus
Nizet, V., Beall, B., Bast, D. J., Datta, V., Kilburn, L., Low, D. E., & de Azavedo, J. C. S. (2000) · Infection and Immunity · doi:10.1128/iai.68.7.4245-4254.2000 · Cited by 216 · see citing works
Discovery of a widely distributed toxin biosynthetic gene cluster
Lee, S. W., Mitchell, D. A., Markley, A. L., Hensler, M. E., Gonzalez, D. J., Wohlrab, A. M., Dorrestein, P. C., Nizet, V., & Dixon, J. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801338105 · Cited by 206 · see citing works
Structure and Mode-of-Action of the Two-Peptide (Class-IIb) Bacteriocins
Nissen-Meyer, J., Oppegård, C., Rogne, P., Haugen, H. S., & Kristiansen, P. E. (2009) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-009-9021-z · Cited by 199 · see citing works
Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates
Melby, J. O., Nard, N. J., & Mitchell, D. A. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.02.027 · Cited by 180 · see citing works
Genetic features of circular bacteriocins produced by Gram-positive bacteria
Maqueda, M., Sánchez‐Hidalgo, M., Fernández, M., Montalbán‐López, M., Valdivia, E., & Martínez‐Bueno, M. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00087.x · Cited by 172 · see citing works
Self-citationThe Two-Peptide Class II Bacteriocins: Structure, Production, and Mode of Action
Oppegård, C., Rogne, P., Emanuelsen, L., Kristiansen, P. E., Fimland, G., & Nissen-Meyer, J. (2007) · Microbial Physiology · doi:10.1159/000104750 · Cited by 170 · see citing works
Cysteine S -glycosylation, a new post-translational modification found in glycopeptide bacteriocins
Stepper, J., Shastri, S., Loo, T. S., Preston, J. C., Novák, P., Man, P., Moore, C. H., Havlı́ček, V., Patchett, M. L., & Norris, G. E. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.023 · Cited by 167 · see citing works
Anti-infective properties of bacteriocins: an update
Hammami, R., Fernandez, B., Lacroix, C., & Fliss, I. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1202-3 · Cited by 165 · see citing works
Joerger, M. C., & Klaenhammer, T. R. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.11.6339-6347.1990 · Cited by 160 · see citing works
Circular Bacteriocins: Biosynthesis and Mode of Action
Gabrielsen, C., Brede, D. A., Nes, I. F., et al. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.02284-14 · Cited by 160 · see citing works
Stoddard, G. W., Petzel, J. P., van Belkum, M. J., et al. (1992) · Applied and Environmental Microbiology · doi:10.1128/aem.58.6.1952-1961.1992 · Cited by 151 · see citing works
Marciset, O., Jeronimus‐Stratingh, M., Mollet, B., & Poolman, B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14277 · Cited by 149 · see citing works
Yoneyama, F., Imura, Y., Ohno, K., Zendo, T., Nakayama, J., Matsuzaki, K., & Sonomoto, K. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00209-09 · Cited by 145 · see citing works
Class IIa bacteriocins from lactic acid bacteria: Antibacterial activity and food preservation
Ennahar, S., Sonomoto, K., & Ishizaki, A. (1999) · Journal of Bioscience and Bioengineering · doi:10.1016/s1389-1723(99)80142-x · Cited by 138 · see citing works
Kjos, M., Borrero, J., Opsata, M., Birri, D. J., Holo, H., Cintas, L. M., Snipen, L. G., Hernández, P. E., Nes, I. F., & Diep, D. B. (2011) · Microbiology · doi:10.1099/mic.0.052571-0 · Cited by 133 · see citing works
YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations
Dunbar, K. L., Melby, J. O., & Mitchell, D. A. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.944 · Cited by 131 · see citing works
Kawulka, K. E., Sprules, T. J., McKay, R. T., et al. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029654t · Cited by 130 · see citing works
In vitro activity of the nisin dehydratase NisB
Garg, N., Salazar-Ocampo, L. M. A., & van der Donk, W. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222488110 · Cited by 126 · see citing works
Class IIa Bacteriocins: Diversity and New Developments
Cui, Y., Zhang, C., Wang, Y., Shi, J., Zhang, L., Ding, Z., Qu, X., & Cui, H. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131216668 · Cited by 125 · see citing works
Heddle, J. G., Blance, S. J., Zamble, D. B., et al. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4562 · Cited by 120 · see citing works
Alegría, Á., Delgado, S., Roces, C., López, B., & Mayo, B. (2010) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2010.07.029 · Cited by 119 · see citing works
Dissecting the Maturation Steps of the Lasso Peptide Microcin J25 in vitro
Yan, K.-P., Li, Y., Zirah, S., et al. (2012) · ChemBioChem · doi:10.1002/cbic.201200016 · Cited by 117 · see citing works
Hillman, J. D., Brooks, T. A., Michalek, S. M., Harmon, C. C., Snoep, J. L., & van der Weijden, C. C. (2000) · Infection and Immunity · doi:10.1128/iai.68.2.543-549.2000 · Cited by 112 · see citing works
Ukuku, D. O., & Fett, W. F. (2004) · Journal of Food Protection · doi:10.4315/0362-028x-67.10.2143 · Cited by 104 · see citing works
Flühe, L., Burghaus, O., Monfort, B., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310542g · Cited by 102 · see citing works
Martin‐Visscher, L. A., Gong, X., Duszyk, M., & Vederas, J. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.036459 · Cited by 99 · see citing works
Kjos, M., Oppegård, C., Diep, D. B., et al. (2014) · Molecular Microbiology · doi:10.1111/mmi.12632 · Cited by 97 · see citing works
AS-48 bacteriocin: close to perfection
Sánchez‐Hidalgo, M., Montalbán‐López, M., Cebrián, R., Valdivia, E., Martínez‐Bueno, M., & Maqueda, M. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0724-4 · Cited by 93 · see citing works
Self-citationAre Bacteriocins Underexploited? NOVEL Applications for OLD Antimicrobials
Montalbán‐López, M., Sánchez‐Hidalgo, M., Valdivia, E., et al. (2011) · Current Pharmaceutical Biotechnology · doi:10.2174/138920111796117364 · Cited by 93 · see citing works
Self-citationStructural basis for hijacking siderophore receptors by antimicrobial lasso peptides
Mathavan, I., Zirah, S., Mehmood, S., Choudhury, H. G., Goulard, C., Li, Y., Robinson, C. V., Rebuffat, S., & Beis, K. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1499 · Cited by 93 · see citing works
An Engineered Lantibiotic Synthetase That Does Not Require a Leader Peptide on Its Substrate
Oman, T. J., Knerr, P. J., Bindman, N. A., Velásquez, J. E., & van der Donk, W. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3017297 · Cited by 92 · see citing works
Gabrielsen, C., Brede, D. A., Hernández, P. E., Nes, I. F., & Diep, D. B. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00314-12 · Cited by 92 · see citing works
Hu, C.-B., Malaphan, W., Zendo, T., Nakayama, J., & Sonomoto, K. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.02264-09 · Cited by 92 · see citing works
Craik, D. J., & Malik, U. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.05.033 · Cited by 92 · see citing works
Bogaardt, C., van Tonder, A. J., & Brueggemann, A. B. (2015) · BMC Genomics · doi:10.1186/s12864-015-1729-4 · Cited by 88 · see citing works
Rogne, P., Fimland, G., Nissen-Meyer, J., & Kristiansen, P. E. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.12.002 · Cited by 88 · see citing works
Martı́nez, B., Fernández, M., Suárez, J. E., et al. (1999) · Microbiology · doi:10.1099/00221287-145-11-3155 · Cited by 87 · see citing works
The Antibacterial Threaded-lasso Peptide Capistruin Inhibits Bacterial RNA Polymerase
Kuznedelov, K. D., Semenova, E., Knappe, T. A., et al. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.060 · Cited by 87 · see citing works
Structure and Biosynthesis of Carnolysin, a Homologue of Enterococcal Cytolysin with d -Amino Acids
Lohans, C. T., Li, J. L., & Vederas, J. C. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5070813 · Cited by 86 · see citing works
Lactococcin 972, a bacteriocin that inhibits septum formation in lactococci
Martı́nez, B., Rodrı́guez, A., & Suárez, J. E. (2000) · Microbiology · doi:10.1099/00221287-146-4-949 · Cited by 84 · see citing works
Development of a bioactive packaging cellophane using NisaplinR as biopreservative agent
Guerra, N. P., Macı́as, C. L., Agrasar, A. T., & Pastrana, L. M. (2005) · Letters in Applied Microbiology · doi:10.1111/j.1472-765x.2004.01649.x · Cited by 84 · see citing works
Lipid II-Based Antimicrobial Activity of the Lantibiotic Plantaricin C
Wiedemann, I., Böttiger, T., Bonelli, R. R., Schneider, T., Sahl, H., & Martı́nez, B. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.4.2809-2814.2006 · Cited by 84 · see citing works
Burgos, M. J. G., López, R. L., Abriouel, H., Valdivia, E., Benomar, N., Maqueda, M., Martínez‐Cañamero, M., & Gálvez, A. (2007) · Journal of Food Protection · doi:10.4315/0362-028x-70.2.405 · Cited by 79 · see citing works
Himeno, K., Rosengren, K. J., Inoue, T., Pérez, R., Colgrave, M. L., Lee, H. S., Chan, L. Y., Henriques, S. T., Fujita, K., Ishibashi, N., et al. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00196 · Cited by 77 · see citing works
Piscotta, F. J., Tharp, J. M., Liu, W. R., et al. (2014) · Chemical Communications · doi:10.1039/c4cc07778d · Cited by 76 · see citing works
Enterocin F4-9, a Novel O -Linked Glycosylated Bacteriocin
Maky, M. A., Ishibashi, N., Zendo, T., Pérez, R., R, J. R. D. P. M., Karmi, M., & Sonomoto, K. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.00940-15 · Cited by 75 · see citing works
Genome Mining for Radical SAM Protein Determinants Reveals Multiple Sactibiotic-Like Gene Clusters
Murphy, K., O’Sullivan, Ó., Rea, M. C., Cotter, P. D., Ross, R. P., & Hill, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020852 · Cited by 74 · see citing works
de Kwaadsteniet, M., Fraser, T., van Reenen, C. A., et al. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.00436-06 · Cited by 74 · see citing works
Structural, Dynamic, and Chemical Characterization of a Novel S-Glycosylated Bacteriocin
Venugopal, H., Edwards, P. J. B., Schwalbe, M., Claridge, J. K., Libich, D. S., Stepper, J., Loo, T. S., Patchett, M. L., Norris, G. E., & Pascal, S. M. (2011) · Biochemistry · doi:10.1021/bi200217u · Cited by 72 · see citing works
Simmonds, R. S., Pearson, L., Kennedy, R. C., & Tagg, J. R. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.12.4536-4541.1996 · Cited by 72 · see citing works
Saß, P., Jansen, A., Szekat, C., et al. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-186 · Cited by 70 · see citing works
Ring A of Nukacin ISK-1: A Lipid II-Binding Motif for Type-A(II) Lantibiotic
Islam, M. R., Nishie, M., Nagao, J.-I., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja300007h · Cited by 70 · see citing works
The circular bacteriocin, carnocyclin A, forms anion-selective channels in lipid bilayers
Gong, X., Martin‐Visscher, L. A., Nahirney, D., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.05.008 · Cited by 69 · see citing works
Uzelac, G., Kojić, M., Lozo, J., Aleksandrzak‐Piekarczyk, T., Gabrielsen, C., Kristensen, T., Nes, I. F., Diep, D. B., & Topisirović, L. (2013) · Journal of Bacteriology · doi:10.1128/jb.00859-13 · Cited by 69 · see citing works
Noll, K. S., Sinko, P. J., & Chikindas, M. L. (2010) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-010-9061-4 · Cited by 68 · see citing works
Diep, D. B., Myhre, R., Johnsborg, O., Aakra, Å., & Nes, I. F. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03310.x · Cited by 67 · see citing works
The Sactibiotic Subclass of Bacteriocins: An Update
Mathur, H., Rea, M. C., Cotter, P. D., Hill, C., & Ross, R. P. (2015) · Current Protein and Peptide Science · doi:10.2174/1389203716666150515124831 · Cited by 66 · see citing works
The genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles
Cox, C. L., Doroghazi, J. R., & Mitchell, D. A. (2015) · BMC Genomics · doi:10.1186/s12864-015-2008-0 · Cited by 65 · see citing works
Solution Structure of Acidocin B, a Circular Bacteriocin Produced by Lactobacillus acidophilus M46
Acedo, J. Z., van Belkum, M. J., Lohans, C. T., et al. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.04265-14 · Cited by 65 · see citing works
Yoneyama, F., Imura, Y., Ichimasa, S., Fujita, K., Zendo, T., Nakayama, J., Matsuzaki, K., & Sonomoto, K. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01827-08 · Cited by 61 · see citing works
Determination of the mode of action of enterolysin A, produced by Enterococcus faecalis B9510
Khan, H., Flint, S., & Yu, P. L. (2013) · Journal of Applied Microbiology · doi:10.1111/jam.12240 · Cited by 59 · see citing works
Lacticin 3147 - Biosynthesis, Molecular Analysis, Immunity, Bioengineering and Applications
Suda, S., Cotter, P. D., Hill, C., & Ross, R. P. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312800785021 · Cited by 59 · see citing works
Discovering the Bacterial Circular Proteins: Bacteriocins, Cyanobactins, and Pilins
Montalbán‐López, M., Sánchez‐Hidalgo, M., Cebrián, R., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.354688 · Cited by 58 · see citing works
Self-citationViedma, P. M., Sobrino‐López, A., Benomar, N., Abriouel, H., López, R. L., Valdivia, E., Martín‐Belloso, O., & Gálvez, A. (2008) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2008.08.014 · Cited by 58 · see citing works
Beukes, M., Bierbaum, G., Sahl, H., & Hastings, J. W. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.1.23-28.2000 · Cited by 58 · see citing works
Identification of an N-Terminal Formylated, Two-Peptide Bacteriocin from Enterococcus faecalis 710C
Liu, X., Vederas, J. C., Whittal, R. M., Zheng, J., Stiles, M. E., Carlson, D., Franz, C. M. A. P., McMullen, L. M., & van Belkum, M. J. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf104751v · Cited by 55 · see citing works
Cebrián, R., Martínez‐Bueno, M., Valdivia, E., et al. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.03.006 · Cited by 48 · see citing works
New type non-lantibiotic bacteriocins: circular and leaderless bacteriocins
Masuda, Y., Zendo, T., & Sonomoto, K. (2012) · Beneficial Microbes · doi:10.3920/bm2011.0047 · Cited by 46 · see citing works
Michael-Type Cyclizations in Lantibiotic Biosynthesis Are Reversible
Yang, X., & van der Donk, W. A. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00007 · Cited by 45 · see citing works
Cruz, V. L., Ramos, J., Melo, M. N., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.05.036 · Cited by 43 · see citing works
Lai, A. C.-K., Tran, S., & Simmonds, R. S. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11382.x · Cited by 43 · see citing works
Lohans, C. T., Towle, K. M., Miskolzie, M., McKay, R. T., van Belkum, M. J., McMullen, L. M., & Vederas, J. C. (2013) · Biochemistry · doi:10.1021/bi400359z · Cited by 41 · see citing works
Substrate Specificity of the Lanthipeptide Peptidase ElxP and the Oxidoreductase ElxO
Ortega, M. A., Velásquez, J. E., Garg, N., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb5002526 · Cited by 41 · see citing works
Mode of action of dysgalacticin: a large heat-labile bacteriocin
Swe, P. M., Cook, G. M., Tagg, J. R., & Jack, R. W. (2009) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkn552 · Cited by 38 · see citing works
Wang, G., Feng, G., Snyder, A. B., et al. (2014) · FEMS Microbiology Letters · doi:10.1111/1574-6968.12486 · Cited by 38 · see citing works
Caseicin, a bacteriocin fromLactobacillus casei
Müller, E., & Radler, F. (1993) · Folia Microbiologica · doi:10.1007/bf02814392 · Cited by 37 · see citing works
Increasing the success rate of lantibiotic drug discovery by Synthetic Biology
Montalbán‐López, M., Zhou, L., Buivydas, A., et al. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.693476 · Cited by 34 · see citing works
Self-citationMu, F., Masuda, Y., Zendo, T., et al. (2013) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2013.06.023 · Cited by 33 · see citing works
Oppegård, C., Emanuelsen, L., Thorbek, L., Fimland, G., & Nissen-Meyer, J. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.02600-09 · Cited by 30 · see citing works
Lethal Hydroxyl Radical Accumulation by a Lactococcal Bacteriocin, Lacticin Q
Li, M., Yoneyama, F., Nayu, T., Zendo, T., Nakayama, J., & Sonomoto, K. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00638-13 · Cited by 29 · see citing works
Iwatani, S., Yoneyama, F., Miyashita, S., et al. (2012) · Microbiology · doi:10.1099/mic.0.062943-0 · Cited by 28 · see citing works
Ås, C. G., Brede, D. A., Salehian, Z., et al. (2013) · Journal of Bacteriology · doi:10.1128/jb.01115-13 · Cited by 27 · see citing works
Expression of bacteriocin LsbB is dependent on a transcription terminator
Uzelac, G., Miljković, M., Lozo, J., Radulović, Z., Tos̆ić, N., & Kojić, M. (2015) · Microbiological Research · doi:10.1016/j.micres.2015.06.011 · Cited by 24 · see citing works
Pulido, R. P., Toledo, J., Burgos, M. J. G., et al. (2014) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2014.11.033 · Cited by 23 · see citing works
A bacteriocin gene cluster able to enhance plasmid maintenance in Lactococcus lactis
Campelo, A. B., Roces, C., Mohedano, M. L., López, P., Rodrı́guez, A., & Martı́nez, B. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-77 · Cited by 23 · see citing works
Haugen, H. S., Kristiansen, P. E., Fimland, G., & Nissen-Meyer, J. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01068-08 · Cited by 22 · see citing works
Sit, C. S., Lohans, C. T., van Belkum, M. J., et al. (2011) · ChemBioChem · doi:10.1002/cbic.201100634 · Cited by 20 · see citing works
Tyrosine 9 is the key amino acid in microcin J25 superoxide overproduction
Chalón, M. C., Bellomio, A., Solbiati, J. O., et al. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01770.x · Cited by 18 · see citing works
Structure and properties of the metastable bacteriocin Lcn972 from Lactococcus lactis
Turner, D. L., Lamosa, P., Rodrı́guez, A., et al. (2012) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2012.09.076 · Cited by 18 · see citing works
Analysis of the Promoters Involved in Enterocin AS-48 Expression
Cebrián, R., Rodríguez‐Ruano, S. M., Martínez‐Bueno, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090603 · Cited by 16 · see citing works
Erratum to: “Cyclotide biosynthesis” [Curr Opin Chem Biol 2013, 17/4:546–554]
Craik, D. J., & Malik, U. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.09.010 · Cited by 12 · see citing works
Structural characterisation of the natively unfolded enterocin EJ97
Neira, J. L., Contreras, L. M., Paños, O. R. D. L., et al. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzq020 · Cited by 10 · see citing works
Gargis, A. S., O’Rourke, A.-L., Sloan, G. L., & Simmonds, R. S. (2009) · Journal of Molecular Evolution · doi:10.1007/s00239-009-9221-x · Cited by 9 · see citing works
Varki, A. P., Cummings, R. D., Esko, J. D., et al. (2009) · Cited by 8 · see citing works
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Metabolism Characteristics of Lactic Acid Bacteria and the Expanding Applications in Food Industry
Wang, Y., Wu, J., Lv, M., Shao, Z., Hungwe, M., Wang, J., Bai, X., Xie, J., Wang, Y., & Geng, W. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.612285 · Cited by 1,001 · see citing works
Postbiotics-Parabiotics: The New Horizons in Microbial Biotherapy and Functional Foods
Nataraj, B. H., Ali, S. A., Behare, P. V., & Yadav, H. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01426-w · Cited by 737 · see citing works
Application of bacteriocins and protective cultures in dairy food preservation
Silva, C. C. G., Silva, S. P. M., & Ribeiro, S. C. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00594 · Cited by 601 · see citing works
Gut Microbiota Profiling: Metabolomics Based Approach to Unravel Compounds Affecting Human Health
Vernocchi, P., Del Chierico, F., & Putignani, L. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01144 · Cited by 426 · see citing works
Lactic Acid Bacteria in Raw-Milk Cheeses: From Starter Cultures to Probiotic Functions
Coelho, M. C., Malcata, F. X., & Silva, C. C. G. (2022) · Foods · doi:10.3390/foods11152276 · Cited by 276 · see citing works
“Therefore, the anti-infective effect of bacteriocins produced by LAB represents a promising alternative to the use of antibiotics, especially in special cases where other methods are not allowed (e.g., pregnancy) [246].”
George, F., Daniel, C., Thomas, M., Singer, E., Guilbaud, A., Tessier, F. J., Revol-Junelles, A.-M., Borges, F., & Foligné, B. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02899 · Cited by 198 · see citing works
Zhao, Z.-T., Ding, J., Wang, B.-Y., Bao, M.-Y., Liu, B.-F., Pang, J.-W., Ren, N.-Q., & Yang, S.-S. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.148444 · Cited by 129 · see citing works
Kaškonienė, V., Stankevičius, M., Bimbiraitė-Survilienė, K., Naujokaitytė, G., Šernienė, L., Mulkytė, K., Malakauskas, M., & Maruška, A. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8088-9 · Cited by 99 · see citing works
Enterocins: Classification, Synthesis, Antibacterial Mechanisms and Food Applications
Wu, Y., Pang, X., Wu, Y., Liu, X., & Zhang, X. (2022) · Molecules · doi:10.3390/molecules27072258 · Cited by 82 · see citing works
Castro-López, C., García, H. S., Guadalupe Martínez-Ávila, G. C., González-Córdova, A. F., Vallejo-Cordoba, B., & Hernández-Mendoza, A. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.12.017 · Cited by 72 · see citing works
Zhang, D., Zhang, J., Kalimuthu, S., Liu, J., Song, Z.-M., He, B.-B., Cai, P., Zhong, Z., Feng, C., Neelakantan, P., et al. (2023) · Microbiome · doi:10.1186/s40168-023-01540-y · Cited by 72 · see citing works
“Previous biosynthetic analysis of LAB in a limited data-set focuses on particular metabolites, proposing their protective roles to host [40, 41].”
Natural bacterial isolates as an inexhaustible source of new bacteriocins
Lozo, J., Topisirovic, L., & Kojic, M. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-11063-3 · Cited by 63 · see citing works
Angelescu, I.-R., Grosu-Tudor, S.-S., Cojoc, L.-R., Maria, G.-M., Chirițoiu, G. N., Munteanu, C. V. A., & Zamfir, M. (2022) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-022-03408-z · Cited by 26 · see citing works
Conjugative DNA Transfer From E. coli to Transformation-Resistant Lactobacilli
Samperio, S., Guzmán-Herrador, D. L., May-Cuz, R., Martín, M. C., Álvarez, M. A., & Llosa, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.606629 · Cited by 25 · see citing works
Do Bacteria Provide an Alternative to Cancer Treatment and What Role Does Lactic Acid Bacteria Play?
Dicks, L. M. T., & Vermeulen, W. (2022) · Microorganisms · doi:10.3390/microorganisms10091733 · Cited by 25 · see citing works
Thayalan, D. T., Abdullah, R., Md Noor, S. S., & Mohamad, S. (2021) · Archives of Orofacial Sciences · doi:10.21315/aos2021.16.2.6 · Cited by 3 · see citing works
Katona, G., Jovanovic Ljeskovic, N., Strahinic, I., Stanisavljevic, N., Vojvodic, S., Djuris, J., & Pavic, A. (2025) · Molecules · doi:10.3390/molecules30204134 · Cited by 1 · see citing works
- Authors
- Alvarez-Sieiro, P., Montalbán-López, M., Mu, D., & Kuipers, O. P.
- Affiliations
- Hefei University of Technology (CN)
- University of Groningen (NL)
- Corresponding author
- Kuipers, Oscar P.
- Venue
- Applied Microbiology and Biotechnology
- Published
- 2016-02-10
- Volume
- 100
- Issue
- 7
- Pages
- 2939-2951
- ISSN
- 0175-7598 (ISSN-L)
- 1432-0614
- PMC
- PMC4786598
- OpenAlex
- W2252348097
- Cited by
- 729
- References
- 126
- Citations by year
- 2026: 43 · 2025: 66 · 2024: 96 · 2023: 88 · 2022: 99 · 2021: 82 · 2020: 84 · 2019: 62 · 2018: 55 · 2017: 40 · 2016: 13
- FWCI
- 6.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Applied Microbiology and Biotechnology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, cc-by)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, cc-by)
- Funders
- China Scholarship Council (2010605032)
- Seventh Framework Programme (Synpeptide)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Keywords
- bacteriocins, lactic acid bacteria, bacteriocin gene clusters, bacteriocin biosynthesis, bacteriocin classification, food biopreservation, antimicrobial peptides, post-translational modification, food industry applications
- MeSH terms
- Bacterial Proteins, Bacteriocins, Bifidobacterium, Fermentation, Food Microbiology, Multigene Family, Lactobacillaceae, Gene Expression, Lactic Acid
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