Antibacterial activities of bacteriocins: Application in foods and pharmaceuticals

Frontiers in Microbiology

Volumn 5, Issue MAY, 2014, Pages

  Yang, Shih Chun ^a,b   Lin, Chih Hung ^a   Sung, Calvin T ^c   Fang, Jia You ^a,b  

^a CHANG GUNG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Taiwan)

^b CHANG GUNG UNIVERSITY   (Taiwan)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Bacteriocin; Cancer treatment; Food; Natural product; Protein

Indexed keywords

ABC TRANSPORTER A1; BACTERIAL PROTEIN; BACTERIOCIN; BACTERIOCIN RELEASE PROTEIN; COLICIN; COLICIN E1; COLICIN E3; FOOD ADDITIVE; FOOD PRESERVATIVE; LACTOCOCCIN; MICROCIN; MICROCIN B17; MICROCIN J25; PEDIOCIN; PORE FORMING CYTOTOXIC PROTEIN; PROBIOTIC AGENT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANTIBACTERIAL ACTIVITY; BACTERIAL FLORA; BACTERIAL GENETICS; BACTERIAL GROWTH; BACTERIAL TRANSLOCATION; BACTERIOLYSIS; BACTERIUM CONTAMINATION; CANCER THERAPY; COLORECTAL CARCINOMA; ESCHERICHIA COLI; FOOD HANDLING; FOOD PRESERVATION; GROWTH INHIBITION; HEAD AND NECK SQUAMOUS CELL CARCINOMA; HEMOLYTIC UREMIC SYNDROME; HUMAN; NONHUMAN; PATHOGENESIS; REVIEW;

EID: 84904901819     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00241     Document Type: Review

References (101)

1. Acuña, L., Picariello, G., Sesma, F., Morero, R. D., and Bellomio, A. (2012). A new hybrid bacteriocin, Ent35-MccV, displays antimicrobial activity against pathogenic Gram-positive and Gram-negative bacteria. FEBS Open Bio 2, 12-19. doi: 10.1016/j.fob.2012.01.002
2. Akutsu, A., Masaki, H., and Ohta, T. (1989). Molecular structure and immunity specificity of colicin E6, an evolutionary intermediate between E-group colicins and cloacin DF13. J. Bacteriol. 171, 6430-6436.
3. Allison, G. E., Fremaux, C., and Klaenhammer, T. R. (1994). Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176, 2235-2241.
4. Babasaki, K., Takao, T., Shimonishi, Y., and Kurahashi, K. (1985). Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis. J. Bacteriol. 98, 585-603.
5. Bernbom, N., Licht, T. R., Brogren, C. H., Jelle, B., Johansen, A. H., Badiola, I., et al. (2006). Effects of Lactococcus lactis on composition of intestinal microbiota: role of nisin. Appl. Environ. Microbiol. 72, 239-244. doi: 10.1128/AEM.72.1.239-244.2006
6. Bures, J., Horák, V., Fixa, B., Komárková, O., Zaydlar, K., Lonski, V., et al. (1986). Colicinogeny in colorectal cancer. Neoplasma 33, 233-237.
7. Burton, J. P., Wescombe, P. A., Macklaim, J. M., Chai, M. H., Macdonald, K., Hale, J. D., et al. (2013). Persistence of the oral probiotic Streptococcus salivarius M18 is dose dependent and megaplasmid transfer can augment their bacteriocin production and adhesion characteristics. PLoS ONE 8:e65991. doi: 10.1371/journal.pone.0065991
8. Cascales, E., Buchanan, S. K., Duche, D., Kleanthous, C., Lloubès, R., Postle, K., et al. (2007). Colicin biology. Microbiol. Mol. Biol. Rev. 71, 158-229. doi: 10.1128/MMBR.00036-06
9. Center, N. (2013). Cancer Facts and Figures 2013. Goyang: Director of National Cancer Center Minister of Health and Welfare.
10. Chak, K. F., Kuo, W. S., Lu, F. M., and James, R. (1991). Cloning and characterization of the ColE7 plasmid. J. Gen. Microbiol. 137, 91-100. doi: 10.1099/00221287-137-1-91
11. Chatterjee, S., Chatterjee, S., Lad, S. J., Phansalkar, M. S., Rupp, R. H., Ganguli, B. N., et al. (1992). Mersacidin, a new antibiotic from Bacillus. Fermentation, isolation, purification and chemical characterization. J. Antibiot. (Tokyo) 45, 832-838. doi: 10.7164/antibiotics.45.832
12. Chumchalová, J., and Smarda, J. (2003). Human tumor cells are selectively inhibited by colicins. Folia Microbiol. (Praha) 48, 111-115. doi: 10.1007/BF02931286
13. Cleveland, J., Montville, T. J., Nes, I. F., and Chikindas, M. L. (2001). Bacteriocins: safe, natural antimicrobials for food preservation. Int. J. Food Microbiol. 71, 1-20. doi: 10.1016/S0168-1605(01)00560-8
14. Collin, F., Thompson, R. E., Jolliffe, K. A., Payne, R. J., and Maxwell, A. (2013). Fragments of the bacterial toxin microcin B17 as gyrase poisons. PLoS ONE 8:e61459. doi: 10.1371/journal.pone.0061459
15. Corr, S. C., Li, Y., Riedel, C. U., O'Toole, P. W., Hill, C., and Gahan, C. G. (2007). Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118. Proc. Natl. Acad. Sci. U.S.A. 104, 7617-7621. doi: 10.1073/pnas.0700440104
16. Corsini, G., Karahanian, E., Tello, M., Fernandez, K., Rivero, D., Saavedra, J. M., et al. (2010). Purification and characterization of the antimicrobial peptide microcin N. FEMS Microbiol. Lett. 312, 119-125. doi: 10.1111/j.1574-6968.2010.02106.x
17. Cotter, P. D., Hill, C., and Ross, R. P. (2005). Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 3, 777-788. doi: 10.1038/nrmicro1273
18. Cotter, P. D., Ross, R. P., and Hill, C. (2013). Bacteriocins-a viable alternative to antibiotics? Nat. Rev. Microbiol. 11, 95-105. doi: 10.1038/nrmicro2937
19. Cursino, L., Chartone-Souza, E., and Nascimento, A. (2002). Recent updated aspects of colicins of Enterobacteriaceae. Braz. J. Microbiol. 33, 185-195. doi: 10.1590/S1517-83822002000300001
20. Cursino, L., Smajs, D., Smarda, J., Nardi, R. M., Nicoli, J. R., Chartone-Souza, E., et al. (2006). Exoproducts of the Escherichia coli strain H22 inhibiting some enteric pathogens both in vitro and in vivo. J. Appl. Microbiol. 100, 821-829. doi: 10.1111/j.1365-2672.2006.02834.x
21. Cutler, S. A., Lonergan, S. M., Cornick, N., Johnson, A. K., and Stahl, C. H. (2007). Dietary inclusion of colicin e1 is effective in preventing postweaning diarrhea caused by F18-positive Escherichia coli in pigs. Antimicrob. Agents Chemother. 51, 3830-3835. doi: 10.1128/AAC.00360-07
22. Dabour, N., Zihler, A., Kheadr, E., Lacroix, C., and Fliss, I. (2009). In vivo study on the effectiveness of pediocin PA-1 and Pediococcus acidilactici UL5 at inhibiting Listeria monocytogenes. Int. J. Food Microbiol. 133, 225-233. doi: 10.1016/j.ijfoodmicro.2009.05.005
23. Deegan, L. H., Cotter, P. D., Hill, C., and Ross, P. (2006). Bacteriocins: biological tools for bio-preservation and shelf-life extension. Int. Dairy J. 16, 1058-1071. doi: 10.1016/j.idairyj.2005.10.026
24. de Lorenzo, V., and Pugsley, A. P. (1985). Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane. Antimicrob. Agents Chemother. 27, 666-669. doi: 10.1128/AAC.27.4.666
25. Dimov, S., Ivanova, P., Harizanova, N., and Ivanova, I. (2005). Bioactive peptides used by bacteria in the concurrence for the ecological niche: eneral classification and mode of action (overview). Biotechnol. Biotechnol. Eq. 3, 3-22. doi: 10.1080/13102818.2005.10817185
26. Dobson, A., Cotter, P. D., Ross, R. P., and Hill, C. (2012). Bacteriocin production: a probiotic trait? Appl. Environ. Microbiol. 78, 1-6. doi: 10.1128/AEM.05576-11
27. Duquesne, S., Petit, V., Peduzzi, J., and Rebuffat, S. (2007). Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J. Mol. Microbiol. Biotechnol. 13, 200-209. doi: 10.1159/000104748
28. FAO/WHO. (2001). Report on Joint FAO/WHO Expert Consultation on Evaluation of Health and Nutritional Properties of Probiotics in Food Including Powder Milk With Live Lactic Acid Bacteria. Córdoba: FAO/WHO.
29. Fath, M. J., Zhang, L. H., Rush, J., and Kolter, R. (1994). Purification and characterization of colicin V from Escherichia coli culture supernatants. Biochemistry 33, 6911-6917. doi: 10.1021/bi00188a021
30. Field, D., Begley, M., O'Connor, P. M., Daly, K. M., Hugenholtz, F., Cotter, P. D., et al. (2012). Bioengineered nisin A derivatives with enhanced activity against both Gram positive and Gram negative pathogens. PLoS ONE 7:e46884. doi: 10.1371/journal.pone.0046884
31. Flynn, S., van Sinderen, D., Thornton, G. M., Holo, H., Nes, I. F., and Collins, J. K. (2002). Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118. Microbiology 148, 973-984.
32. Foulquié Moreno, M. R., Sarantinopoulos, P., Tsakalidou, E., and De Vuyst, L. (2006). The role and application of enterococci in food and health. Int. J. Food Microbiol. 106, 1-24. doi: 10.1016/j.ijfoodmicro.2005.06.026
33. Fremaux, C., Ahn, C., and Klaenhammer, T. R. (1993). Molecular analysis of the lactacin F operon. Appl. Environ. Microbiol. 59, 3906-3915.
34. Fuller, R. (1989). Probiotics in man and animals. Experientia 35, 406-407.
35. Fuska, J., Fuskova, A., Smarda, J., and Mach, J. (1979). Effect of colicin E3 on leukemia cells P388 in vitro. Experientia 35, 406-407. doi: 10.1007/BF01964380
36. Ghrairi, T., Chaftar, N., and Hani, K. (2012). "Bacteriocins: recent advances and opportunities" in Progress in Food Preservation, Chapter 23. eds R. Bhat, A. Karim Alias and G. Paliyath (Oxford: Wiley-Blackwell), 485-511.
37. Gillor, O., Giladi, I., and Riley, M. A. (2009). Persistence of colicinogenic Escherichia coli in the mouse gastrointestinal tract. BMC Microbiol. 9:165. doi: 10.1186/1471-2180-9-165
38. Gong, X., Martin-Visscher, L. A., Nahirney, D., Vederas, J. C., and Duszyk, M. (2009). The circular bacteriocin, carnocyclin A, forms anion-selective channels in lipid bilayers. Biochim. Biophys. Acta 1788, 1797-1803. doi: 10.1016/j.bbamem.2009.05.008
39. Gratia, A. (1925). Sur un remarquable example d'antagonisme entre deux souches de colibacille. Comput. Rend. Soc. Biol. 93, 1040-1042.
40. Grinter, R., Milner, J., and Walker, D. (2012). Bacteriocins active against plant pathogenic bacteria. Biochem. Soc. Trans. 40, 1498-1502. doi: 10.1042/BST20120206
41. Guasch, J. F., Enfedaque, J., Ferrer, S., Gargallo, D., and Regue, M. (1995). Bacteriocin 28b, a chromosomally encoded bacteriocin produced by most Serratia marcescens biotypes. Res. Microbiol. 146, 477-483. doi: 10.1016/0923-2508(96)80293-2
42. Henderson, J. T., Chopko, A. L., and van Wassenaar, P. D. (1992). Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch. Biochem. Biophys. 295, 5-12. doi: 10.1016/0003-9861(92)90480-K
43. Herschman, H. R., and Helinski, D. R. (1967). Purification and characterization of colicin E2 and colicin E3. J. Biol. Chem. 242, 5360-5368.
44. Holo, H., Nilssen, O., and Nes, I. F. (1991). Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. J. Bacteriol. 173, 3879-3887.
45. Ito, Y., Kawai, Y., Arakawa, K., Honme, Y., Sasaki, T., and Saito, T. (2009). Conjugative plasmid from Lactobacillus gasseri LA39 that carries genes for production of and immunity to the circular bacteriocin gassericin A. Appl. Environ. Microbiol. 75, 6340-6351. doi: 10.1128/AEM.00195-09
46. Joerger, M. C., and Klaenhammer, T. R. (1986). Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481. J. Bacteriol. 167, 439-446.
47. Joerger, M. C., and Klaenhammer, T. R. (1990). Cloning, expression, and nucleotide sequence of the Lactobacillus helveticus 481 gene encoding the bacteriocin helveticin J. J. Bacteriol. 172, 6339-6347.
48. Joerger, R. D. (2003). Alternatives to antibiotics: bacteriocins, antimicrobial peptides and bacteriophages. Poult. Sci. 82, 640-647. doi: 10.1093/ps/82.4.640
49. Joo, N. E., Ritchie, K., Kamarajan, P., Miao, D., and Kapila, Y. L. (2012). Nisin, an apoptogenic bacteriocin and food preservative, attenuates HNSCC tumorigenesis via CHAC1. Cancer Med. 1, 295-305. doi: 10.1002/cam4.35
50. Jordi, B. J., Boutaga, K., van Heeswijk, C. M., van Knapen, F., and Lipman, L. J. (2001). Sensitivity of Shiga toxin-producing Escherichia coli (STEC) strains for colicins under different experimental conditions. FEMS. Microbiol. Lett. 204, 329-334. doi: 10.1111/j.1574-6968.2001.tb10906.x
51. Józefiak, D., Kieroñczyk, B., Juœkiewicz, J., Zduñczyk, Z., Rawski, M., Dlugosz, J., et al. (2013). Dietary nisin modulates the gastrointestinal microbial ecology and enhances growth performance of the broiler chickens. PLoS ONE 8:e85347. doi: 10.1371/journal.pone.0085347
52. Kawulka, K. E., Sprules, T., Diaper, C. M., Whittal, R. M., McKay, R. T., Mercier, P., et al. (2004). Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to alpha-carbon cross-links: formation and reduction of alpha-thio-alpha-amino acid derivatives. Biochemistry 43, 3385-3395. doi: 10.1021/bi0359527
53. Kleanthous, C. (2010). Swimming against the tide: progress and challenges in our understanding of colicin translocation. Nat. Rev. Microbiol. 8, 843-848. doi: 10.1038/nrmicro2454
54. Kock, J., Olschlager, T., Kamp, R. M., and Braun, V. (1987). Primary structure of colicin M, an inhibitor of murein biosynthesis. J. Bacteriol. 169, 3358-3361.
55. Konisky, J., and Richards, F. M. (1970). Characterization of Colicin Ia and Colicin Ib purification and some physical properties. J. Biol. Chem. 245, 2972-2978.
56. Lancaster, L. E., Wintermeyer, W., and Rodnina, M. V. (2007). Colicins and their potential in cancer treatment. Blood Cells Mol. Dis. 38, 15-18. doi: 10.1016/j.bcmd.2006.10.006
57. Lilly, D. M., and Stillwell, R. H. (1965). Porbiotics: growth-promoting factors produced by microorganisms. Science 147, 747-748. doi: 10.1126/science.147.3659.747
58. Macdonald, C. J., Tozawa, K., Collins, E. S., Penfold, C. N., James, R., Kleanthous, C., et al. (2004). Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9. J. Biomol. NMR 30, 81-96. doi: 10.1023/B:JNMR.0000042963.71790.19
59. Males, B. M., and Stocker, B. A. (1982). Colicins E4, E5, E6 and A and properties of btuB+ colicinogenic transconjugants. J. Gen. Microbiol. 128, 95-106.
60. Martinez, J. L., and Perez-Diaz, J. C. (1986). Isolation, characterization, and mode of action on Escherichia coli strains of microcin D93. Antimicrob. Agents Chemother. 29, 456-460. doi: 10.1128/AAC.29.3.456
61. Martínez-Bueno, M., Maqueda, M., Gálvez, A., Samyn, B., Van Beeumen, J., Coyette, J., et al. (1994). Determination of the gene sequence and the molecular structure of the enterococcal peptide antibiotic AS-48. J. Bacteriol. 176, 6334-6339.
62. Martin-Visscher, L. A., Gong, X., Duszyk, M., and Vederas, J. C. (2009). The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif. J. Biol. Chem. 284, 28674-28681. doi: 10.1074/jbc.M109.036459
63. Martin-Visscher, L. A., van Belkum, M. J., Garneau-Tsodikova, S., Whittal, R. M., Zheng, J., McMullen, L. M., et al. (2008). Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307. Appl. Environ. Microbiol. 74, 4756-4763. doi: 10.1128/AEM.00817-08
64. Meindl, K., Schmiederer, T., Schneider, K., Reicke, A., Butz, D., Keller, S., et al. (2010). Labyrinthopeptins: a new class of carbacyclic lantibiotics. Angew. Chem. Int. Ed. Engl. 49, 1151-1154. doi: 10.1002/anie.200905773
65. Millette, M., Cornut, G., Dupont, C., Shareck, F., Archambault, D., and Lacroix, M. (2008). Capacity of human nisin- and pediocin-producing lactic Acid bacteria to reduce intestinal colonization by vancomycin-resistant enterococci. Appl. Environ. Microbiol. 74, 1997-2003. doi: 10.1128/AEM.02150-07
66. Morlon, J., Lloubes, R., Varenne, S., Chartier, M., and Lazdunski, C. (1983). Complete nucleotide sequence of the structural gene for colicin A, a gene translated at non-uniform rate. J. Mol. Biol. 170, 271-285. doi: 10.1016/S0022-2836(83)80148-X
67. Mulders, J. W., Boerrigter, I. J., Rollema, H. S., Siezen, R. J., and de Vos, W. M. (1991). Identification and characterization of the lantibiotic nisin Z, a natural nisin variant. Eur. J. Biochem. 201, 581-584. doi: 10.1111/j.1432-1033.1991.tb16317.x
68. Müller, E., and Radler, F. (1993). Caseicin, a bacteriocin from Lactobacillus casei. Folia Microbiol. (Praha) 38, 441-446. doi: 10.1007/BF02814392
69. Nilsen, T., Nes, I. F., and Holo, H. (2003). Enterolysin A, a cell wall-degrading bacteriocin from Enterococcus faecalis LMG 2333. Appl. Environ. Microbiol. 69, 2975-2984. doi: 10.1128/AEM.69.5.2975-2984.2003
70. Pilsl, H., and Braun, V. (1995a). Evidence that the immunity protein inactivates colicin 5 immediately prior to the formation of the transmembrane channel. J. Bacteriol. 177, 6966-6972.
71. Pilsl, H., and Braun, V. (1995b). Novel colicin 10: assignment of four domains to TonB-and TolC dependent uptake via the Tsx receptor and to pore formation. Mol. Microbiol. 16, 57-67. doi: 10.1111/j.1365-2958.1995.tb02391.x
72. Pilsl, H., and Braun, V. (1995c). Strong function-related homology between the pore-forming colicins K and 5. J. Bacteriol. 177, 6973-6977.
73. Pilsl, H., Smajs, D., and Braun, V. (1999). Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane. J. Bacteriol. 181, 3578-3581.
74. Pons, A. M., Delalande, F., Duarte, M., Benoit, S., Lanneluc, I., Sable, S., et al. (2004). Genetic analysis and complete primary structure of microcin L. Antimicrob. Agents Chemother. 48, 505-513. doi: 10.1128/AAC.48.2.505-513.2004
75. Pons, A. M., Zorn, N., Vignon, D., Delalande, F., Van Dorsselaer, A., and Cottenceau, G. (2002). Microcin E492 is an unmodified peptide related in structure to colicin V. Antimicrob. Agents Chemother. 46, 229-230. doi: 10.1128/AAC.46.1.229-230.2002
76. Pugsley, A. P. (1987). Nucleotide sequencing of the structural gene for colicin N reveals homology between the catalytic, C-terminal domains of colicins A and N. Mol. Microbiol. 1, 317-325. doi: 10.1111/j.1365-2958.1987.tb01938.x
77. Rebuffat, S. (2012). Microcins in action: amazing defence strategies of Enterobacteria. Biochem. Soc. Trans. 40, 1456-1462. doi: 10.1042/BST20120183
78. Riboulet-Bisson, E., Sturme, M. H., Jeffery, I. B., O'Donnell, M. M., Neville, B. A., Forde, B. M., et al. (2012). Effect of Lactobacillus salivarius bacteriocin Abp118 on the mouse and pig intestinal microbiota. PLoS ONE 7:e31113. doi: 10.1371/journal.pone.0031113
79. Riley, M. A., and Wertz, J. E. (2002). Bacteriocins: evolution, ecology, and application. Annu. Rev. Microbiol. 56, 117-137. doi: 10.1146/annurev.micro.56.012302.161024
80. Rogers, L. A. (1928). The inhibiting effect of Streptococcus lactis on Lactobacillus bulgaricus. J. Bacteriol. 16, 321-325.
81. Roos, U., Harkness, R. E., and Braun, V. (1989). Assembly of colicin genes from a few DNA fragments. Nucleotide sequence of colicin D. Mol. Microbiol. 3, 891-902. doi: 10.1111/j.1365-2958.1989.tb00238.x
82. Samyn, B., Martinez-Bueno, M., Devreese, B., Maqueda, M., Galvez, A., Valdivia, E., et al. (1994). The cyclic structure of the enterococcal peptide antibiotic AS-48. FEBS Lett. 352, 87-90. doi: 10.1016/0014-5793(94)00925-2
83. Sandiford, S., and Upton, M. (2012). Identification, characterization, and recombinant expression of epidermicin NI01, a novel unmodified bacteriocin produced by Staphylococcus epidermidis that displays potent activity against Staphylococci. Antimicrob. Agents Chemother. 56, 1539-1547. doi: 10.1128/AAC.05397-11
84. Schramm, E., Mende, J., Braun, V., and Kamp, R. M. (1987). Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J. Bacteriol. 169, 3350-3357.
85. Settanni, L., and Corsetti, A. (2008). Application of bacteriocins in vegetable food biopreservation. Int. J. Food Microbiol. 121, 123-138. doi: 10.1016/j.ijfoodmicro.2007.09.001
86. Severinov, K., Semenova, E., Kazakov, A., Kazakov, T., and Gelfand, M. S. (2007). Low-molecular-weight post-translationally modified microcins. Mol. Microbiol. 65, 1380-1394. doi: 10.1111/j.1365-2958.2007.05874.x
87. Siegel, R., Naishadham, D., and Jemal, A. (2013). Cancer statistics, 2013. CA Cancer J. Clin. 63, 11-30. doi: 10.3322/caac.21166
88. Smajs, D., Pilsl, H., and Braun, V. (1997). Colicin U, a novel colicin produced by Shigella boydii. J. Bacteriol. 179, 4919-4928.
89. Stahl, C. H., Callaway, T. R., Lincoln, L. M., Lonergan, S. M., and Genovese, K. J. (2004). Inhibitory activities of colicins against Escherichia coli strains responsible for postweaning diarrhea and edema disease in swine. Antimicrob. Agents Chemother. 48, 3119-3121. doi: 10.1128/AAC.48.8.3119-3121.2004
90. Stern, N. J., Svetoch, E. A., Eruslanov, B. V., Perelygin, V. V., Mitsevich, E. V., Mitsevich, I. P., et al. (2006). Isolation of a Lactobacillus salivarius strain and purification of its bacteriocin, which is inhibitory to Campylobacter jejuni in the chicken gastrointestinal system. Antimicrob. Agents Chemother. 50, 3111-3116. doi: 10.1128/AAC.00259-06
91. Toba, M., Masaki, H., and Ohta, T. (1988). Colicin E8, a DNase which indicates an evolutionary relationship between colicins E2 and E3. J. Bacteriol. 170, 3237-3242.
92. Todorov, S. D., Franco, B. D., and Wiid, I. J. (2014). In vitro study of beneficial properties and safety of lactic acid bacteria isolated from Portuguese fermented meat products. Benef. Microbes. 24, 1-16. doi: 10.3920/BM2013.0030
93. Tulini, F. L., Lohans, C. T., Bordon, K. C., Zheng, J., Arantes, E. C., Vederas, J. C., et al. (2014). Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2. Int. J. Food Microbiol. 173, 81-88. doi: 10.1016/j.ijfoodmicro.2013.12.019
94. van den Elzen, P. J., Walters, H. H., Veltkamp, E., and Nijkamp, H. J. J. (1983). Molecular structure and function of the bacteriocin gene and bacteriocin protein of plasmid Clo DF13. Nucleic Acids Res. 11, 2465-2477. doi: 10.1093/nar/11.8.2465
95. van Heel, A. J., Montalban-Lopez, M., and Kuipers, O. P. (2011). Evaluating the feasibility of lantibiotics as an alternative therapy against bacterial infections in humans. Expert Opin. Drug Metab. Toxicol. 7, 675-680. doi: 10.1517/17425255.2011.573478
96. Varenne, S., Cavard, D., and Lazdunski, C. (1981). Biosynthesis and export of colicin A in Citrobacter freundii CA31. Eur. J. Biochem. 116, 615-620. doi: 10.1111/j.1432-1033.1981.tb05380.x
97. Vassiliadis, G., Destoumieux-Garzon, D., Lombard, C., Rebuffat, S., and Peduzzi, J. (2010). Isolation and characterization of two members of the siderophore-microcin family, microcins M and H47. Antimicrob. Agents Chemother. 54, 288-297. doi: 10.1128/AAC.00744-09
98. Wilson, K. A., Kalkum, M., Ottesen, J., Yuzenkova, J., Chait, B. T., Landick, R., et al. (2003). Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail. J. Am. Chem. Soc. 125, 12475-12483. doi: 10.1021/ja036756q
99. Wirawan, R. E., Klesse, N. A., Jack, R. W., and Tagg, J. R. (2006). Molecular and genetic characterization of a novel nisin variant produced by Streptococcus uberis. Appl. Environ. Microbiol. 72, 1148-1156. doi: 10.1128/AEM.72.2.1148-1156.2006
100. Yamada, M., Ebina, Y., Miyata, T., Nakazawa, T., and Nakazawa, A. (1982). Nucleotide sequence of the structural gene for colicin E1 and predicted structure of the protein. Proc. Natl. Acad. Sci. U.S.A. 79, 2827-2831. doi: 10.1073/pnas.79.9.2827
101. Yang, E., Fan, L., Jiang, Y., Doucette, C., and Fillmore, S. (2012). Antimicrobial activity of bacteriocin-producing lactic acid bacteria isolated from cheeses and yogurts. AMB Exp. 2, 48. doi: 10.1186/2191-0855-2-48