메뉴 건너뛰기




Volumn 62, Issue 3, 2013, Pages 223-235

Characteristic of bacteriocines and their application

Author keywords

Antimicrobial peptides; Bacteriocines; Enterocines; Lactic acid bacteria; Lactobacillus sp.; Lantibiotics

Indexed keywords

ACIDOCIN B; ANTIINFECTIVE AGENT; AVICIN A; BACTERIOCIN; CARNOBACTERIOCIN A; CURVACIN A; CYTOLYSIN; ENTEROCIN A; ENTEROCIN I; ENTEROCIN P; ENTEROCIN Q; GLYCOCIN F; HELVETICIN J; LACTACIN F; LACTOBIN A; LACTOCIN 705; LACTOCOCCIN; LEUCOCIN A; MESENTERICIN Y105; MUTACIN B NY266; NISIN A; NISIN U; NISIN Z; PEDIOCIN PA 1; PLANTARICIN F; SALIVARICIN A; SUBTILOSIN A; UBERICIN A; UBEROLISIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84886793538     PISSN: 17331331     EISSN: None     Source Type: Journal    
DOI: 10.33073/pjm-2013-030     Document Type: Review
Times cited : (49)

References (144)
  • 1
    • 0028220778 scopus 로고
    • Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon
    • Allison G.E., C. Fremaux and T.R. Klaenhammer. 1994. Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176: 2235-2241. (Pubitemid 24118171)
    • (1994) Journal of Bacteriology , vol.176 , Issue.8 , pp. 2235-2241
    • Allison, G.E.1    Fremaux, C.2    Klaenhammer, T.R.3
  • 2
    • 34548630324 scopus 로고    scopus 로고
    • Evaluation of the antagonistic effect of Lactobacillus acidophilus on clinical strains of Helicobacter pylori (in Polish)
    • Andrzejewska E. and A. Szkaradkiewicz. 2007. Evaluation of the antagonistic effect of Lactobacillus acidophilus on clinical strains of Helicobacter pylori (in Polish). Med. Dośw. 59: 59-64.
    • (2007) Med. Dośw. , vol.59 , pp. 59-64
    • Andrzejewska, E.1    Szkaradkiewicz, A.2
  • 5
    • 0030012762 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins
    • Aymerich T., H. Holo, L.S. Håvarstein, M. Hugas, M. Garriga and I.F. Nes. 1996. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microbiol. 62: 1676-1682. (Pubitemid 26143442)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.5 , pp. 1676-1682
    • Aymerich, T.1    Holo, H.2    Havarstein, L.S.3    Hugas, M.4    Garriga, M.5    Nes, I.F.6
  • 6
    • 0035111967 scopus 로고    scopus 로고
    • The structure, function, and origin of the microcin H47 ATP-binding cassette exporter indicate its relatedness to that of colicin V
    • DOI 10.1128/AAC.45.3.969-972.2001
    • Azpiroz M.F., E. Rodriguez and M. Lavina. 2001. The structure, function, and origin of the microcin H47 ATP-binding cassette exporter indicate its relatedness to that of colicin V. Antimicrob. Agents Chemother. 45: 969-972. (Pubitemid 32182059)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.3 , pp. 969-972
    • Azpiroz, M.F.1    Rodriguez, E.2    Lavina, M.3
  • 10
    • 0021135655 scopus 로고
    • Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B
    • Barefoot S.F. and T.R. Klaenhammer. 1984. Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B. Antimicrob. Agents Chemother. 26: 328-334. (Pubitemid 14006018)
    • (1984) Antimicrobial Agents and Chemotherapy , vol.26 , Issue.3 , pp. 328-334
    • Barefoot, S.F.1    Klaenhammer, T.R.2
  • 11
    • 47349108506 scopus 로고    scopus 로고
    • Antimicrobial activity of Enterococcus faecium L50, a strain producing enterocin L50 (L50A and L50B), P and Q, against beer-spoilage lactic acid bacteria in broth, wort (hopped and unhopped), and alcoholic and non-alcoholic lager beers
    • Basanta A., J. Sánchez, B. Gómez-Sala, C. Herranz, P.E. Hernández and L.M. Cintas. 2008. Antimicrobial activity of Enterococcus faecium L50, a strain producing enterocin L50 (L50A and L50B), P and Q, against beer-spoilage lactic acid bacteria in broth, wort (hopped and unhopped), and alcoholic and non-alcoholic lager beers. Int. J. Food Microbiol. 125: 293-307.
    • (2008) Int. J. Food Microbiol. , vol.125 , pp. 293-307
    • Basanta, A.1    Sánchez, J.2    Gómez-Sala, B.3    Herranz, C.4    Hernández, P.E.5    Cintas, L.M.6
  • 12
    • 84865541312 scopus 로고    scopus 로고
    • Bacteriocins from lactic acid bacteria: Microorganisms of potential biotechnological importance for the diary industry
    • Beshkova D. and G. Frengova. 2012. Bacteriocins from lactic acid bacteria: microorganisms of potential biotechnological importance for the diary industry. Eng. Life Sci. 12: 1-14.
    • (2012) Eng. Life Sci. , vol.12 , pp. 1-14
    • Beshkova, D.1    Frengova, G.2
  • 13
    • 75249089137 scopus 로고    scopus 로고
    • Molecular and genetic characterization of a novel bacteriocin locus in Enterococcus avium isolates from infants
    • Birri D.J., D.A. Brede, T. Forberg, H. Holo and I.F. Nes. 2010. Molecular and genetic characterization of a novel bacteriocin locus in Enterococcus avium isolates from infants. Appl. Environ. Microbiol. 76: 483-492.
    • (2010) Appl. Environ. Microbiol. , Issue.76 , pp. 483-492
    • Birri, D.J.1    Brede, D.A.2    Forberg, T.3    Holo, H.4    Nes, I.F.5
  • 14
    • 79955544137 scopus 로고    scopus 로고
    • In vitro studies indicate a high resistance potential for the lantibiotic nisin in Staphylococcus aureus and define a genetic basis for nisin resistance
    • Blake K.L., C.P. Randall and A.J. O'Neill. 2011. In vitro studies indicate a high resistance potential for the lantibiotic nisin in Staphylococcus aureus and define a genetic basis for nisin resistance. Antimicrob. Agents Chemother. 55: 2362-2368.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 2362-2368
    • Blake, K.L.1    Randall, C.P.2    O'Neill, A.J.3
  • 15
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • DOI 10.1016/S0300-9084(02)01427-X, PII S030090840201427X
    • Braun V., S.I. Patzer and K. Hantke. 2002. Ton-dependent colicins and microcins: modular design and evolution. Biochimie. 84: 365-380. (Pubitemid 35350867)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 16
    • 0028952641 scopus 로고
    • Mode of action of the lantibiotic mersacidin: Inhibition of peptidoglycan biosynthesis via a novel mechanism? Antimicrob
    • Brotz H., G. Bierbaum, A. Markus, E. Molitor and H.G. Sahl. 1995. Mode of action of the lantibiotic mersacidin: inhibition of peptidoglycan biosynthesis via a novel mechanism? Antimicrob. Agents Chemother. 39: 714-719.
    • (1995) Agents Chemother. , vol.39 , pp. 714-719
    • Brotz, H.1    Bierbaum, G.2    Markus, A.3    Molitor, E.4    Sahl, H.G.5
  • 17
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • Brotz H., G. Bierbaum, P.E. Reynolds and H.G. Sahl. 1997. The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation. Eur. J. Biochem. 246: 193-199. (Pubitemid 27229687)
    • (1997) European Journal of Biochemistry , vol.246 , Issue.1 , pp. 193-199
    • Brotz, H.1    Bierbaum, G.2    Reynolds, P.E.3    Sahl, H.-G.4
  • 19
    • 0030789029 scopus 로고    scopus 로고
    • Enterocin B, a new bacteriocin from enterococcus faecium T136 which can act synergistically with enterocin A
    • Casaus P., T. Nilsen, L.M. Cintas, I.F. Nes, P.E. Hernández and H. Holo. 1997. Enterocin B, a new bacteriocin from Enterococcus faecium T136 which can act synergistically with enterocin A. Microbiology 143 : 2287-2294. (Pubitemid 27356762)
    • (1997) Microbiology , vol.143 , Issue.7 , pp. 2287-2294
    • Casaus, P.1    Nilsen, T.2    Cintas, L.M.3    Nes, I.F.4    Hernandez, P.E.5    Holo, H.6
  • 23
    • 0030999249 scopus 로고    scopus 로고
    • Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationshipto a predicted tertiary structure
    • Chen Y., R. Shapira, M. Eisenstein and T.J. Montville. 1997. Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure. Appl. Environ. Microbiol. 63: 524-531. (Pubitemid 27121334)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.2 , pp. 524-531
    • Chen, Y.1    Shapira, R.2    Eisenstein, M.3    Montville, T.J.4
  • 24
    • 0027367211 scopus 로고
    • Plasmid-associated hemolysin and aggregation substance production contribute to virulence in experimental enterococcal endocarditis
    • Chow J.W., L.A. Thal, M.B. Perri, J.A. Vazquez, S.M. Donabedian, D.B. Clewell and M.J. Zervos. 1993. Plasmid-associated hemolysin and aggregation substance production contribute to virulence in experimental enterococcal endocarditis. Antimicrob. Agents Chemother. 37: 2474-2477. (Pubitemid 23324477)
    • (1993) Antimicrobial Agents and Chemotherapy , vol.37 , Issue.11 , pp. 2474-2477
    • Chow, J.W.1    Thal, L.A.2    Perri, M.B.3    Vazquez, J.A.4    Donabedian, S.M.5    Clewell, D.B.6    Zervos, M.J.7
  • 25
    • 0034462540 scopus 로고    scopus 로고
    • Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin p, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q
    • DOI 10.1128/JB.182.23.6806-6814.2000
    • Cintas L.M., P. Casaus, C. Herranz, L.S. Havarstein, H. Holo,P.E. Hernandez and I.F. Nes. 2000. Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q.J. Bacteriol. 182: 6806-6814. (Pubitemid 32249265)
    • (2000) Journal of Bacteriology , vol.182 , Issue.23 , pp. 6806-6814
    • Cintas, L.M.1    Casaus, P.2    Herranz, C.3    Havarstein, L.S.4    Holo, H.5    Hernandez, P.E.6    Nes, I.F.7
  • 26
    • 0032104340 scopus 로고    scopus 로고
    • Comparative antimicrobial activity of enterocin L50, pediocin PA-1, nisin A and lactocin S against spoilage and foodborne pathogenic bacteria
    • DOI 10.1006/fmic.1997.0160
    • Cintas L.M., P. Casaus, M.F. Fernández and P.E. Hernández. 1998; Comparative antimicrobial activity of enterocin L50, pediocin PA01, nisin A and lactocin S against spoilage and foodborne pathogenic bacteria. Food Microbiol. 15: 289-298. (Pubitemid 28338698)
    • (1998) Food Microbiology , vol.15 , Issue.3 , pp. 289-298
    • Cintas, L.M.1    Casaus, P.2    Fernandez, M.F.3    Hernandez, P.E.4
  • 28
    • 0141725789 scopus 로고    scopus 로고
    • The Enterococcus faecalis cytolysin: A novel toxin active against eukaryotic and prokaryotic cells
    • DOI 10.1046/j.1462-5822.2003.00310.x
    • Coburn P.S. and M.S. Gilmore. 2003. The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells. Cell Microbiol. 5: 661-669. (Pubitemid 37185043)
    • (2003) Cellular Microbiology , vol.5 , Issue.10 , pp. 661-669
    • Coburn, P.S.1    Gilmore, M.S.2
  • 29
    • 11144287200 scopus 로고    scopus 로고
    • Enterococcus faecalis senses target cells and in response expresses cytolysin
    • DOI 10.1126/science.1103996
    • Coburn P.S., C.M. Pillar, B.D. Jett, W. Haas and M.S. Gilmore. 2004. Enterococcus faecalis senses target cells and in response expresses cytolysin. Science 306: 2270-2272. (Pubitemid 40024467)
    • (2004) Science , vol.306 , Issue.5705 , pp. 2270-2272
    • Coburn, P.S.1    Pillar, C.M.2    Jett, B.D.3    Haas, W.4    Gilmore, M.S.5
  • 30
    • 0031765113 scopus 로고    scopus 로고
    • Antagonistic activity against Helicobacter infection in vitro and in vivo by the human Lactobacillus acidophilus strain LB
    • Coconnier M.-H., V. Lievin, E. Hemery and A.L. Servin. 1998. Antagonistic activity against Helicobacter infection in vitro and in vivo by the human Lactobacillus acidophilus strain LB. Appl. Environ. Microbiol. 64: 4573-4580. (Pubitemid 28538035)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.11 , pp. 4573-4580
    • Coconnier, M.-H.1    Lievin, V.2    Hemery, E.3    Servin, A.L.4
  • 31
    • 0022002775 scopus 로고
    • Molecular characterisation of the colicin E2 operon and identification of its products
    • DOI 10.1007/BF00332940
    • Cole S.T., B. Saint-Joanis and A.P. Pugsley. 1985. Molecular characterisation of the colicin E2 operon and identification of its products. Mol. Gen Genet. 198: 465-472. (Pubitemid 15106286)
    • (1985) Molecular and General Genetics , vol.198 , Issue.3 , pp. 465-472
    • Cole, S.T.1    Saint-Joanis, B.2    Pugsley, A.P.3
  • 33
    • 13844316746 scopus 로고    scopus 로고
    • Enterococcal cytolysin: A novel two component peptide system that serves as a bacterial defense against eukaryotic and prokaryotic cells
    • DOI 10.2174/1389203053027557
    • Cox C.R., P.S. Coburn and M.S. Gilmore. 2005. Enterococcal cytolysin: a novel two component peptide system that serves as a bacterial defense against eukaryotic and prokaryotic cells. Curr. Protein Pept. Sci. 6: 77-84. (Pubitemid 40259803)
    • (2005) Current Protein and Peptide Science , vol.6 , Issue.1 , pp. 77-84
    • Cox, C.R.1    Coburn, P.S.2    Gilmore, M.S.3
  • 34
    • 0034656248 scopus 로고    scopus 로고
    • Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lactobacillus casei CRL 705
    • DOI 10.1016/S0378-1097(00)00093-8, PII S0378109700000938
    • Cuozzo S.A., F. Sesma, J.M. Palacios, A.P. de Ruiz Holgado and R.R. Raya. 2000. Identification and nucleotide sequence of genes invol-ved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lactobacillus casei CRL 705. FEMS Microbiol. Lett. 185: 157-161. (Pubitemid 30168992)
    • (2000) FEMS Microbiology Letters , vol.185 , Issue.2 , pp. 157-161
    • Cuozzo, S.A.1    Sesma, F.2    Palacios, J.M.3    De Ruiz Holgado, A.P.4    Raya, R.R.5
  • 36
    • 0021987955 scopus 로고
    • Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane
    • de Lorenzo V. and A.P. Pugsley. 1985. Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane. Antimicrob Agents Chemother. 27: 666-669. (Pubitemid 15097685)
    • (1985) Antimicrobial Agents and Chemotherapy , vol.27 , Issue.4 , pp. 666-669
    • De Lorenzo, V.1    Pugsley, A.P.2
  • 37
    • 0346850954 scopus 로고    scopus 로고
    • The lactobin A and amylovorin L471 encoding genes are identical, and their distribution seems to be restricted to the species Lactobacillus amylovorus that is of interest for cereal fermentations
    • DOI 10.1016/S0168-1605(03)00298-8
    • De Vuyst L., L. Avonts, P. Neysens, B. Hoste, M. Vancanneyt,J. Swings and R. Callewaert. 2004. The lactobin A and amylovorin L471 encoding genes are identical, and their distribution seems to be restricted to the species Lactobacillus amylovorus that is of interest for cereal fermentations. Int. J. Food Microbiol. 90: 93-106. (Pubitemid 37522211)
    • (2004) International Journal of Food Microbiology , vol.90 , Issue.1 , pp. 93-106
    • De Vuyst, L.1    Avonts, L.2    Neysens, P.3    Hoste, B.4    Vancanneyt, M.5    Swings, J.6    Callewaert, R.7
  • 39
    • 0029565798 scopus 로고
    • A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11
    • Diep D.B., L.S. Håvarstein and I.F. Nes. 1995. A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol. Microbiol. 18: 631-639. (Pubitemid 26008844)
    • (1995) Molecular Microbiology , vol.18 , Issue.4 , pp. 631-639
    • Diep, D.B.1    Havarstein, L.S.2    Nes, I.F.3
  • 40
    • 0031864513 scopus 로고    scopus 로고
    • Disparate findings on the role of virulence factors of Enterococcus faecalis in mouse and rat models of peritonitis
    • Dupton H., P. Montravers, J. Mohler and C. Carbon. 1998. Disparate findings on the role of virulence factors of Enterococcus faecalis in mouse and rat model. Infect. Immun. 66: 2570-2575. (Pubitemid 28261754)
    • (1998) Infection and Immunity , vol.66 , Issue.6 , pp. 2570-2575
    • Dupont, H.1    Montravers, P.2    Mohler, J.3    Carbon, C.4
  • 41
    • 69449104828 scopus 로고    scopus 로고
    • Characterization of mundticin L, a class IIa anti-Listeria bacteriocin from Enterococcus mundtii CUGF08
    • Feng G., G.K.P. Guron, J.J. Churey and R.W. Worobo. 2009. Characterization of mundticin L, a class IIa anti-Listeria bacteriocin from Enterococcus mundtii CUGF08. Appl. Environ. Microbiol. 75: 5708-5713.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5708-5713
    • Feng, G.1    Guron, G.K.P.2    Churey, J.J.3    Worobo, R.W.4
  • 42
    • 0035960722 scopus 로고    scopus 로고
    • Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product
    • DOI 10.1016/S0378-1097(01)00435-9, PII S0378109701004359
    • Ferchichi M., J. Frère, K. Mabrouk and M. Manai. 2001. Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product. FEMS Microbiol. Lett. 205: 49-55. (Pubitemid 33135438)
    • (2001) FEMS Microbiology Letters , vol.205 , Issue.1 , pp. 49-55
    • Ferchichi, M.1    Frere, J.2    Mabrouk, K.3    Manai, M.4
  • 44
    • 0036230805 scopus 로고    scopus 로고
    • 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
    • Flynn S., D. van Sinderen, G.M. Thornton, H. Holo, I.F. Nes and J.K. Collins. 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. Microbiol. 148: 973-984. (Pubitemid 34436774)
    • (2002) Microbiology , vol.148 , Issue.4 , pp. 973-984
    • Flynn, S.1    Van Sinderen, D.2    Thornton, G.M.3    Holo, H.4    Nes, I.F.5    Collins, J.K.6
  • 45
    • 34047114842 scopus 로고    scopus 로고
    • Diversity of enterococcal bacteriocins and their grouping in a new classification scheme
    • DOI 10.1111/j.1574-6976.2007.00064.x
    • Franz C.M.A.P., M.J. van Belkum, W.H. Holzapfel, H. Abriouel and A. Gálvez. 2007. Diversity of enterococcal bacteriocins and their grouping in a new classification scheme. FEMS Microbiol. Rev. 31: 293-310. (Pubitemid 46525308)
    • (2007) FEMS Microbiology Reviews , vol.31 , Issue.3 , pp. 293-310
    • Franz, C.M.A.P.1    Van Belkum, M.J.2    Holzapfel, W.H.3    Abriouel, H.4    Galvez, A.5
  • 46
    • 0029094242 scopus 로고
    • Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105
    • Fremaux C., Y. Héchard and Y. Cenatiempo. 1995. Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105. Microbiology 141: 1637-1645.
    • (1995) Microbiology , vol.141 , pp. 1637-1645
    • Fremaux, C.1    Héchard, Y.2    Cenatiempo, Y.3
  • 47
    • 84985161098 scopus 로고
    • Probiotics in man and animals
    • Fuller R. 1989. Probiotics in man and animals. J. Appl. Bacteriol. 66: 365-378.
    • (1989) J. Appl. Bacteriol. , vol.66 , pp. 365-378
    • Fuller, R.1
  • 48
    • 4544293744 scopus 로고    scopus 로고
    • Isolation and characterization of enterocin EJ97, a bacteriocin produced by Enterococcus faecalis EJ97
    • DOI 10.1007/s002030050678
    • Gálvez A., E. Valdivia, H. Abriouel, E. Camafeita, E. Mendez,M. Martinez-Bueno and M. Maqueda. 1998. Isolation and characterization of enterocin EJ97, a bacteriocin produced by Enterococcus faecalis EJ97. Arch. Microbiol. 171: 59-65. (Pubitemid 29142555)
    • (1998) Archives of Microbiology , vol.171 , Issue.1 , pp. 59-65
    • Galvez, A.1    Valdivia, E.2    Abriouel, H.3    Camafeita, E.4    Mendez, E.5    Martinez-Bueno, M.6    Maqueda, M.7
  • 49
    • 0030724154 scopus 로고    scopus 로고
    • Acceleration of flavour formation in cheese by a bacteriocin-producing adjunct lactic culture
    • DOI 10.1023/A:1018451401925
    • Garde S., P. Gaya, M. Medina and M. Nunez. 1997. Acceleration of flavour formation in cheese by a bacteriocin-producing adjunct lactic culture. Biotechnol Lett. 10: 1011-1014. (Pubitemid 27466448)
    • (1997) Biotechnology Letters , vol.19 , Issue.10 , pp. 1011-1014
    • Garde, S.1    Gaya, P.2    Medina, M.3    Nunez, M.4
  • 50
    • 0036589172 scopus 로고    scopus 로고
    • Two-peptide bacteriocins produced by lactic acid bacteria
    • DOI 10.1016/S0300-9084(02)01414-1, PII S0300908402014141
    • Garneau S., N.I. Martin and J.C. Vederas. 2002. Two-peptide bacteriocins produced by lactic acid bacteria. Biochimie 84: 577-592. (Pubitemid 35350889)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 577-592
    • Garneau, S.1    Martin, N.I.2    Vederas, J.C.3
  • 51
    • 0028238737 scopus 로고
    • Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin
    • González B., P. Arca, B. Mayo and J.E. Suárez. 1994. Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of diary origin. Appl. Environ. Microbiol. 60: 2158-2163. (Pubitemid 24165870)
    • (1994) Applied and Environmental Microbiology , vol.60 , Issue.6 , pp. 2158-2163
    • Gonzalez, B.1    Arca, P.2    Mayo, B.3    Suarez, J.E.4
  • 52
    • 33746924921 scopus 로고    scopus 로고
    • Bacteriocins - Properties and antimicrobial activity (in Polish)
    • Gwiazdowska D. and K. Trojanowska. 2005. Bacteriocins - properties and antimicrobial activity (in Polish). Biotechnologia 1: 114-130.
    • (2005) Biotechnologia , vol.1 , pp. 114-130
    • Gwiazdowska, D.1    Trojanowska, K.2
  • 53
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • DOI 10.1016/S0140-6736(97)80051-7
    • Hancock R.E.W. 1997. Peptide antibiotics. Lancet 349: 418-422. (Pubitemid 27077684)
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.W.1
  • 54
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings J.W., M. Sailer, K. Johnson, K.L. Roy, J.C. Vederas and M.E. Stiles. 1991. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173: 7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1    Sailer, M.2    Johnson, K.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 55
    • 0027080504 scopus 로고
    • Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides
    • Héchard Y., B. Dérijard, F. Letellier and Y. Cenatiempo. 1992. Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides. J. Gen. Microbiol. 138(12): 2725-2731. (Pubitemid 23041028)
    • (1992) Journal of General Microbiology , vol.138 , Issue.12 , pp. 2725-2731
    • Hechard, Y.1    Derijard, B.2    Letellier, F.3    Cenatiempo, Y.4
  • 56
    • 38449091969 scopus 로고    scopus 로고
    • Ubericin A, a class IIa bacteriocin produced by Streptococcus uberis
    • Heng N.C., G.A. Burtenshaw, R.W. Jack and J.R. Tagg. 2007. Ubericin A, a class IIa bacteriocin produced by Streptococcus uberis. Appl. Environ. Microbiol. 73: 7763-7766.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7763-7766
    • Heng, N.C.1    Burtenshaw, G.A.2    Jack, R.W.3    Tagg, J.R.4
  • 58
    • 0028217590 scopus 로고
    • Purification and cloning of piscicolin 61, a bacteriocin from Carnobacterium piscicola LV61
    • DOI 10.1007/BF01575750
    • Holck A.L., L. Axelsson and U. Schillinger. 1994. Purification and cloning of piscicolin 61, a bacteriocin from Carnobacterium piscicola LV61. Curr. Microbiol. 29: 63-68. (Pubitemid 24190880)
    • (1994) Current Microbiology , vol.29 , Issue.2 , pp. 63-68
    • Holck, A.L.1    Axelsson, L.2    Schillinger, U.3
  • 59
    • 49849092147 scopus 로고    scopus 로고
    • Description of durancin TW-49M, a novel enterocin B-homologous bacteriocin in carrot-isolated Enterococcus durans QU 49
    • Hu C.B., T. Zendo, J. Nakayama and K. Sonomoto. 2008. Description of durancin TW-49M, a novel enterocin B-homologous bacteriocin in carrot-isolated Enterococcus durans QU 49. J. Appl. Microbiol. 105: 681-690.
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 681-690
    • Hu, C.B.1    Zendo, T.2    Nakayama, J.3    Sonomoto, K.4
  • 60
    • 77954298757 scopus 로고    scopus 로고
    • Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides
    • Hu C.B., W. Malaphan, T. Zendo, J. Nakayama and K. Sonomoto. 2010. Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides. Appl. Environ. Microbiol. 76: 4542-4545.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4542-4545
    • Hu, C.B.1    Malaphan, W.2    Zendo, T.3    Nakayama, J.4    Sonomoto, K.5
  • 61
    • 84880153479 scopus 로고    scopus 로고
    • Characterization and application of enterocin RM6, a bacteriocin from Enterococcus faecalis
    • Article ID 206917
    • Huang E., Z. Liwen, Y.-K. Chung, Z. Zheng and A.E. Yousef.2013. Characterization and application of enterocin RM6, a bacteriocin from Enterococcus faecalis. BioMed. Res. Int. 2013, Article ID 206917.
    • (2013) BioMed. Res. Int. , vol.2013
    • Huang, E.1    Liwen, Z.2    Chung, Y.-K.3    Zheng, Z.4    Yousef, A.E.5
  • 63
    • 67649603187 scopus 로고    scopus 로고
    • Enterocin 96, a novel class II bacteriocin produced by Enterococcus faecalis WHE 96, isolated from Munster cheese
    • Izquierdo E., C. Wagner, E. Marchioni, D. Aoude-Werner andS. Ennahar. 2009. Enterocin 96, a novel class II bacteriocin produced by Enterococcus faecalis WHE 96, isolated from Munster cheese. Appl. Environ. Microbiol. 75: 4273-4276.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4273-4276
    • Izquierdo, E.1    Wagner, C.2    Marchioni, E.3    Aoude-Werner, D.4    Ennahar, S.5
  • 64
    • 0028990155 scopus 로고
    • Bacteriocins of Gram-positive bacteria
    • Jack R.W., J.R. Tagg and B. Ray. 1995. Bacteriocins of Gram-positive bacteria. Microbiol. Rev. 59: 171-200.
    • (1995) Microbiol. Rev. , vol.59 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 65
    • 0022465775 scopus 로고
    • Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481
    • Joerger M.C. and T.R. Klaenhammer. 1986. Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481.J. Bacteriol. 167: 439-446. (Pubitemid 16049953)
    • (1986) Journal of Bacteriology , vol.167 , Issue.2 , pp. 439-446
    • Joerger, M.C.1    Klaenhammer, T.R.2
  • 66
    • 84882741189 scopus 로고    scopus 로고
    • Nisin, an apoptogenic bacteriocin and food preservative, attenuates HNSCC tumorigenesis via CHAC1
    • Joo N.E., K. Ritchie, P. Kamarajan, D. Miao and Y.L. Kapila. 2012. Nisin, an apoptogenic bacteriocin and food preservative, attenuates HNSCC tumorigenesis via CHAC1. Cancer Med. 1: 295-305.
    • (2012) Cancer Med. , vol.1 , pp. 295-305
    • Joo, N.E.1    Ritchie, K.2    Kamarajan, P.3    Miao, D.4    Kapila, Y.L.5
  • 68
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer T.R. 1993. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12: 39-86.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-86
    • Klaenhammer, T.R.1
  • 69
    • 84855647326 scopus 로고    scopus 로고
    • Changes in gut microbiota in children with atopic dermatitis administered the bacteria Lactobacillus casei DN-114001
    • Klewicka E., B. Cukrowska, Z. Libudzisz, K. Slizewska andI. Motyl. 2011. Changes in gut microbiota in children with atopic dermatitis administered the bacteria Lactobacillus casei DN-114001. Pol. J. Microbiol. 60: 329-333.
    • (2011) Pol. J. Microbiol. , vol.60 , pp. 329-333
    • Klewicka, E.1    Cukrowska, B.2    Libudzisz, Z.3    Slizewska, K.4    Motyl, I.5
  • 70
    • 0026663308 scopus 로고
    • Genetics of ribosomally synthesized peptide antibiotics
    • Kolter R. and F. Moreno. 1992. Genetics of ribosomally synthesized peptide antibiotics. Annu. Rev. Microbiol. 46: 141-163.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 141-163
    • Kolter, R.1    Moreno, F.2
  • 71
    • 4644313503 scopus 로고    scopus 로고
    • Mersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model
    • DOI 10.1093/jac/dkh387
    • Kruszewska D., H.G. Sahl, G. Bierbaum, U. Pag, S.O. Hynes and A. Ljungh. 2004. Mersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model. J. Antimicrob. Chemother. 54: 648-653. (Pubitemid 39263907)
    • (2004) Journal of Antimicrobial Chemotherapy , vol.54 , Issue.3 , pp. 648-653
    • Kruszewska, D.1    Sahl, H.-G.2    Bierbaum, G.3    Pag, U.4    Hynes, S.O.5    Ljungh, A.6
  • 73
    • 0027533645 scopus 로고
    • Microcin E492 forms ion channels in phospholipid bilayer membranes
    • DOI 10.1016/0014-5793(93)80096-D
    • Lagos R., M. Wilkens, C. Vergara, X. Cecchi and O. Monasterio. 1993. Microcin E492 forms ion channels in phospholipid bilayer membrane. FEBS Lett. 321: 145-148. (Pubitemid 23114065)
    • (1993) FEBS Letters , vol.321 , Issue.2-3 , pp. 145-148
    • Lagos, R.1    Wilkens, M.2    Vergara, C.3    Cecchi, X.4    Monasterio, O.5
  • 74
    • 0021771497 scopus 로고
    • Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3
    • Lau P.C.K., R.W. Rowsome, M. Zuker and L.P. Visentin. 1984. Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3. Nucleic Acids Res. 12: 8733-8745.
    • (1984) Nucleic Acids Res , vol.12 , pp. 8733-8745
    • Lau, P.C.K.1    Rowsome, R.W.2    Zuker, M.3    Visentin, L.P.4
  • 75
    • 84874559681 scopus 로고    scopus 로고
    • Antimicrobial effect of bacteriocin KU24 produced by Lactococcus lactis KU24 against methicillin-resistant Staphylococcus aureus
    • Lee N.-K., E.J. Han, K.J. Han, and H.-D. Paik. 2013. Antimicrobial effect of bacteriocin KU24 produced by Lactococcus lactis KU24 against methicillin-resistant Staphylococcus aureus. J. Food Sci. 78: M465-M469.
    • (2013) J. Food Sci. , vol.78
    • Lee, N.-K.1    Han, E.J.2    Han, K.J.3    Paik, H.-D.4
  • 76
    • 0029121699 scopus 로고
    • Genetic analysis of acidocin B, a novel bacteriocin produced by Lactobacillus acidophilus
    • Leer R.J., J.M.B.M. van der Vossen, M. van Giezen, J.M. van Noort and P.H. Pouwels. 1995. Genetic analysis of acidocin B, a novel bacteriocin produced by Lactobacillus acidophilus. Microbiol. 141: 1629-1635.
    • (1995) Microbiol. , vol.141 , pp. 1629-1635
    • Leer, R.J.1    Van Dervossen, M.B.J.M.2    Van Giezen, M.3    Van Noort, J.M.4    Pouwels, P.H.5
  • 78
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Lozano J.C.N., J.N. Meyer, K. Sletten, C. Peláz and I.F. Nes. 1992. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 138: 1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Lozano, J.C.N.1    Meyer, J.N.2    Sletten, K.3    Peláz, C.4    Nes, I.F.5
  • 79
    • 0027395666 scopus 로고
    • Isolation and purification of propionicin PLG-1, a bacteriocin produced by a strain of Propionibacterium thoenii
    • Lyon W.J. and B.A. Glatz. 1993. Isolation and purification of propionicin PLG-1, a bacteriocin produced by a strain of Propionibacterium thoenii. Appl. Environ. Microbiol. 59: 83-88. (Pubitemid 23028371)
    • (1993) Applied and Environmental Microbiology , vol.59 , Issue.1 , pp. 83-88
    • Lyon, W.J.1    Glatz, B.A.2
  • 80
    • 0030921926 scopus 로고    scopus 로고
    • Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor
    • DOI 10.1074/jbc.272.22.14277
    • Marciset O., M.C. Jeronimus-Stratingh, B. Mollet and B. Poolman. 1997. Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor. J. Biol. Chem. 272: 14277-14284. (Pubitemid 27232841)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14277-14284
    • Marciset, O.1    Jeronimus-Stratingh, M.C.2    Mollet, B.3    Poolman, B.4
  • 81
    • 0026091089 scopus 로고
    • Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2
    • Marki F., E. Hanni, A. Fredenhagen and J. Oostrum. 1991. Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2. Biochem. Pharmacol. 42: 2027-2035.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 2027-2035
    • Marki, F.1    Hanni, E.2    Fredenhagen, A.3    Oostrum, J.4
  • 82
    • 0035004672 scopus 로고    scopus 로고
    • Lantibiotics: Structure, biosynthesis and mode of action
    • DOI 10.1016/S0168-6445(00)00065-6, PII S0168644500000656
    • McAuliffe O., R.P. Ross and C. Hill. 2001. Lantibiotics: structure, biosynthesis and mode of action. FEMS Microbiol. Rev. 25: 285-308. (Pubitemid 32429585)
    • (2001) FEMS Microbiology Reviews , vol.25 , Issue.3 , pp. 285-308
    • McAuliffe, O.1    Ross, R.P.2    Hill, C.3
  • 84
    • 0030744235 scopus 로고    scopus 로고
    • Purification and structure of mutacin B-Ny266: A new lantibiotic produced by Streptococcus mutans
    • DOI 10.1016/S0014-5793(97)00425-0, PII S0014579397004250
    • Mota-Meira M., C. Lacroix, G. LaPointe and M.C. Lavoie. 1997. Purification and structure of mutacin B-Ny266: a new lantibiotic produced by Streptococcus mutans. FEBS Lett. 410: 275-279. (Pubitemid 27304078)
    • (1997) FEBS Letters , vol.410 , Issue.2-3 , pp. 275-279
    • Mota-Meira, M.1    Lacroix, C.2    Lapointe, G.3    Lavoie, M.C.4
  • 85
    • 0033988560 scopus 로고    scopus 로고
    • MICs of mutacin B-Ny266, nisin A, vancomycin, and oxacillin against bacterial pathogens
    • Mota-Meira M., G. LaPointe, C. Lacroix and M.C. Lavoie. 2000. MICs of mutacin B-Ny266, nisin A, vancomycin, and oxacillin against bacterial pathogens. Antimicrob. Agents Chemother. 44: 24-29. (Pubitemid 30010667)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.1 , pp. 24-29
    • Mota-Meira, M.1    LaPointe, G.2    Lacroix, C.3    Lavoie, M.C.4
  • 86
    • 0026062942 scopus 로고
    • Identification and characterization of the lantibiotic nisin Z, a natural nisin variant
    • Mulders J.W., I.J. Boerrigter, H.S. Rollema, R.J. Siezen andW.M. de Vos. 1991. Identification and characterization of the lantibiotic nisin Z, a natural nisin variant. Eur. J. Biochem. 201: 581-584.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 581-584
    • Mulders, J.W.1    Boerrigter, I.J.2    Rollema, H.S.3    Siezen, R.J.4    De Vos, W.M.5
  • 87
    • 33846913393 scopus 로고    scopus 로고
    • Bacteriocin diversity in Streptococcus and Enterococcus
    • DOI 10.1128/JB.01254-06
    • Nes I.F., D.B. Diep and H. Holo. 2007. Bacteriocin diversity in Streptococcus and Enterococcus. J. Bacteriol. 189: 1189-1198. (Pubitemid 46239740)
    • (2007) Journal of Bacteriology , vol.189 , Issue.4 , pp. 1189-1198
    • Nes, I.F.1    Diep, D.B.2    Holo, H.3
  • 88
    • 0037882258 scopus 로고    scopus 로고
    • Enterolysin A, a cell wall-degrading bacteriocin from Enterococcus faecalis LMG 2333
    • DOI 10.1128/AEM.69.5.2975-2984.2003
    • Nilsen T., F.N. Ingolf and H. Holo. 2003. Enterolysin A, a cell wall-degrading bacteriocin from Enterococcus faecalis LMG 2333. Appl. Environ. Microbiol. 69: 2975-2984. (Pubitemid 36560382)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.5 , pp. 2975-2984
    • Nilsen, T.1    Nes, I.F.2    Holo, H.3
  • 89
    • 84858841767 scopus 로고    scopus 로고
    • Antibacterial peptides "bacteriocins": An overview of their diverse characteristics and applications
    • Nishie M., J. Nagao and K. Sonomoto. 2012. Antibacterial peptides "bacteriocins": an overview of their diverse characteristics and applications. Biocontrol Sci. 17: 1-16.
    • (2012) Biocontrol Sci , vol.17 , pp. 1-16
    • Nishie, M.1    Nagao, J.2    Sonomoto, K.3
  • 90
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer J., H. Holo, L.S. Håvarstein, K. Sletten and I.F. Nes. 1992. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J. Bacteriol. 174: 5686-5692.
    • (1992) J. Bacteriol. , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Håvarstein, L.S.3    Sletten, K.4    Nes, I.F.5
  • 91
    • 65149100197 scopus 로고    scopus 로고
    • Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by Gram-positive bacteria
    • Nissen-Meyer J., P. Rogne, C. Oppegård, H.S. Haugen andP.E. Kristiansen. 2009. Structure-function relationships of the non-lanthionine- containing peptide (class II) bacteriocins produced by Gram-positive bacteria. Curr. Pharm. Biotechnol. 10: 19-37.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 19-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegård, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 92
    • 0023626122 scopus 로고
    • Sequence, expression, a localization of the immunity protein for colicin M
    • Olschläger T. and V. Braun. 1987. Sequence, expression, and localization of the immunity protein for colicin M. J. Bacteriol. 169: 4765-4769. (Pubitemid 18052236)
    • (1987) Journal of Bacteriology , vol.169 , Issue.10 , pp. 4765-4769
    • Olschlager, T.1    Braun, V.2
  • 94
    • 0033850623 scopus 로고    scopus 로고
    • Characterization and mechanism of action of cerein 7, a bacteriocin produced by Bacillus cereus Bc7
    • Oscáriz J.C. and A.G. Pisabarro. 2000. Characterization and mechanism of action of cerein 7, a bacteriocin produced by Bacillus cereus Bc7. J. Appl. Microbiol. 89: 361-369.
    • (2000) J. Appl. Microbiol. , vol.89 , pp. 361-369
    • Oscáriz, J.C.1    Pisabarro, A.G.2
  • 95
    • 0034527346 scopus 로고    scopus 로고
    • Probiotics: A review of human studies to date and methodological approaches
    • DOI 10.1080/089106000750060251
    • Pathmakanthan S., S. Meance and C.A. Edwards. 2000. Probiotics: A review of human studies to date and methodological approaches. Microb. Ecol. Health Dis. 12(suppl. 2): 10-30. (Pubitemid 32056919)
    • (2000) Microbial Ecology in Health and Disease , vol.12 , Issue.SUPPL. 2 , pp. 10-30
    • Pathmakanthan, S.1    Meance, S.2    Edwards, C.A.3
  • 96
    • 0001586791 scopus 로고
    • Inhibiting factors produced by lactic acid bacteria. 2. Bacteriocins and other antibacterial substances
    • Piard J.C. and M. Desmazeaud. 1992. Inhibiting factors produced by lactic acid bacteria. 2. Bacteriocins and other antibacterial substances. Lait. 72: 113-142.
    • (1992) Lait , vol.72 , pp. 113-142
    • Piard, J.C.1    Desmazeaud, M.2
  • 97
    • 0036589246 scopus 로고    scopus 로고
    • New developments in non-post translationally modified microcins
    • DOI 10.1016/S0300-9084(02)01416-5, PII S0300908402014165
    • Pons A.M., I. Lanneluc, G. Cottencau and S. Sable. 2002. New developments in non-post translationally modified microcins. Biochimie. 84: 531-537. (Pubitemid 35350884)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 531-537
    • Pons, A.-M.1    Lanneluc, I.2    Cottenceau, G.3    Sable, S.4
  • 98
    • 0033305858 scopus 로고    scopus 로고
    • Inhibition of pathogenic Salmonella enteritidis growth mediated by Escherichia coli microcin J25 producing strains
    • Portrait V., S. Gendron-Gaillard, G. Cottenceau and AM. Pons. 1999. Inhibition of pathogenic Salmonella enteritidis growth mediated by Escherichia coli microcin J25 producing strains. Can. J. Microbiol. 45: 168-175.
    • (1999) Can. J. Microbiol. , vol.45 , pp. 168-175
    • Portrait, V.1    Gendron-Gaillard, S.2    Cottenceau, G.3    Pons, A.M.4
  • 100
    • 0029055617 scopus 로고
    • The role of lactic acid bacteria in colon cancer prevention
    • Rafter J. 1995. The role of lactic acid bacteria in colon cancer prevention. Scand. J. Gastroenterol. 30: 497-502.
    • (1995) Scand. J. Gastroenterol. , vol.30 , pp. 497-502
    • Rafter, J.1
  • 101
    • 0033105191 scopus 로고    scopus 로고
    • The ecological role of bacteriocins in bacterial competition
    • DOI 10.1016/S0966-842X(99)01459-6, PII S0966842X99014596
    • Riley M.A. and D.M. Gordon. 1999. The ecological role of bacteriocins in bacterial competition. Trends Microbiol. 7: 129-133. (Pubitemid 29272001)
    • (1999) Trends in Microbiology , vol.7 , Issue.3 , pp. 129-133
    • Riley, M.A.1    Gordon, D.M.2
  • 102
    • 0035856589 scopus 로고    scopus 로고
    • The antibacterial action of microcin J25: Evidence for disruption of cytoplasmic membrane energization in Salmonella newport
    • DOI 10.1016/S0378-1097(01)00416-5, PII S0378109701004165
    • Rintoul M.R., B.F. de Arcuri, R.A. Salomon, R.N. Farias andR.D. Morero. 2001. The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport. FEMS Microbiol. Lett. 204: 265-270. (Pubitemid 33145264)
    • (2001) FEMS Microbiology Letters , vol.204 , Issue.2 , pp. 265-270
    • Rintoul, M.R.1    De Arcuri, B.F.2    Salomon, R.A.3    Farias, R.N.4    Morero, R.D.5
  • 103
    • 0344562871 scopus 로고    scopus 로고
    • The structural gene for microcin H47 encodes a peptide precursor with antibiotic activity
    • Rodríguez E., C. Gaggero and M. Lavina. 1999. The structural gene for microcin H47 encodes a peptide precursor with antibiotic activity. Antimicrob. Agents Chemother. 43: 2176-2182. (Pubitemid 29421197)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.9 , pp. 2176-2182
    • Rodriguez, E.1    Gaggero, C.2    Lavina, M.3
  • 104
    • 0036222084 scopus 로고    scopus 로고
    • Pediocin PA-1,a wide-spectrum bacteriocin from lactic acid bacteria
    • Rodriguez J.M., M.I. Martinez and J. Kok. 2002. Pediocin PA-1,a wide-spectrum bacteriocin from lactic acid bacteria. Crit. Rev. Food Sci. Nutr. 42: 91-121.
    • (2002) Crit. Rev. Food Sci. Nutr. , vol.42 , pp. 91-121
    • Rodriguez, J.M.1    Martinez, M.I.2    Kok, J.3
  • 105
    • 0033972717 scopus 로고    scopus 로고
    • The role of probiotic cultures in the control of gastrointestinal health
    • Rolfe R.D. 2000. The role of probiotic cultures in the control of gastrointestinal health. J. Nutr. 130: 396S-402S. (Pubitemid 30073758)
    • (2000) Journal of Nutrition , vol.130 , Issue.2 SUPPL.
    • Rolfe, R.D.1
  • 106
    • 0027279657 scopus 로고
    • Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3
    • Ross K.F., C.W. Ronson and J.R. 1993. Tagg. Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3. Appl. Environ. Microbiol. 59: 2014-2021. (Pubitemid 23205782)
    • (1993) Applied and Environmental Microbiology , vol.59 , Issue.7 , pp. 2014-2021
    • Ross, K.F.1    Ronson, C.W.2    Tagg, J.R.3
  • 107
  • 108
    • 0026526445 scopus 로고
    • Microcin 25, a novel antimicrobial peptide produced by Escherichia coli
    • Salomón R.A. and R.N. Farías. 1992. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J. Bacteriol. 174: 7428-7435.
    • (1992) J. Bacteriol. , vol.174 , pp. 7428-7435
    • Salomón, R.A.1    Farías, R.N.2
  • 109
    • 34247098486 scopus 로고    scopus 로고
    • Amino acid and nucleotide sequence, adjacent genes, and heterologous expression of hiracin JM79, a sec-dependent bacteriocin produced by Enterococcus hirae DCH5, isolated from Mallard ducks (Anas platyrhynchos)
    • DOI 10.1111/j.1574-6968.2007.00673.x
    • Sánchez J., D.B. Diep, C. Herranz, I.F. Nes, L.M. Cintas andP.E. Hernández. 2007. Amino acid and nucleotide sequence, adjacent genes, and heterologous expression of hirancin JM79,a sec-dependent bacteriocin produced by Enterococcus hirae DCH5, isolated from Mallard ducks (Anas platyrhynchos). FEMS Microbiol. Lett. 270: 227-236. (Pubitemid 46597361)
    • (2007) FEMS Microbiology Letters , vol.270 , Issue.2 , pp. 227-236
    • Sanchez, J.1    Diep, D.B.2    Herranz, C.3    Nes, I.F.4    Cintas, L.M.5    Hernandez, P.E.6
  • 112
    • 34748829707 scopus 로고    scopus 로고
    • The bacterial peptide pheromone plantaricin A permeabilizes cancerous, but not normal, rat pituitary cells and differentiates between the outer and inner membrane leaflet
    • DOI 10.1007/s00232-007-9030-3
    • Sand S.L., T.M. Haug, J. Nissen-Meyer and O. Sand. 2007. The bacterial peptide pheromone plantaricin A permeabilizes cancerous, but not normal, rat pituitary cells and differentiates between the outer and inner membrane leaflet. J. Membr. Biol. 216: 61-71. (Pubitemid 47479550)
    • (2007) Journal of Membrane Biology , vol.216 , Issue.2-3 , pp. 61-71
    • Sand, S.L.1    Haug, T.M.2    Nissen-Meyer, J.3    Sand, O.4
  • 113
    • 0033969143 scopus 로고    scopus 로고
    • Considerations for use of probiotic bacteria to modulate human health
    • Sanders M.E. 2000. Consideration for use of probiotic bacteria to modulate human health. J. Nutr. 130: 384S-390S. (Pubitemid 30073756)
    • (2000) Journal of Nutrition , vol.130 , Issue.2 SUPPL.
    • Sanders, M.E.1
  • 115
    • 0000284412 scopus 로고    scopus 로고
    • Potential of antagonistic microorganisms and bacteriocins for the biological preservation of foods
    • Schillinger U., R. Geigen and W.H. Holzapfel. 1996. Potential of antagonistic microorganisms and bacteriocins for the biological preservation of foods. Trends Food Sci. Technol. 7: 158-164. (Pubitemid 126663486)
    • (1996) Trends in Food Science and Technology , vol.7 , Issue.5 , pp. 158-164
    • Schillinger, U.1    Geisen, R.2    Holzapfel, W.H.3
  • 116
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • Schramm E., J. Mende, V. Braun and R.M. Kamp. 1987. Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J. Bacteriol. 169: 3350-3357. (Pubitemid 17106365)
    • (1987) Journal of Bacteriology , vol.169 , Issue.7 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 118
    • 77954806445 scopus 로고    scopus 로고
    • Bacteriocins of probiotic rods of the Lactobacillus genus (in Polish)
    • Słońska A. and D. Klimuszko. 2010. Bacteriocins of probiotic rods of the Lactobacillus genus (in Polish). Post. Mikrobiol. 40: 87-96.
    • (2010) Post. Mikrobiol. , vol.40 , pp. 87-96
    • Słońska, A.1    Klimuszko, D.2
  • 119
    • 0030789223 scopus 로고    scopus 로고
    • Colicin U, a novel colicin produced by Shigella boydii
    • Šmajs D., H. Pilsl and V. Braun. 1997. Colicin U, a novel colicin produced by Shigella boydii. J. Bacteriol. 179: 4919-4928. (Pubitemid 27339741)
    • (1997) Journal of Bacteriology , vol.179 , Issue.15 , pp. 4919-4928
    • Smajs, D.1    Pilsl, H.2    Braun, V.3
  • 120
    • 0032249313 scopus 로고    scopus 로고
    • Colicins - Exocellular Lethal Proteins of Escherichia coli
    • Šmarda J. and D. Šmajs. 1998. Colicins - exocellular lethal proteins of Escherichia coli. Folia Microbiol. 43: 563-582. (Pubitemid 128441327)
    • (1998) Folia Microbiologica , vol.43 , Issue.6 , pp. 563-582
    • Smarda, J.1    Smajs, D.2
  • 121
    • 77749340962 scopus 로고    scopus 로고
    • Technology innovations as a factor of food safety (in Polish)
    • Steinka I. 2009. Technology innovations as a factor of food safety (in Polish). Ann. Acad. Med. Gedan. 39: 123-132.
    • (2009) Ann. Acad. Med. Gedan. , vol.39 , pp. 123-132
    • Steinka, I.1
  • 122
    • 84856844948 scopus 로고    scopus 로고
    • Lactobacillus spp. of oral cavity microflora in chronic periodontitis
    • Szkaradkiewicz A.K. and J. Stopa. 2008. Lactobacillus spp. of oral cavity microflora in chronic periodontitis. Pol. J. Environ. Stud. 17: 236-242.
    • (2008) Pol. J. Environ. Stud. , vol.17 , pp. 236-242
    • Szkaradkiewicz, A.K.1    Stopa, J.2
  • 125
    • 0030970757 scopus 로고    scopus 로고
    • Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Stphylococcus simulans biovar staphylolyticus
    • DOI 10.1046/j.1365-2958.1997.2911657.x
    • Thumm G. and F. Gotz. 1997. Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus. Mol. Microbiol. 23: 1251-1265. (Pubitemid 27122210)
    • (1997) Molecular Microbiology , vol.23 , Issue.6 , pp. 1251-1265
    • Thumm, G.1    Gotz, F.2
  • 126
    • 0027326620 scopus 로고
    • Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174
    • Tichaczek P.S., R.F. Vogel and W.P. Hammes. 1993. Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174. Arch. Microbiol. 160: 279-283. (Pubitemid 23277986)
    • (1993) Archives of Microbiology , vol.160 , Issue.4 , pp. 279-283
    • Tichaczek, P.S.1    Vogel, R.F.2    Hammes, W.P.3
  • 127
    • 0023897935 scopus 로고
    • Colicin E8, a DNase which indicates an evolutionary relationship between colicins E2 and E3
    • Toba M., H. Masaki and T. Ohta. 1988. Colicin E8, a DNase which indicates an evolutionary relationship between colicins E2 and E3. J. Bacteriol. 170: 3237-3242.
    • (1988) J. Bacteriol. , vol.170 , pp. 3237-3242
    • Toba, M.1    Masaki, H.2    Ohta, T.3
  • 128
    • 0033963661 scopus 로고    scopus 로고
    • A pAD1-encoded small RNA molecule, mD, negatively regulates Enterococcus faecalis pheromone response by enhancing transcription termination
    • DOI 10.1128/JB.182.4.1062-1073.2000
    • Tomita H. and D.B. Clewell. 2000. A pAD1-encoded small RNA molecule, mD, negatively regulates Enterococcus faecalis pheromone response by enhancing transcription termination. J. Bacteriol. 182: 1062-1073. (Pubitemid 30075030)
    • (2000) Journal of Bacteriology , vol.182 , Issue.4 , pp. 1062-1073
    • Tomita, H.1    Clewell, D.B.2
  • 129
    • 40449084234 scopus 로고    scopus 로고
    • Cloning and genetic analyses of the bacteriocin 41 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI14: A novel bacteriocin complemented by two extracellular components (lysin and activator)
    • DOI 10.1128/JB.01056-07
    • Tomita H., E. Kamei and Y. Ike. 2008. Cloning and genetic analyses of the bacteriocin 41 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI14: a novel bacteriocin complemented by two extracellular components (lysin and activator) J. Bacteriol. 190: 2075-2085. (Pubitemid 351355331)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2075-2085
    • Tomita, H.1    Kamei, E.2    Ike, Y.3
  • 130
    • 0023430037 scopus 로고
    • Nucleotide sequences from the colicin E8 operon: Homology with plasmid ColE2-P9
    • Uchimura T. and P.C.K. Lau. 1987. Nucleotide sequences from the colicin E8 operon: homology with plasmid ColE2-P9. Mol. Gen. Genet. 209: 489-493.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 489-493
    • Uchimura, T.1    Lau, P.C.K.2
  • 132
    • 0033859263 scopus 로고    scopus 로고
    • Nonlantibiotic antimicrobial peptides from lactic acid bacteria
    • van Belkum M.J. and M.E. Stiles. 2000. Nonlantibiotic antimicrobial peptides from lactic acid bacteria. Nat. Prod. Rep. 17: 323-365.
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 323-365
    • Van Belkum, M.J.1    Stiles, M.E.2
  • 135
    • 0029972106 scopus 로고    scopus 로고
    • Control of Listeria monocytogenes in ground beef by 'Lactocin 705', a bacteriocin produced by Lactobacillus casei CRL 705
    • Vignolo G., S. Fadda, M.N. de Kairuz, A.A. de Ruiz Holgado and G. Oliver. 1996. Control of Listeria monocytogenes in ground beef by 'Lactocin 705', a bacteriocin produced by Lactobacillus casei CRL 705. Int. J. Food Microbiol. 29: 397-402.
    • (1996) Int. J. Food Microbiol. , vol.29 , pp. 397-402
    • Vignolo, G.1    Fadda, S.2    De Kairuz, M.N.3    De Holgado Ruiz, A.A.4    Oliver, G.5
  • 136
    • 79952574817 scopus 로고    scopus 로고
    • Purifcation, characterization and in vitro cytotoxicity of the bacteriocin from Pediococcus acidilactici K2a2-3 against human colon adenocarcinoma (HT29) and human cervical carcinoma (HeLa) cells
    • Villarante K.I., F.B. Elegado, S. Iwatani, T. Zendo, K. Sonomoto and E.E. de Guzman. 2011. Purifcation, characterization and in vitro cytotoxicity of the bacteriocin from Pediococcus acidilactici K2a2-3 against human colon adenocarcinoma (HT29) and human cervical carcinoma (HeLa) cells. World J. Microbiol. Biotechnol. 27: 975-980.
    • (2011) World J. Microbiol. Biotechnol. , vol.27 , pp. 975-980
    • Villarante, K.I.1    Elegado, F.B.2    Iwatani, S.3    Zendo, T.4    Sonomoto, K.5    De Guzman, E.E.6
  • 137
    • 0025964113 scopus 로고
    • The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. Coli DNA gyrase
    • Vizán J.L., C. Hernández-Chico, I. del Castillo and F. Moreno. 1991. The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase. EMBO J. 10: 467-476. (Pubitemid 21905498)
    • (1991) EMBO Journal , vol.10 , Issue.2 , pp. 467-476
    • Vizan, J.L.1    Hernandez-Chico, C.2    Del Castillo, I.3    Moreno, F.4
  • 138
    • 0026598420 scopus 로고
    • Effect of subinhibitory concentrations of antibiotics on extracellular Shiga-like toxin i
    • Walterspiel J.N., S. Ashkenazi, A.L. Morrowand and T.G. Cleary. 1992. Effect of subinhibitory concentrations of antibiotics on extracellular Shiga-like toxin I. Infect. Immun. 20: 25-29.
    • (1992) Infect. Immun. , vol.20 , pp. 25-29
    • Walterspiel, J.N.1    Ashkenazi, S.2    Morrowand, A.L.3    Cleary, T.G.4
  • 140
    • 34249068328 scopus 로고    scopus 로고
    • Uberolysin: A novel cyclic bacteriocin produced by Streptococcus uberis
    • DOI 10.1099/mic.0.2006/005967-0
    • Wirawan R.E., K.M. Swanson, T. Kleffmann, R.W. Jack andJ.R. Tagg. 2007. Uberolysin: a novel cyclic bacteriocin produced by Streptococcus uberis. Microbiol. 153: 1619-1630. (Pubitemid 46780017)
    • (2007) Microbiology , vol.153 , Issue.5 , pp. 1619-1630
    • Wirawan, R.E.1    Swanson, K.M.2    Kleffmann, T.3    Jack, R.W.4    Tagg, J.R.5
  • 141
    • 33144466523 scopus 로고    scopus 로고
    • Molecular and genetic characterization of a novel nisin variant produced by Streptococcus uberis
    • DOI 10.1128/AEM.72.2.1148-1156.2006
    • Wirawan R.E., N.A. Klesse, R.W. Jack and J.R. Tagg. 2006.Molecular and genetic characterization of a novel nisin variant produced by Streptococcus uberis. Appl. Environ. Microbiol. 72: 1148-1156. (Pubitemid 43271221)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.2 , pp. 1148-1156
    • Wirawan, R.E.1    Klesse, N.A.2    Jack, R.W.3    Tagg, J.R.4
  • 142
    • 14644440934 scopus 로고    scopus 로고
    • Phenotypic diversity of bacteria encoded by plasmids
    • (in Polish)
    • Włodarczyk M. 2002. Phenotypic diversity of bacteria encoded by plasmids (in Polish). Kosmos. 51: 241-254.
    • (2002) Kosmos , vol.51 , pp. 241-254
    • Włodarczyk, M.1
  • 143
    • 84865732323 scopus 로고    scopus 로고
    • Synergy between novel antimicrobials and conventional antibiotics or bacteriocins
    • Wolska K.I., K. Grześ and A. Kurek. 2012. Synergy between novel antimicrobials and conventional antibiotics or bacteriocins. Pol.J. Microbiol. 61: 95-104.
    • (2012) Pol.J. Microbiol. , vol.61 , pp. 95-104
    • Wolska, K.I.1    Grześ, K.2    Kurek, A.3
  • 144
    • 0028324911 scopus 로고
    • Characteristics and genetic determinant of a hydrophobic peptide bacteriocin, carnobacteriocin A, produced by Carnobacterium piscicola LV17A
    • Worobo R.W., T. Henkel, M. Sailer, K.L. Roy, J.C. Vederas and M.E. Stiles. 1994. Characteristics and genetic determinant of a hydrophobic peptide bacteriocin, carnobacteriocin A, produced by Carnobacterium piscicola LV17A. Microbiology. 140: 517-526. (Pubitemid 24090620)
    • (1994) Microbiology , vol.140 , Issue.3 , pp. 517-526
    • Worobo, R.W.1    Henkel, T.2    Sailer, M.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.