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Volumn 16, Issue 5, 2007, Pages 675-690

Ribosomally synthesiszed antimicrobial peptides (bacteriocins) in lactic acid bacteria: A review

Author keywords

Bacteriocin; Classification; Gene regulation; Lactic acid bacteria; Modes of action

Indexed keywords

BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 45749122840     PISSN: 12267708     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (113)

References (199)
  • 1
    • 0034666527 scopus 로고    scopus 로고
    • Action of lysozyme and nisin mixtures against lactic acid bacteria
    • Chun W, Hancock RE. Action of lysozyme and nisin mixtures against lactic acid bacteria. Int. J. Food Microbiol. 60: 25-32 (2000)
    • (2000) Int. J. Food Microbiol , vol.60 , pp. 25-32
    • Chun, W.1    Hancock, R.E.2
  • 2
    • 0028210224 scopus 로고    scopus 로고
    • Schved F, Henis Y, Juven BJ. Response of spheroplasts and chelator-permeabilized cells of Gram-negative bacteria to the actionof the bacteriocins pediocin SJ-1 and nisin. Inc. J. Food Microbiol. 21: 305-314 (1994)
    • Schved F, Henis Y, Juven BJ. Response of spheroplasts and chelator-permeabilized cells of Gram-negative bacteria to the actionof the bacteriocins pediocin SJ-1 and nisin. Inc. J. Food Microbiol. 21: 305-314 (1994)
  • 3
    • 0024566355 scopus 로고
    • Bactericidal and bacteriolytic action of peptide antibiotic AS-48 against Grampositive and Gram-negative bacteria and other organisms
    • Galvez A, Maqueda M, Martinez-Bueno M, Valdivia E. Bactericidal and bacteriolytic action of peptide antibiotic AS-48 against Grampositive and Gram-negative bacteria and other organisms. Res. Microbiol. 140: 57-68 (1989)
    • (1989) Res. Microbiol , vol.140 , pp. 57-68
    • Galvez, A.1    Maqueda, M.2    Martinez-Bueno, M.3    Valdivia, E.4
  • 4
    • 17644433467 scopus 로고    scopus 로고
    • Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria
    • Luders T, BirkemoGA, Fimland G, Nissen-Meyer J, Nes IF. Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria. Appl. Environ. Microb. 69: 1797-1799 (2003)
    • (2003) Appl. Environ. Microb , vol.69 , pp. 1797-1799
    • Luders, T.1    Birkemo, G.A.2    Fimland, G.3    Nissen-Meyer, J.4    Nes, I.F.5
  • 5
    • 0020350235 scopus 로고    scopus 로고
    • Konisky J. Colicins and other bacteriocins with established modes of action. Ann. Rev. Microbiol. 36: 125-144 (1982)
    • Konisky J. Colicins and other bacteriocins with established modes of action. Ann. Rev. Microbiol. 36: 125-144 (1982)
  • 6
    • 42149190914 scopus 로고    scopus 로고
    • Effect of encapsulated bacteriocin on acid production and growth of starter cultures in yoghurt
    • Oh SJ, Heo HJ, Park DJ, Kim SH, Lee SJ, Imm JY. Effect of encapsulated bacteriocin on acid production and growth of starter cultures in yoghurt. Food Sci. Biotechnol. 15: 902-907 (2006)
    • (2006) Food Sci. Biotechnol , vol.15 , pp. 902-907
    • Oh, S.J.1    Heo, H.J.2    Park, D.J.3    Kim, S.H.4    Lee, S.J.5    Imm, J.Y.6
  • 7
    • 49749106457 scopus 로고    scopus 로고
    • Characterization of bacteriocin produced by Enterococcus faecium MJ-14 Isolated from meju
    • Lim SM, Park MY, Chang DS. Characterization of bacteriocin produced by Enterococcus faecium MJ-14 Isolated from meju. Food Sci. Biotechnol. 14: 49-57 (2005)
    • (2005) Food Sci. Biotechnol , vol.14 , pp. 49-57
    • Lim, S.M.1    Park, M.Y.2    Chang, D.S.3
  • 8
    • 49749115052 scopus 로고    scopus 로고
    • Optimized production of lacticin NK24, a bacteriocin produced by Lactococcus lactis NK24 isolated from jeotgal
    • Lee NK, Kim KT, Kim CJ, Paik HD. Optimized production of lacticin NK24, a bacteriocin produced by Lactococcus lactis NK24 isolated from jeotgal. Food Sci. Biotechnol. 13: 6-10 (2004)
    • (2004) Food Sci. Biotechnol , vol.13 , pp. 6-10
    • Lee, N.K.1    Kim, K.T.2    Kim, C.J.3    Paik, H.D.4
  • 9
    • 0026663308 scopus 로고
    • Genetics of ribosomally synthesized peptide antibiotics
    • Kolter R, Moreno F. Genetics of ribosomally synthesized peptide antibiotics. Ann. Rev. Microbiol. 46: 141-163 (1992)
    • (1992) Ann. Rev. Microbiol , vol.46 , pp. 141-163
    • Kolter, R.1    Moreno, F.2
  • 10
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter PD, Hill C, Ross RP. Bacteriocins: Developing innate immunity for food. Nat. Rev. Microbiol. 3: 777-788 (2005)
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 11
    • 35448980542 scopus 로고    scopus 로고
    • Lanli biotics
    • Handbook of Biological Active Peptides. Academic Press, San Diego, CA, USA 2006
    • Bonelli RG, Wiedemann I, Sahl HG. Lanli biotics. pp. 97-105. In: Handbook of Biological Active Peptides. Academic Press, San Diego, CA, USA (2006)
    • Bonelli, R.G.1    Wiedemann, I.2    Sahl, H.G.3
  • 12
    • 33748490494 scopus 로고    scopus 로고
    • A lesson in efficient killing from two-component lantibiotics
    • Breukink E. A lesson in efficient killing from two-component lantibiotics. Mol. Microbiol. 61: 271-273 (2006)
    • (2006) Mol. Microbiol , vol.61 , pp. 271-273
    • Breukink, E.1
  • 15
    • 33846863326 scopus 로고    scopus 로고
    • The biology of lantibiotics from the lacticin 481 group is coming of age
    • Dufour A, Hindre T, Haras D, Le Pennec JP. The biology of lantibiotics from the lacticin 481 group is coming of age. FEMS Microbiol. Rev. 31: 134-167 (2007)
    • (2007) FEMS Microbiol. Rev , vol.31 , pp. 134-167
    • Dufour, A.1    Hindre, T.2    Haras, D.3    Le Pennec, J.P.4
  • 16
    • 0034117808 scopus 로고    scopus 로고
    • Lantibiotics and microcins: Polypeptides with unusual chemical diversity
    • Jack RW, Jung G. Lantibiotics and microcins: Polypeptides with unusual chemical diversity. Curr. Opin. Chem. Biol. 4: 310-317 (2000)
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 310-317
    • Jack, R.W.1    Jung, G.2
  • 17
    • 4544251455 scopus 로고    scopus 로고
    • Quorum sensing control of lantibiotic production; nisin and subtilin autoregulate their own biosynthesis
    • Kleerebezem M. Quorum sensing control of lantibiotic production; nisin and subtilin autoregulate their own biosynthesis. Peptides 25: 1405-1414 (2004)
    • (2004) Peptides , vol.25 , pp. 1405-1414
    • Kleerebezem, M.1
  • 18
    • 25144458128 scopus 로고    scopus 로고
    • New developments in lantibiotic biosynthesis and mode of action
    • Patton GC, van der Donk WA. New developments in lantibiotic biosynthesis and mode of action. Curr. Opin. Microbiol. 8: 543-551 (2005)
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 543-551
    • Patton, G.C.1    van der Donk, W.A.2
  • 19
    • 0036692989 scopus 로고    scopus 로고
    • Lantibiotics produced by lactic acid bacteria: Structure, function, and applications. Anton
    • Twomey D, Ross RP, Ryan M, Meaney B, Hill C. Lantibiotics produced by lactic acid bacteria: Structure, function, and applications. Anton. Van Leeuw. 82: 165-185 (2002)
    • (2002) Van Leeuw , vol.82 , pp. 165-185
    • Twomey, D.1    Ross, R.P.2    Ryan, M.3    Meaney, B.4    Hill, C.5
  • 20
    • 4644372683 scopus 로고    scopus 로고
    • Post-translational modifications during lantibiotic biosynthesis
    • Xie L, van der Donk WA. Post-translational modifications during lantibiotic biosynthesis. Curr. Opin. Chem. Biol. 8: 498-507 (2004)
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 498-507
    • Xie, L.1    van der Donk, W.A.2
  • 22
    • 0003148144 scopus 로고    scopus 로고
    • Lantibiotics: A survey
    • eds, ESCOM Science Publishers, Leiden, The Netherlands 1991
    • Jung G. Lantibiotics: A survey. pp. 1-35. In: Nisin and Novel Lantibiotics. Jung G, Sahl H-G (eds). ESCOM Science Publishers, Leiden, The Netherlands (1991)
    • Nisin and Novel Lantibiotics , pp. 1-35
    • Jung, G.1
  • 23
    • 0036257622 scopus 로고    scopus 로고
    • Multiple activities in lantibiotics-models for the design of novel antibiotics?
    • Pag U, Sahl HG. Multiple activities in lantibiotics-models for the design of novel antibiotics? Curr. Pharm. Design 8: 815-833 (2002)
    • (2002) Curr. Pharm. Design , vol.8 , pp. 815-833
    • Pag, U.1    Sahl, H.G.2
  • 24
    • 13844314218 scopus 로고    scopus 로고
    • Bacterial lantibiotics: Strategies to improve therapeutic potential
    • Cotter PD, Hill C, Ross RP. Bacterial lantibiotics: Strategies to improve therapeutic potential. Curr. Protein Pepe. Sc. 6: 61-75 (2005)
    • (2005) Curr. Protein Pepe. Sc , vol.6 , pp. 61-75
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 25
    • 0033851437 scopus 로고    scopus 로고
    • Posttranslationally modified bacteriocins-the lantibiotics
    • Guder A, Wiedemann I, Sahl HG. Posttranslationally modified bacteriocins-the lantibiotics. Biopolymers 55: 62-73 (2000)
    • (2000) Biopolymers , vol.55 , pp. 62-73
    • Guder, A.1    Wiedemann, I.2    Sahl, H.G.3
  • 27
    • 0030046733 scopus 로고    scopus 로고
    • Comparison of lantibiotic gene clusters and encoded proteins. Anton
    • Siezen RJ, Kuipers OP, de Vos WM. Comparison of lantibiotic gene clusters and encoded proteins. Anton. Van Leeuw. 69: 171-184 (1996)
    • (1996) Van Leeuw , vol.69 , pp. 171-184
    • Siezen, R.J.1    Kuipers, O.P.2    de Vos, W.M.3
  • 29
    • 0033828147 scopus 로고    scopus 로고
    • Each peptide of the two-component lantibiotic lacticin 3147 requires a separate modification enzyme for activity
    • McAuliffe O, Hill C, Ross RP. Each peptide of the two-component lantibiotic lacticin 3147 requires a separate modification enzyme for activity. Microbiology 146: 2147-2154 (2000)
    • (2000) Microbiology , vol.146 , pp. 2147-2154
    • McAuliffe, O.1    Hill, C.2    Ross, R.P.3
  • 30
    • 0035081130 scopus 로고    scopus 로고
    • Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics
    • Holo H, Jeknic Z, Daeschel M, Stevanovic S, Nes IF. Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics. Microbiology 147: 643-651 (2001)
    • (2001) Microbiology , vol.147 , pp. 643-651
    • Holo, H.1    Jeknic, Z.2    Daeschel, M.3    Stevanovic, S.4    Nes, I.F.5
  • 31
    • 12944260576 scopus 로고    scopus 로고
    • Genetic analysis of a unique bacteriocin, Smb, produced by Streptococcus mutans GS5
    • Yonezawa H, Kuramitsu HK. Genetic analysis of a unique bacteriocin, Smb, produced by Streptococcus mutans GS5. Antimicrob. Agents Ch. 49: 541-548 (2005)
    • (2005) Antimicrob. Agents Ch , vol.49 , pp. 541-548
    • Yonezawa, H.1    Kuramitsu, H.K.2
  • 32
    • 0032897165 scopus 로고    scopus 로고
    • Effects of gene disruptions in the nisin gene cluster of Lactococcus lactis on nisin production and producer immunity
    • Ra R, Beerthuyzen MM, de Vos WM, Saris PE, Kuipers OP. Effects of gene disruptions in the nisin gene cluster of Lactococcus lactis on nisin production and producer immunity. Microbiology 145: 1227-1233 (1999)
    • (1999) Microbiology , vol.145 , pp. 1227-1233
    • Ra, R.1    Beerthuyzen, M.M.2    de Vos, W.M.3    Saris, P.E.4    Kuipers, O.P.5
  • 33
    • 0028017686 scopus 로고
    • The leader peptide of colicin V shares consensus sequences with leader peptides that are common among peptide bacteriocins produced by Gram-positive bacteria
    • Havarstein LS, Holo H, Nes IF. The leader peptide of colicin V shares consensus sequences with leader peptides that are common among peptide bacteriocins produced by Gram-positive bacteria. Microbiology 140: 2383-2389 (1994)
    • (1994) Microbiology , vol.140 , pp. 2383-2389
    • Havarstein, L.S.1    Holo, H.2    Nes, I.F.3
  • 34
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Havarstein LS, Diep DB, Nes IF. A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export. Mol. Microbiol. 16: 229-240 (1995)
    • (1995) Mol. Microbiol , vol.16 , pp. 229-240
    • Havarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 35
    • 0033621484 scopus 로고    scopus 로고
    • Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147
    • Ryan MP, Jack RW, Josten M, Sahl HG, Jung G, Ross RP, Hill C. Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. J. Biol. Chem. 274: 37544-37550 (1999)
    • (1999) J. Biol. Chem , vol.274 , pp. 37544-37550
    • Ryan, M.P.1    Jack, R.W.2    Josten, M.3    Sahl, H.G.4    Jung, G.5    Ross, R.P.6    Hill, C.7
  • 37
    • 29444457743 scopus 로고    scopus 로고
    • Posttranslational conversion of L-serines to D-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147
    • Cotter PD, O'Connor PM, Draper LA, Lawton EM, Deegan LH, Hill C, Ross RP. Posttranslational conversion of L-serines to D-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147. P. Natl. Acad. Sci. USA 102: 18584-18589 (2005)
    • (2005) P. Natl. Acad. Sci. USA , vol.102 , pp. 18584-18589
    • Cotter, P.D.1    O'Connor, P.M.2    Draper, L.A.3    Lawton, E.M.4    Deegan, L.H.5    Hill, C.6    Ross, R.P.7
  • 39
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • Li B, Yu JP, Brunzelle JS, Moll GN, van der Donk WA, Nair SK. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science 311: 1464-1467 (2006)
    • (2006) Science , vol.311 , pp. 1464-1467
    • Li, B.1    Yu, J.P.2    Brunzelle, J.S.3    Moll, G.N.4    van der Donk, W.A.5    Nair, S.K.6
  • 41
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles
    • Ruhr E, Sahl. HG. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob. Agents Ch. 27: 841-845 (1985)
    • (1985) Antimicrob. Agents Ch , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 42
    • 0030024926 scopus 로고    scopus 로고
    • Genetics of subtilin and nisin biosyntheses: Biosynthesis of lantibiotics. Anton
    • Entian KD, de Vos WM. Genetics of subtilin and nisin biosyntheses: Biosynthesis of lantibiotics. Anton. Van Leeuw. 69: 109-117 (1996)
    • (1996) Van Leeuw , vol.69 , pp. 109-117
    • Entian, K.D.1    de Vos, W.M.2
  • 44
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin, and other lantibiotics
    • Brotz H, Josten M, Wiedemann I, Schneider U, Gotz F, Bierbaum, Sahl HG. Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin, and other lantibiotics. Mol. Microbiol. 30: 317-327 (1998)
    • (1998) Mol. Microbiol , vol.30 , pp. 317-327
    • Brotz, H.1    Josten, M.2    Wiedemann, I.3    Schneider, U.4    Gotz, F.5    Bierbaum6    Sahl, H.G.7
  • 45
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann I, Breukink E, van Kraaij C, Kuipers OP, Bierbaum G, de Kruijff B, Sahl HG Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. 276: 1772-1779 (2001)
    • (2001) J. Biol. Chem , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    de Kruijff, B.6    Sahl, H.G.7
  • 46
    • 0028952641 scopus 로고
    • Mode of action of the lantibiotic mersacidin: Inhibition of peptidoglycan biosynthesis via a novel mechanism?
    • Brotz H, Bierbaum G, Markus A, Molitor E, Sahl HG. Mode of action of the lantibiotic mersacidin: Inhibition of peptidoglycan biosynthesis via a novel mechanism? Antimicrob. Agents Ch. 39: 714-719 (1995)
    • (1995) Antimicrob. Agents Ch , vol.39 , pp. 714-719
    • Brotz, H.1    Bierbaum, G.2    Markus, A.3    Molitor, E.4    Sahl, H.G.5
  • 47
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • Brotz H, Bierbaum G, Reynolds PE, Sahl HG. The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation. Eur. J. Biochem. 246: 193-199 (1997)
    • (1997) Eur. J. Biochem , vol.246 , pp. 193-199
    • Brotz, H.1    Bierbaum, G.2    Reynolds, P.E.3    Sahl, H.G.4
  • 48
  • 50
    • 21744443281 scopus 로고    scopus 로고
    • Purification, partial amino acid sequence, and mode of action of pediocin PD-1, a bacteriocin produced by Pediococcus damnosus NCFB 1832
    • Bauer R, Chikindas ML, Dicks LM. Purification, partial amino acid sequence, and mode of action of pediocin PD-1, a bacteriocin produced by Pediococcus damnosus NCFB 1832. Int. J. Food Microbiol. 101: 17-27 (2005)
    • (2005) Int. J. Food Microbiol , vol.101 , pp. 17-27
    • Bauer, R.1    Chikindas, M.L.2    Dicks, L.M.3
  • 51
    • 0032768670 scopus 로고    scopus 로고
    • Identification of genes encoding two-component lantibiotic production in Staphylococcus aureus C55 and other phage group II S. aureus strains and demonstration of an association with the exfoliative toxin B gene
    • Navaratna MA, Sahl HG, Tagg JR. Identification of genes encoding two-component lantibiotic production in Staphylococcus aureus C55 and other phage group II S. aureus strains and demonstration of an association with the exfoliative toxin B gene. Infect. Immun. 67: 4268-4271 (1999)
    • (1999) Infect. Immun , vol.67 , pp. 4268-4271
    • Navaratna, M.A.1    Sahl, H.G.2    Tagg, J.R.3
  • 52
    • 0027971912 scopus 로고
    • Genetic structure of the Enterococcus faecalis plasmid pAD1-encoded cytolytic toxin system and its relationship to lantibiotic determinants
    • Gilmore MS, Segarra RA, Booth MC, Bogie CP, Hall LR, Clewell DB. Genetic structure of the Enterococcus faecalis plasmid pAD1-encoded cytolytic toxin system and its relationship to lantibiotic determinants. J. Bacterid. 176: 7335-7344 (1994)
    • (1994) J. Bacterid , vol.176 , pp. 7335-7344
    • Gilmore, M.S.1    Segarra, R.A.2    Booth, M.C.3    Bogie, C.P.4    Hall, L.R.5    Clewell, D.B.6
  • 54
    • 27444437741 scopus 로고    scopus 로고
    • Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin
    • Hyink O, Balakrishnan M, Tagg JR. Streptococcus rattus strain BHT produces both a class I two-component lantibiotic and a class II bacteriocin. FEMS Microbiol. Lett. 252: 235-241 (2005)
    • (2005) FEMS Microbiol. Lett , vol.252 , pp. 235-241
    • Hyink, O.1    Balakrishnan, M.2    Tagg, J.R.3
  • 55
    • 34247623480 scopus 로고    scopus 로고
    • Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics, and biological activity
    • O'Connor EB, Cotter PD, O'Connor P, O'Sullivan O, Tagg JR, Ross RP, Hill C. Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics, and biological activity. BMC Microbiol 7: 24 (2007)
    • (2007) BMC Microbiol , vol.7 , pp. 24
    • O'Connor, E.B.1    Cotter, P.D.2    O'Connor, P.3    O'Sullivan, O.4    Tagg, J.R.5    Ross, R.P.6    Hill, C.7
  • 56
    • 21444431674 scopus 로고    scopus 로고
    • Sequential actions of the two component peptides of the lantibiotic lacticin 3147 explain its antimicrobial activity at nanomolar concentrations
    • Morgan SM, O'Connor P, Cotter PD, Ross RP, Hill C. Sequential actions of the two component peptides of the lantibiotic lacticin 3147 explain its antimicrobial activity at nanomolar concentrations. Antimicrob. Agents Ch. 49: 2606-2611 (2005)
    • (2005) Antimicrob. Agents Ch , vol.49 , pp. 2606-2611
    • Morgan, S.M.1    O'Connor, P.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 58
    • 0037205949 scopus 로고    scopus 로고
    • Combination of antibiotic mechanisms in lantibiotics
    • Hoffmann A, Pag U, Wiedemann I, Sahl HG. Combination of antibiotic mechanisms in lantibiotics. Farmaco 57: 685-691 (2002)
    • (2002) Farmaco , vol.57 , pp. 685-691
    • Hoffmann, A.1    Pag, U.2    Wiedemann, I.3    Sahl, H.G.4
  • 59
    • 33846851726 scopus 로고    scopus 로고
    • What's in a name? Class distinction for bacteriocins
    • Available online at, Accessed Sept. 1, 2006
    • Heng NCK, Tagg JR. What's in a name? Class distinction for bacteriocins. Nature Reviews Microbiology 4. Available online at http://www.nature.com/ nrmicro/journal/v4/full/nrmicro1273-cI.html. Accessed Sept. 1, 2006.
    • Nature Reviews Microbiology , vol.4
    • Heng, N.C.K.1    Tagg, J.R.2
  • 61
    • 0029565798 scopus 로고
    • A bacteriocin-like peptide induces bacteriocin synthesis in Lb. plantation C11
    • Diep DB, Havarstein LS, Nes IF. A bacteriocin-like peptide induces bacteriocin synthesis in Lb. plantation C11. Mol. Microbiol. 18: 631-639 (1995)
    • (1995) Mol. Microbiol , vol.18 , pp. 631-639
    • Diep, D.B.1    Havarstein, L.S.2    Nes, I.F.3
  • 63
    • 0029772572 scopus 로고    scopus 로고
    • Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11
    • Diep DB, Havarstein LS, Nes IF. Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J. Bacteriol. 178: 4472-4483 (1996)
    • (1996) J. Bacteriol , vol.178 , pp. 4472-4483
    • Diep, D.B.1    Havarstein, L.S.2    Nes, I.F.3
  • 64
    • 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
    • Cintas LM, Casaus P, Herranz C, Havarstein LS, Holo H, Hernandez PE, Nes IF. 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 (2000)
    • (2000) J. Bacteriol , vol.182 , 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
  • 65
    • 0029916904 scopus 로고    scopus 로고
    • Topology of LcnD, a protein implicated in the transport of bacteriocins from Lactococcus lactis
    • Franke CM, Leenhouts KJ, Haandrikman AJ, Kok J, Venema G, Venema K. Topology of LcnD, a protein implicated in the transport of bacteriocins from Lactococcus lactis. J. Bacteriol. 178: 1766-1769 (1996)
    • (1996) J. Bacteriol , vol.178 , pp. 1766-1769
    • Franke, C.M.1    Leenhouts, K.J.2    Haandrikman, A.J.3    Kok, J.4    Venema, G.5    Venema, K.6
  • 66
    • 0035856593 scopus 로고    scopus 로고
    • Proteins of the lactococcin A secretion system: LcnD encodes two in-frame proteins
    • Varcamonti M, Nicastro G, Venema G, Kok J. Proteins of the lactococcin A secretion system: lcnD encodes two in-frame proteins. FEMS Microbiol. Lett. 204: 259-263 (2001)
    • (2001) FEMS Microbiol. Lett , vol.204 , pp. 259-263
    • Varcamonti, M.1    Nicastro, G.2    Venema, G.3    Kok, J.4
  • 67
    • 0030698620 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum
    • Cintas LM, Casaus P, Havarstein LS, Hernandez PE, Nes IF. Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum. Appl. Environ. Microb. 63: 4321-4330 (1997)
    • (1997) Appl. Environ. Microb , vol.63 , pp. 4321-4330
    • Cintas, L.M.1    Casaus, P.2    Havarstein, L.S.3    Hernandez, P.E.4    Nes, I.F.5
  • 69
    • 0030000298 scopus 로고    scopus 로고
    • Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI17
    • Tomita H, Fujimoto S, Tanimoto K, Ike Y. Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI17. J. Bacteriol. 178: 3585-3593 (1996)
    • (1996) J. Bacteriol , vol.178 , pp. 3585-3593
    • Tomita, H.1    Fujimoto, S.2    Tanimoto, K.3    Ike, Y.4
  • 71
    • 0026802510 scopus 로고
    • Characterization of the bacteriocins curvacin-a from Lactobacillus curvatus Lth1174 and sakacin-P from Lb. sake Lth673
    • Tichaczek PS, Nissenmeyer J, Nes IF, Vogel RF, Hammes WP. Characterization of the bacteriocins curvacin-a from Lactobacillus curvatus Lth1174 and sakacin-P from Lb. sake Lth673. Syst. Appl. Microbiol. 15: 460-468 (1992)
    • (1992) Syst. Appl. Microbiol , vol.15 , pp. 460-468
    • Tichaczek, P.S.1    Nissenmeyer, J.2    Nes, I.F.3    Vogel, R.F.4    Hammes, W.P.5
  • 72
    • 0027077825 scopus 로고
    • Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706
    • Holck A, Axelsson L, Birkeland SE, Aukrust T, Blom H. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706. J. Gen. Microbiol. 138: 2715-2720 (1992)
    • (1992) J. Gen. Microbiol , vol.138 , pp. 2715-2720
    • Holck, A.1    Axelsson, L.2    Birkeland, S.E.3    Aukrust, T.4    Blom, H.5
  • 73
    • 34347206678 scopus 로고    scopus 로고
    • Growth and bacteriocin production by lactic acid bacteria in vegetable broth and their effectiveness at reducing Listeria monocytogenes in vitro and in fresh-cut lettuce
    • Allende A, Martinez B, Selma V, Gil MI, Suarez JE, Rodriguez A. Growth and bacteriocin production by lactic acid bacteria in vegetable broth and their effectiveness at reducing Listeria monocytogenes in vitro and in fresh-cut lettuce. Food Microbiol. 24: 759-766 (2007)
    • (2007) Food Microbiol , vol.24 , pp. 759-766
    • Allende, A.1    Martinez, B.2    Selma, V.3    Gil, M.I.4    Suarez, J.E.5    Rodriguez, A.6
  • 74
    • 35448982527 scopus 로고    scopus 로고
    • The non-lantibiotic heat-stable bacteriocins in Gram-positive bacteria
    • ed, Academic Press, San Diego, CA, USA 2006
    • Nes IF, Brede DA, Holo H. The non-lantibiotic heat-stable bacteriocins in Gram-positive bacteria. pp. 107-114. In: Handbook of Biological Active Peptides. Kastin J (ed). Academic Press, San Diego, CA, USA (2006)
    • Handbook of Biological Active Peptides , pp. 107-114
    • Nes, I.F.1    Brede, D.A.2    Holo, H.3
  • 75
    • 0032788906 scopus 로고    scopus 로고
    • Class IIa bacteriocins from lactic acid bacteria: Antibacterial activity and food preservation
    • Ennahar S, Sonomoto K, Ishizaki A. Class IIa bacteriocins from lactic acid bacteria: Antibacterial activity and food preservation. J. Biosci. Bioeng. 87: 705-716 (1999)
    • (1999) J. Biosci. Bioeng , vol.87 , pp. 705-716
    • Ennahar, S.1    Sonomoto, K.2    Ishizaki, A.3
  • 76
    • 0026724915 scopus 로고
    • Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0
    • Henderson JT, Chopko AL, van Wassenaar PD. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch. Biochem. Biophys. 295: 5-12 (1992)
    • (1992) Arch. Biochem. Biophys , vol.295 , pp. 5-12
    • Henderson, J.T.1    Chopko, A.L.2    van Wassenaar, P.D.3
  • 78
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto Lozano JC, Meyer JN, Sletten K, Pelaz C, Nes IF. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 138: 1985-1990 (1992)
    • (1992) J. Gen. Microbiol , vol.138 , pp. 1985-1990
    • Nieto Lozano, J.C.1    Meyer, J.N.2    Sletten, K.3    Pelaz, C.4    Nes, I.F.5
  • 79
    • 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, Holo H, Havarstein LS, Hugas M, Garriga M, Nes IF. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microb. 62: 1676-1682 (1996)
    • (1996) Appl. Environ. Microb , vol.62 , pp. 1676-1682
    • Aymerich, T.1    Holo, H.2    Havarstein, L.S.3    Hugas, M.4    Garriga, M.5    Nes, I.F.6
  • 80
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings JW, Sailer M, Johnson K, Roy KL, Vederas JC, Stiles ME. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173: 7491-7500 (1991)
    • (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
  • 81
    • 0027080504 scopus 로고
    • Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides
    • Hechard Y, Derijard B, Letellier F, Cenatiempo Y. Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides. J. Gen. Microbiol. 138: 2725-2731(1992)
    • (1992) J. Gen. Microbiol , vol.138 , pp. 2725-2731
    • Hechard, Y.1    Derijard, B.2    Letellier, F.3    Cenatiempo, Y.4
  • 82
    • 0031717018 scopus 로고    scopus 로고
    • Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles
    • Chen Y, Ludescher RD, Montville TJ. Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles. Appl. Environ. Microb. 64: 3530-3532 (1998)
    • (1998) Appl. Environ. Microb , vol.64 , pp. 3530-3532
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 85
    • 0042029595 scopus 로고    scopus 로고
    • Differences in susceptibility of Listeria monocytogenes strains to sakacin P, sakacin A, pediocin PA-1, and nisin
    • Katla T, Naterstad K, Vancanneyt M, Swings J, Axelsson L. Differences in susceptibility of Listeria monocytogenes strains to sakacin P, sakacin A, pediocin PA-1, and nisin. Appl. Environ. Microb. 69: 4431-4417 (2003)
    • (2003) Appl. Environ. Microb , vol.69 , pp. 4431-4417
    • Katla, T.1    Naterstad, K.2    Vancanneyt, M.3    Swings, J.4    Axelsson, L.5
  • 86
    • 33745467496 scopus 로고    scopus 로고
    • Fimland G, Pirneskoski J, Kaewsrichan J, Jutila A, Kristiansen PE, Kinnunen PK, Nissen-Meyer J. Mutational analysis and membrane-interactions of the beta-sheet-like N-terminal domain of the pediocin-like antimicrobial peptide sakacin P. Biochim. Biophys. Acta 1764: 1132-1140 (2006)
    • Fimland G, Pirneskoski J, Kaewsrichan J, Jutila A, Kristiansen PE, Kinnunen PK, Nissen-Meyer J. Mutational analysis and membrane-interactions of the beta-sheet-like N-terminal domain of the pediocin-like antimicrobial peptide sakacin P. Biochim. Biophys. Acta 1764: 1132-1140 (2006)
  • 87
    • 0034120768 scopus 로고    scopus 로고
    • Anti-Listeria effect of enterocin A, produced by cheese-isolated Enterococcus faecium EFM01, relative to other bacteriocins from lactic acid bacteria
    • Ennahar S, Deschamps N. Anti-Listeria effect of enterocin A, produced by cheese-isolated Enterococcus faecium EFM01, relative to other bacteriocins from lactic acid bacteria. J. Appl. Microb. 88: 449-457 (2000)
    • (2000) J. Appl. Microb , vol.88 , pp. 449-457
    • Ennahar, S.1    Deschamps, N.2
  • 88
    • 0034005323 scopus 로고    scopus 로고
    • A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum
    • Fimland G, Johnsen L, Axelsson L, Brurberg MB, Nes IF, Eijsink VG, Nissen-Meyer J. A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum. J. Bacteriol. 182: 2643-2648 (2000)
    • (2000) J. Bacteriol , vol.182 , pp. 2643-2648
    • Fimland, G.1    Johnsen, L.2    Axelsson, L.3    Brurberg, M.B.4    Nes, I.F.5    Eijsink, V.G.6    Nissen-Meyer, J.7
  • 89
    • 0041848440 scopus 로고    scopus 로고
    • Comparative studies of immunity proteins of pediocin-like bacteriocins
    • Fimland G, Eijsink VG, Nissen-Meyer J, Comparative studies of immunity proteins of pediocin-like bacteriocins. Microbiology 148: 3661-3670 (2002)
    • (2002) Microbiology , vol.148 , pp. 3661-3670
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 90
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins construcced by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland G, Blingsmo OR, Sletten K, Jung F, Nes IF, Nissen-Meyer J. New biologically active hybrid bacteriocins construcced by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity. Appl. Environ. Microb. 62: 3313-3318 (1996)
    • (1996) Appl. Environ. Microb , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.R.2    Sletten, K.3    Jung, F.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 91
    • 15744401646 scopus 로고    scopus 로고
    • The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum
    • Johnsen L, Fimland G, Nissen-Meyer J. The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum. J. Biol. Chem. 280: 9243-9250 (2005)
    • (2005) J. Biol. Chem , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 92
    • 0031793223 scopus 로고    scopus 로고
    • The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C-terminus
    • Fimland G, Jack R, Jung G, Nes IF, Nissen-Meyer J. The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C-terminus. Appl. Environ. Microb. 64: 5057-5060 (1998)
    • (1998) Appl. Environ. Microb , vol.64 , pp. 5057-5060
    • Fimland, G.1    Jack, R.2    Jung, G.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 93
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of carnobacteriocin B2 and implications for structure-activity relation-ships among type IIa bacteriocins from lactic acid bacteria
    • Wang Y, Henz ME, Gallagher NL, Chai S, Gibbs AC, Yan LZ, Stiles ME, Wishart DS, Vederas JC. Solution structure of carnobacteriocin B2 and implications for structure-activity relation-ships among type IIa bacteriocins from lactic acid bacteria. Biochemistry 38: 15438-15447 (1999)
    • (1999) Biochemistry , vol.38 , pp. 15438-15447
    • Wang, Y.1    Henz, M.E.2    Gallagher, N.L.3    Chai, S.4    Gibbs, A.C.5    Yan, L.Z.6    Stiles, M.E.7    Wishart, D.S.8    Vederas, J.C.9
  • 94
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Fregeau Gallagher NL, Sailer M, Niemczura WP, Nakashima TT, Stiles ME, Vederas JC. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria. Biochemistry 36: 15062-15072 (1997)
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Fregeau Gallagher, N.L.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 95
    • 0141817944 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge
    • Uteng M, Hauge HH, Markwick PR, Fimland G, Mantzilas D, Nissen-Meyer J, Muhle-Goll C. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge. Biochemistry 42: 11417-11426 (2003)
    • (2003) Biochemistry , vol.42 , pp. 11417-11426
    • Uteng, M.1    Hauge, H.H.2    Markwick, P.R.3    Fimland, G.4    Mantzilas, D.5    Nissen-Meyer, J.6    Muhle-Goll, C.7
  • 96
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland G, Eijsink VG, Nissen-Meyer J. Mutational analysis of the role of tryptophan residues in an antimicrobial peptide. Biochemistry 41: 9508-9515 (2002)
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 97
    • 4143107127 scopus 로고    scopus 로고
    • Mutational analysis of mesentericin y105, an anti-Listeria bacteriocin, for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction
    • Morisset D, Berjeaud JM, Marion D, Lacombe C, Frere J. Mutational analysis of mesentericin y105, an anti-Listeria bacteriocin, for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction. Appl. Environ. Microb. 70: 4672-4680 (2004)
    • (2004) Appl. Environ. Microb , vol.70 , pp. 4672-4680
    • Morisset, D.1    Berjeaud, J.M.2    Marion, D.3    Lacombe, C.4    Frere, J.5
  • 98
    • 33847796246 scopus 로고    scopus 로고
    • Common mechanisms of target cell recognition and immunity for class II bacteriocins
    • Diep DB, Skaugen M, Salehian Z, Holo H, Nes IF. Common mechanisms of target cell recognition and immunity for class II bacteriocins. P. Natl. Acad. Sci. USA 104: 2384-2389 (2007)
    • (2007) P. Natl. Acad. Sci. USA , vol.104 , pp. 2384-2389
    • Diep, D.B.1    Skaugen, M.2    Salehian, Z.3    Holo, H.4    Nes, I.F.5
  • 99
    • 0036589172 scopus 로고
    • Two-peptide bacteriocins produced by lactic acid bacteria
    • Gameau S, Martin NI, Vederas JC. Two-peptide bacteriocins produced by lactic acid bacteria. Biochimie 84: 577-592 (1986)
    • (1986) Biochimie , vol.84 , pp. 577-592
    • Gameau, S.1    Martin, N.I.2    Vederas, J.C.3
  • 100
    • 0029957692 scopus 로고    scopus 로고
    • Functional analysis of the gene encoding immunity to lactacin F, lafI, and its use as a Lactobacillus-specific, food-grade genetic marker
    • Allison GE, Klaenhammer TR. Functional analysis of the gene encoding immunity to lactacin F, lafI, and its use as a Lactobacillus-specific, food-grade genetic marker. Appl. Environ. Microb. 62: 4450-4460 (1996)
    • (1996) Appl. Environ. Microb , vol.62 , pp. 4450-4460
    • Allison, G.E.1    Klaenhammer, T.R.2
  • 101
    • 0031775980 scopus 로고    scopus 로고
    • Antagonistic activity of Lb. plantarumC11: Two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A
    • Anderssen EL, Diep DB, Nes IF, Eijsink VG, Nissen-Meyer J. Antagonistic activity of Lb. plantarumC11: Two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A. Appl. Environ. Microb. 64: 2269-2272 (1998)
    • (1998) Appl. Environ. Microb , vol.64 , pp. 2269-2272
    • Anderssen, E.L.1    Diep, D.B.2    Nes, I.F.3    Eijsink, V.G.4    Nissen-Meyer, J.5
  • 102
    • 34249871146 scopus 로고    scopus 로고
    • Salivaricin P, one of a family of two-component antilisterial bacteriocins produced by intestinal isolates of Lactobacillus salivarius
    • Barrett E, Hayes M, O'Connor P, Gardiner G, Fitzgerald GF, Stanton C, Ross RP, Hill C. Salivaricin P, one of a family of two-component antilisterial bacteriocins produced by intestinal isolates of Lactobacillus salivarius. Appl. Environ. Microb. 73: 3719-3723 (2007)
    • (2007) Appl. Environ. Microb , vol.73 , pp. 3719-3723
    • Barrett, E.1    Hayes, M.2    O'Connor, P.3    Gardiner, G.4    Fitzgerald, G.F.5    Stanton, C.6    Ross, R.P.7    Hill, C.8
  • 103
    • 0033038921 scopus 로고    scopus 로고
    • Characterization, production, and purification of leucocin H, a two-peptide bacteriocin from Leuconostoc MF215B
    • Blom H, Katla T, Holck A, Sletten K, Axelsson L, Holo H. Characterization, production, and purification of leucocin H, a two-peptide bacteriocin from Leuconostoc MF215B. Curr. Microbiol. 39: 43-48 (1999)
    • (1999) Curr. Microbiol , vol.39 , pp. 43-48
    • Blom, H.1    Katla, T.2    Holck, A.3    Sletten, K.4    Axelsson, L.5    Holo, H.6
  • 104
    • 0034656248 scopus 로고    scopus 로고
    • Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lb. casei CRL 705
    • Cuozzo SA, Sesma F, Palacios JM, de Ruiz Holgado AP, Raya RR. Identification and nucleotide sequence of genes involved in the synthesis of lactocin 705, a two-peptide bacteriocin from Lb. casei CRL 705. FEMS Microbiol. Lett. 185: 157-161 (2000)
    • (2000) FEMS Microbiol. Lett , vol.185 , pp. 157-161
    • Cuozzo, S.A.1    Sesma, F.2    Palacios, J.M.3    de Ruiz Holgado, A.P.4    Raya, R.R.5
  • 105
    • 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, van Sinderen D, Thornton GM, Holo H, Nes IF, Collins JK. 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 (2002)
    • (2002) Microbiology , vol.148 , 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
  • 106
  • 107
    • 28444483938 scopus 로고    scopus 로고
    • Lactococcin MMT24, a novel two-peptide bacteriocin produced by Lactococcus lactis isolated from rigouta cheese
    • Ghrairi T, Frere J, Berjeaud JM, Manai M. Lactococcin MMT24, a novel two-peptide bacteriocin produced by Lactococcus lactis isolated from rigouta cheese. Int. J. Food Microbiol. 105: 389-398 (2005)
    • (2005) Int. J. Food Microbiol , vol.105 , pp. 389-398
    • Ghrairi, T.1    Frere, J.2    Berjeaud, J.M.3    Manai, M.4
  • 108
    • 1542329046 scopus 로고    scopus 로고
    • DNA analysis of the genes encoding acidocin LF221 A and acidocin LF221 B, two bacteriocins produced by Lb. gasseri LF221
    • Majhenic AC, Venema K, Allison GE, Matijasic BB, Rogelj I, Klaenhammer TR. DNA analysis of the genes encoding acidocin LF221 A and acidocin LF221 B, two bacteriocins produced by Lb. gasseri LF221. Appl. Microbio. Biot. 63: 705-714 (2004)
    • (2004) Appl. Microbio. Biot , vol.63 , pp. 705-714
    • Majhenic, A.C.1    Venema, K.2    Allison, G.E.3    Matijasic, B.B.4    Rogelj, I.5    Klaenhammer, T.R.6
  • 109
    • 0037173482 scopus 로고    scopus 로고
    • The locus responsible for production of plantaricin S, a class lib bacteriocin produced by Lb. plantarum LPCO10, is widely distributed among wild-type Lb. plantarum strains isolated from olive fermentations
    • Maldonado A, Ruiz-Barba JL, Floriano B, Jimenez-Diaz R. The locus responsible for production of plantaricin S, a class lib bacteriocin produced by Lb. plantarum LPCO10, is widely distributed among wild-type Lb. plantarum strains isolated from olive fermentations. Int. J. Food Microbiol. 77: 117-124 (2002)
    • (2002) Int. J. Food Microbiol , vol.77 , pp. 117-124
    • Maldonado, A.1    Ruiz-Barba, J.L.2    Floriano, B.3    Jimenez-Diaz, R.4
  • 110
    • 0031767742 scopus 로고    scopus 로고
    • Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754
    • McCormick JK, Poon A, Sailer M, Gao Y, Roy KL, McMullen LM, Vederas JC, Stiles ME, Van Belkum MJ. Genetic characterization and heterologous expression of brochocin-C, an antibotulinal, two-peptide bacteriocin produced by Brochothrix campestris ATCC 43754. Appl. Environ. Microb. 64: 4757-4766 (1998)
    • (1998) Appl. Environ. Microb , vol.64 , pp. 4757-4766
    • McCormick, J.K.1    Poon, A.2    Sailer, M.3    Gao, Y.4    Roy, K.L.5    McMullen, L.M.6    Vederas, J.C.7    Stiles, M.E.8    Van Belkum, M.J.9
  • 112
    • 1542308527 scopus 로고    scopus 로고
    • Functional characterization of a composite bacteriocin locus from malt, isolate Lactobacillus sakei 5
    • Vaughan A, Eijsink VG, Van Sinderen D. Functional characterization of a composite bacteriocin locus from malt, isolate Lactobacillus sakei 5. Appl. Environ. Microb. 69: 7194-7203 (2003)
    • (2003) Appl. Environ. Microb , vol.69 , pp. 7194-7203
    • Vaughan, A.1    Eijsink, V.G.2    Van Sinderen, D.3
  • 113
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer J, Holo H, Havarstein LS, Sletten K, Nes IF. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J. Bacteriol. 174: 5686-5692 (1992)
    • (1992) J. Bacteriol , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Havarstein, L.S.3    Sletten, K.4    Nes, I.F.5
  • 115
    • 0032005933 scopus 로고    scopus 로고
    • Amphiphilic alpha-helices are important structural motifs in the alpha and beta peptides that constitute the bacteriocin lactococcin G-enhancement of helix formation upon alpha-beta interaction
    • Hauge HH, Nissen-Meyer J, Nes IF, Eijsink VG. Amphiphilic alpha-helices are important structural motifs in the alpha and beta peptides that constitute the bacteriocin lactococcin G-enhancement of helix formation upon alpha-beta interaction. Eur. J. Biochem. 251: 565-572 (1998)
    • (1998) Eur. J. Biochem , vol.251 , pp. 565-572
    • Hauge, H.H.1    Nissen-Meyer, J.2    Nes, I.F.3    Eijsink, V.G.4
  • 116
    • 0032890798 scopus 로고    scopus 로고
    • Membrane-mimicking entities induce structuring of the two-peptide bacteriocins plantaricin E/F and plantaricin J/K
    • Hauge HH, Mantzilas D, Eijsink VG, Nissen-Meyer J. Membrane-mimicking entities induce structuring of the two-peptide bacteriocins plantaricin E/F and plantaricin J/K. J. Bacteriol. 181: 740-747 (1999)
    • (1999) J. Bacteriol , vol.181 , pp. 740-747
    • Hauge, H.H.1    Mantzilas, D.2    Eijsink, V.G.3    Nissen-Meyer, J.4
  • 117
    • 33646544691 scopus 로고    scopus 로고
    • Zendo T, Koga S, Shigeri Y, Nakayama J, Sonomoto K. Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4. Appl. Environ. Microb. 72: 3383-3389 (2006)
    • Zendo T, Koga S, Shigeri Y, Nakayama J, Sonomoto K. Lactococcin Q, a novel two-peptide bacteriocin produced by Lactococcus lactis QU 4. Appl. Environ. Microb. 72: 3383-3389 (2006)
  • 118
    • 34248158850 scopus 로고    scopus 로고
    • Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis
    • Oppegard C, Fimland G, Thorbaek L, Nissen-Meyer J. Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis. Appl. Environ. Microb. 73: 2931-2938 (2007)
    • (2007) Appl. Environ. Microb , vol.73 , pp. 2931-2938
    • Oppegard, C.1    Fimland, G.2    Thorbaek, L.3    Nissen-Meyer, J.4
  • 120
    • 49749115554 scopus 로고    scopus 로고
    • Skaugen M, Cintas L, Nes IF. Genetics of bacteriocin production in lactic acid bacteria. 3, pp. 225-249. In: Genetic of Lactic Acid Bacteria. Wood BJB, Warner PJ (eds). Kluwer Academic/ Plenum Publishers, London, UK (2003)
    • Skaugen M, Cintas L, Nes IF. Genetics of bacteriocin production in lactic acid bacteria. Vol. 3, pp. 225-249. In: Genetic of Lactic Acid Bacteria. Wood BJB, Warner PJ (eds). Kluwer Academic/ Plenum Publishers, London, UK (2003)
  • 121
    • 0025861639 scopus 로고    scopus 로고
    • Holo H, Nilssen O, Nes IF. Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: Isolation and characterization of the protein and its gene. J. Bacteriol. 173: 3879-3887 (1991)
    • Holo H, Nilssen O, Nes IF. Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: Isolation and characterization of the protein and its gene. J. Bacteriol. 173: 3879-3887 (1991)
  • 122
    • 0031032315 scopus 로고    scopus 로고
    • Synergistic hemolytic activity of Staphylococcus lugdunensis is mediated by three peptides encoded by a non-agr genetic locus
    • Donvito B, Etienne J, Denoroy L, Greenland T, Benito Y, Vandenesch F. Synergistic hemolytic activity of Staphylococcus lugdunensis is mediated by three peptides encoded by a non-agr genetic locus. Infect. Immun. 65: 95-100 (1997)
    • (1997) Infect. Immun , vol.65 , pp. 95-100
    • Donvito, B.1    Etienne, J.2    Denoroy, L.3    Greenland, T.4    Benito, Y.5    Vandenesch, F.6
  • 123
    • 0024287797 scopus 로고
    • The amino acid sequence of a gonococcal growth inhibitor from Staphylococcus haemolyticus
    • Watson DC, Yaguchi M, Bisaillon JG, Beaudet R, Morosoli R. The amino acid sequence of a gonococcal growth inhibitor from Staphylococcus haemolyticus. Biochem. J. 252: 87-93 (1988)
    • (1988) Biochem. J , vol.252 , pp. 87-93
    • Watson, D.C.1    Yaguchi, M.2    Bisaillon, J.G.3    Beaudet, R.4    Morosoli, R.5
  • 124
    • 78651115644 scopus 로고
    • Probable identity of a group D hemolysin with a bacteriocine
    • Brock TD, Davie JM. Probable identity of a group D hemolysin with a bacteriocine. J. Bacteriol. 86: 708-712 (1963)
    • (1963) J. Bacteriol , vol.86 , pp. 708-712
    • Brock, T.D.1    Davie, J.M.2
  • 125
    • 0029016239 scopus 로고
    • Isolation and characterization of pediocin L50, a new bacteriocin from Pediococcus acidilactici with a broad inhibitory spectrum
    • Cintas LM, Rodriguez JM, Fernandez MF, Sletten K, Nes IF, Hernandez PE, Holo H. Isolation and characterization of pediocin L50, a new bacteriocin from Pediococcus acidilactici with a broad inhibitory spectrum. Appl. Environ. Microb. 61: 2643-2648 (1995)
    • (1995) Appl. Environ. Microb , vol.61 , pp. 2643-2648
    • Cintas, L.M.1    Rodriguez, J.M.2    Fernandez, M.F.3    Sletten, K.4    Nes, I.F.5    Hernandez, P.E.6    Holo, H.7
  • 126
    • 0141557576 scopus 로고    scopus 로고
    • Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins
    • Gajic O, Buist G, Kojic M, Topisirovic L, Kuipers OP, Kok J. Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins. J. Biol. Chem. 278: 34291-34298 (2003)
    • (2003) J. Biol. Chem , vol.278 , pp. 34291-34298
    • Gajic, O.1    Buist, G.2    Kojic, M.3    Topisirovic, L.4    Kuipers, O.P.5    Kok, J.6
  • 127
    • 0035979791 scopus 로고    scopus 로고
    • Netz DJ, Sahl HG. Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. J. Mol. Biol. 311: 939-949 (2001)
    • Netz DJ, Sahl HG. Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. J. Mol. Biol. 311: 939-949 (2001)
  • 128
    • 33750071105 scopus 로고    scopus 로고
    • Complete sequence of the enterocin Q-encoding plasmid pCIZ2 from the multiple bcteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity
    • Criado R, Diep DB, Aakra A, Gutierrez J, Nes IF, Hernandez PE, Cintas LM. Complete sequence of the enterocin Q-encoding plasmid pCIZ2 from the multiple bcteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity. Appl. Environ. Microb. 72: 6653-6656 (2006)
    • (2006) Appl. Environ. Microb , vol.72 , pp. 6653-6656
    • Criado, R.1    Diep, D.B.2    Aakra, A.3    Gutierrez, J.4    Nes, I.F.5    Hernandez, P.E.6    Cintas, L.M.7
  • 129
    • 0031922351 scopus 로고    scopus 로고
    • Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins
    • Cintas LM, Casaus P, Holo H, Hernandez PE, Nes IF, Havarstein LS. Enterocins L50A and L50B, two novel bacteriocins from Enterococcus faecium L50, are related to staphylococcal hemolysins. J. Bacteriol. 180: 1988-1994 (1998)
    • (1998) J. Bacteriol , vol.180 , pp. 1988-1994
    • Cintas, L.M.1    Casaus, P.2    Holo, H.3    Hernandez, P.E.4    Nes, I.F.5    Havarstein, L.S.6
  • 130
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: A lactoferrin-derived peptide with, antimicrobial, antiviral, antitumor, and immunological properties. Cell Mol
    • Gifford JL, Hunter HN, Vogel HJ. Lactoferricin: A lactoferrin-derived peptide with, antimicrobial, antiviral, antitumor, and immunological properties. Cell Mol. Life Sci. 62: 2588-2598 (2005)
    • (2005) Life Sci , vol.62 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 131
    • 0042121501 scopus 로고    scopus 로고
    • Birkemo GA, Luders T, Andersen O, Nes IF, Nissen-Meyer J. Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.). Biochim. Biophys. Acta 1646: 207-215 (2003)
    • Birkemo GA, Luders T, Andersen O, Nes IF, Nissen-Meyer J. Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.). Biochim. Biophys. Acta 1646: 207-215 (2003)
  • 133
    • 19544375249 scopus 로고    scopus 로고
    • Proline conformation-dependent antimicrobial activity of a prolinerich histone h1 N-terminal peptide fragment isolated from the skin mucus of Atlantic salmon
    • Luders T, Birkemo GA, Nissen-Meyer J, Andersen O, Nes IF. Proline conformation-dependent antimicrobial activity of a prolinerich histone h1 N-terminal peptide fragment isolated from the skin mucus of Atlantic salmon. Antimicrob. Agents Ch. 49: 2399-2406 (2005)
    • (2005) Antimicrob. Agents Ch , vol.49 , pp. 2399-2406
    • Luders, T.1    Birkemo, G.A.2    Nissen-Meyer, J.3    Andersen, O.4    Nes, I.F.5
  • 134
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from Bufo bufo gargarizans
    • Park CB, Kim MS, Kim SC. A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res. Co. 218: 408-413 (1996)
    • (1996) Biochem. Biophys. Res. Co , vol.218 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 135
    • 0001439249 scopus 로고    scopus 로고
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. P. Nat. Aca. Sci. USA 97: 8245-8250 (2000)
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. P. Nat. Aca. Sci. USA 97: 8245-8250 (2000)
  • 137
    • 0033594420 scopus 로고    scopus 로고
    • Antibacterial peptide from Helicobacter pylori
    • Putsep K, Branden CI, Boman HQ Normark S. Antibacterial peptide from Helicobacter pylori. Nature 398: 671-672 (1999)
    • (1999) Nature , vol.398 , pp. 671-672
    • Putsep, K.1    Branden, C.I.2    Boman, H.Q.3    Normark, S.4
  • 138
    • 29144517842 scopus 로고    scopus 로고
    • Heterologous production of propionicin F, a bacteriocin from Propionibacterium freudenreichii
    • Brede DA, Faye T, Johnsborg O, Odegêard I, Nes IF, Holo H. Heterologous production of propionicin F, a bacteriocin from Propionibacterium freudenreichii. Appl. Environ. Microb. 71: 8077-8084 (2004)
    • (2004) Appl. Environ. Microb , vol.71 , pp. 8077-8084
    • Brede, D.A.1    Faye, T.2    Johnsborg, O.3    Odegêard, I.4    Nes, I.F.5    Holo, H.6
  • 139
    • 0036286488 scopus 로고    scopus 로고
    • An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii
    • Faye T, Brede DA, Langsrud T, Nes IF, Holo H. An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii. J. Bacteriol. 184: 3649-3656 (2002)
    • (2002) J. Bacteriol , vol.184 , pp. 3649-3656
    • Faye, T.1    Brede, D.A.2    Langsrud, T.3    Nes, I.F.4    Holo, H.5
  • 140
    • 10444284285 scopus 로고    scopus 로고
    • Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii
    • Brede DA, Faye T, Johnsborg O, Odegard I, Nes IF, Holo H. Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii. Appl. Environ. Microb. 70: 7303-7310 (2004)
    • (2004) Appl. Environ. Microb , vol.70 , pp. 7303-7310
    • Brede, D.A.1    Faye, T.2    Johnsborg, O.3    Odegard, I.4    Nes, I.F.5    Holo, H.6
  • 141
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 29: 1097-1106 (2001)
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 142
    • 0032726081 scopus 로고    scopus 로고
    • Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin
    • Zheng G, Yan LZ, Vederas JC, Zuber P. Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin. J. Bacteriol. 181: 7346-7355 (1999)
    • (1999) J. Bacteriol , vol.181 , pp. 7346-7355
    • Zheng, G.1    Yan, L.Z.2    Vederas, J.C.3    Zuber, P.4
  • 143
    • 2542507303 scopus 로고    scopus 로고
    • Identification and structural analysis of the antimicrobial domain in hipposin, a 51-mer antimicrobial peptide isolated from Atlantic halibut
    • Birkemo GA, Mantzilas D, Luders T, Nes IF, Nissen-Meyer J. Identification and structural analysis of the antimicrobial domain in hipposin, a 51-mer antimicrobial peptide isolated from Atlantic halibut. Biochim. Biophys. Acta 1699: 221-227 (2004)
    • (2004) Biochim. Biophys. Acta , vol.1699 , pp. 221-227
    • Birkemo, G.A.1    Mantzilas, D.2    Luders, T.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 144
    • 0032561422 scopus 로고    scopus 로고
    • Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus
    • Park IY, Park CB, Kim MS, Kim SC. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett. 437: 258-262 (1998)
    • (1998) FEBS Lett , vol.437 , pp. 258-262
    • Park, I.Y.1    Park, C.B.2    Kim, M.S.3    Kim, S.C.4
  • 145
    • 0142136187 scopus 로고    scopus 로고
    • Functional analysis of the gene cluster involved in production of the bacteriocin circularin A by Clostridium beijerinckii ATCC 25752
    • Kemperman R, Jonker M, Nauta A, Kuipers OP, Kok J. Functional analysis of the gene cluster involved in production of the bacteriocin circularin A by Clostridium beijerinckii ATCC 25752. Appl. Environ. Microb. 69: 5839-5848 (2003)
    • (2003) Appl. Environ. Microb , vol.69 , pp. 5839-5848
    • Kemperman, R.1    Jonker, M.2    Nauta, A.3    Kuipers, O.P.4    Kok, J.5
  • 146
    • 0029802393 scopus 로고    scopus 로고
    • Purification and characterization of enterocin 4, a bacteriocin produced by Enterococcus faecalis INIA 4
    • Joosten HM, Nunez M, Devreese B, Van Beeumen J, Marugg JD. Purification and characterization of enterocin 4, a bacteriocin produced by Enterococcus faecalis INIA 4. Appl. Environ. Microb. 62: 4220-4223 (1996)
    • (1996) Appl. Environ. Microb , vol.62 , pp. 4220-4223
    • Joosten, H.M.1    Nunez, M.2    Devreese, B.3    Van Beeumen, J.4    Marugg, J.D.5
  • 147
    • 0030735454 scopus 로고    scopus 로고
    • Cloning and genetic and sequence analyses of the bacteriocin 21 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative Plasmid pPD1
    • Tomita H, Fujimoto S, Tanimoto K, Ike Y. Cloning and genetic and sequence analyses of the bacteriocin 21 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative Plasmid pPD1. J. Bacterid. 179: 7843-7855 (1997)
    • (1997) J. Bacterid , vol.179 , pp. 7843-7855
    • Tomita, H.1    Fujimoto, S.2    Tanimoto, K.3    Ike, Y.4
  • 149
    • 0031962435 scopus 로고    scopus 로고
    • Analysis of the gene cluster involved in production and immunity of the peptide antibiotic AS-48 in Enterococcus faecalis
    • Martinez-Bueno M, Valdivia E, Galvez A, Coyette J, Maqueda M. Analysis of the gene cluster involved in production and immunity of the peptide antibiotic AS-48 in Enterococcus faecalis. Mol. Microbiol. 27: 347-358 (1998)
    • (1998) Mol. Microbiol , vol.27 , pp. 347-358
    • Martinez-Bueno, M.1    Valdivia, E.2    Galvez, A.3    Coyette, J.4    Maqueda, M.5
  • 150
    • 0031048694 scopus 로고    scopus 로고
    • PCR detection of sequences similarto the AS-48 structural gene in bacteriocin-producing enterococci
    • Joosten HM, Rodriguez E, Nunez M. PCR detection of sequences similarto the AS-48 structural gene in bacteriocin-producing enterococci. Lett. Appl. Microbiol. 24: 40-42 (1997)
    • (1997) Lett. Appl. Microbiol , vol.24 , pp. 40-42
    • Joosten, H.M.1    Rodriguez, E.2    Nunez, M.3
  • 151
    • 0034633634 scopus 로고    scopus 로고
    • Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin
    • Gonzalez C, Langdon GM, Bruix M, Galvez A, Valdivia E, Maqueda M, Rico M. Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin. P. Natl. Acad. Sci. USA 97: 11221-11226 (2000)
    • (2000) P. Natl. Acad. Sci. USA , vol.97 , pp. 11221-11226
    • Gonzalez, C.1    Langdon, G.M.2    Bruix, M.3    Galvez, A.4    Valdivia, E.5    Maqueda, M.6    Rico, M.7
  • 152
    • 24144459102 scopus 로고    scopus 로고
    • Purification and partial chemical characterization of the antimicrobial peptide cerein 8A
    • Bizani D, Dominguez AP, Brandelli A. Purification and partial chemical characterization of the antimicrobial peptide cerein 8A. Lett. Appl. Microbiol. 41: 269-273 (2005)
    • (2005) Lett. Appl. Microbiol , vol.41 , pp. 269-273
    • Bizani, D.1    Dominguez, A.P.2    Brandelli, A.3
  • 156
    • 0032240766 scopus 로고    scopus 로고
    • Gassericin A; an uncommon cyclic bacteriocin produced by Lactobacillus gasseri LA39 linked at N- and C-terminal ends
    • Kawai Y, Saito T, Kitazawa H, Itoh T. Gassericin A; an uncommon cyclic bacteriocin produced by Lactobacillus gasseri LA39 linked at N- and C-terminal ends. Biosci. Biotech. Bioch. 62: 2438-2440 (1998)
    • (1998) Biosci. Biotech. Bioch , vol.62 , pp. 2438-2440
    • Kawai, Y.1    Saito, T.2    Kitazawa, H.3    Itoh, T.4
  • 157
    • 2442641891 scopus 로고    scopus 로고
    • Kawai. Y, Ishii Y, Arakawa K, Uemura K, Saitoh B, Nishimura J, Kitazawa H, Yamazaki Y, TatenoY, Itoh T, Saito T. Structural and functional differences in two cyclic bacteriocins with the same sequences produced by lactobacilli. Appl. Environ. Microb. 70: 2906-2911 (2004)
    • Kawai. Y, Ishii Y, Arakawa K, Uemura K, Saitoh B, Nishimura J, Kitazawa H, Yamazaki Y, TatenoY, Itoh T, Saito T. Structural and functional differences in two cyclic bacteriocins with the same sequences produced by lactobacilli. Appl. Environ. Microb. 70: 2906-2911 (2004)
  • 158
    • 0037335990 scopus 로고    scopus 로고
    • Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574
    • Kemperman R, Kuipers A, Karsens H, Nauta A, Kuipers OP, Kok J. Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574. Appl. Environ. Microb. 69: 1589-1597 (2003)
    • (2003) Appl. Environ. Microb , vol.69 , pp. 1589-1597
    • Kemperman, R.1    Kuipers, A.2    Karsens, H.3    Nauta, A.4    Kuipers, O.P.5    Kok, J.6
  • 159
    • 0035216679 scopus 로고    scopus 로고
    • Dalet K, Cenatiempo Y, Cossart P, Hechard Y. A. sigma(54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 147: 3263-3269 (2001)
    • Dalet K, Cenatiempo Y, Cossart P, Hechard Y. A. sigma(54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 147: 3263-3269 (2001)
  • 160
    • 0034969179 scopus 로고    scopus 로고
    • Analysis of sigma (54)-dependent genes in Enterococcus faecalis: A mannose PTS permease EII(Man) is involved in sensitivity to a bacteriocin, mesentericin Y105
    • Hechard Y, Pelletier C, Cenatiempo Y, Frere J. Analysis of sigma (54)-dependent genes in Enterococcus faecalis: A mannose PTS permease EII(Man) is involved in sensitivity to a bacteriocin, mesentericin Y105. Microbiology 147: 1575-1580 (2001)
    • (2001) Microbiology , vol.147 , pp. 1575-1580
    • Hechard, Y.1    Pelletier, C.2    Cenatiempo, Y.3    Frere, J.4
  • 161
    • 0033930978 scopus 로고    scopus 로고
    • Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Ramnath M, Beukes M, Tamura K, Hastings JW Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Appl. Environ. Microb. 66: 3098-3101 (2000)
    • (2000) Appl. Environ. Microb , vol.66 , pp. 3098-3101
    • Ramnath, M.1    Beukes, M.2    Tamura, K.3    Hastings, J.W.4
  • 162
    • 15844422273 scopus 로고    scopus 로고
    • Identification of the DNA-binding site of the Rgg-like regulator LasX within the lactocin S promoter region
    • Rawlinson EL, Nes IF, Skaugen M. Identification of the DNA-binding site of the Rgg-like regulator LasX within the lactocin S promoter region. Microbiology 151: 813-823 (2005)
    • (2005) Microbiology , vol.151 , pp. 813-823
    • Rawlinson, E.L.1    Nes, I.F.2    Skaugen, M.3
  • 163
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem M, Quadri LE, Kuipers OP, de Vos WM. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol. Microbiol. 24: 895-904 (1997)
    • (1997) Mol. Microbiol , vol.24 , pp. 895-904
    • Kleerebezem, M.1    Quadri, L.E.2    Kuipers, O.P.3    de Vos, W.M.4
  • 164
    • 49749094215 scopus 로고    scopus 로고
    • Kleerebezem M, de Vos WM, Kuipers OP. The lantibiotics nisin and subtilin act as extracellular regulators of their own biosynthesis, pp. 159-174. In: Cell-Cell Signaling in Bacteria. Dunny GM, Winans SC (eds). ASM Press, Washington DC, USA (1999)
    • Kleerebezem M, de Vos WM, Kuipers OP. The lantibiotics nisin and subtilin act as extracellular regulators of their own biosynthesis, pp. 159-174. In: Cell-Cell Signaling in Bacteria. Dunny GM, Winans SC (eds). ASM Press, Washington DC, USA (1999)
  • 165
    • 49749087390 scopus 로고    scopus 로고
    • Nes IF, Eijsink VGH. Regulation of group H peptide bacteriocin synthesis by quorum-sensing mechansims. pp. 175-192. In: Cell-Cell Signaling in Bacteria. Dunny GM, Winans SC (eds). ASM Press, Washington DC, USA (1999)
    • Nes IF, Eijsink VGH. Regulation of group H peptide bacteriocin synthesis by quorum-sensing mechansims. pp. 175-192. In: Cell-Cell Signaling in Bacteria. Dunny GM, Winans SC (eds). ASM Press, Washington DC, USA (1999)
  • 166
    • 0037238666 scopus 로고    scopus 로고
    • Inducible bacteriocin production in Lactobacillus is regulated by differential expression of the pin operons and by two antagonizing response regulators, the activity of which is enhanced upon phosphorylation
    • Diep DB, Myhre R, Johnsborg O, Aakra A, Nes IF. Inducible bacteriocin production in Lactobacillus is regulated by differential expression of the pin operons and by two antagonizing response regulators, the activity of which is enhanced upon phosphorylation. Mol. Microbiol. 47: 483-494 (2003)
    • (2003) Mol. Microbiol , vol.47 , pp. 483-494
    • Diep, D.B.1    Myhre, R.2    Johnsborg, O.3    Aakra, A.4    Nes, I.F.5
  • 167
    • 0031662663 scopus 로고    scopus 로고
    • Identification of the DNA-binding sites for two response regulators involved in control of bacteriocin synthesis in Lactobacillus plantarum C11
    • Risoen PA, Havarstein LS, Diep DB, Nes IF. Identification of the DNA-binding sites for two response regulators involved in control of bacteriocin synthesis in Lactobacillus plantarum C11. Mol. Gen. Genet. 259: 224-232 (1998)
    • (1998) Mol. Gen. Genet , vol.259 , pp. 224-232
    • Risoen, P.A.1    Havarstein, L.S.2    Diep, D.B.3    Nes, I.F.4
  • 168
    • 0035091509 scopus 로고    scopus 로고
    • Risoen PA, Johnsborg O, Diep DB, Hamoen L, Venema G, Nes IF. Regulation of bacteriocin production in Lactobacillus plantarum depends on a conserved promoter arrangement with consensus binding sequence. Md. Genet. Genomics 265: 198-206 (2001)
    • Risoen PA, Johnsborg O, Diep DB, Hamoen L, Venema G, Nes IF. Regulation of bacteriocin production in Lactobacillus plantarum depends on a conserved promoter arrangement with consensus binding sequence. Md. Genet. Genomics 265: 198-206 (2001)
  • 169
    • 0034893775 scopus 로고    scopus 로고
    • Evidence for dual, functionality of the operon plnABCD in the regulation of bacteriocin production in Lactobacillus plantarum
    • Diep DB, Johnsborg O, Risoen PA, Nes IF. Evidence for dual, functionality of the operon plnABCD in the regulation of bacteriocin production in Lactobacillus plantarum. Mol. Microbiol. 41: 633-644 (2001)
    • (2001) Mol. Microbiol , vol.41 , pp. 633-644
    • Diep, D.B.1    Johnsborg, O.2    Risoen, P.A.3    Nes, I.F.4
  • 170
    • 0033862072 scopus 로고    scopus 로고
    • Functional analysis of promoters involved in quorum sensing-based regulation of bacteriocin production in Lactobacillus
    • Risoen PA, Brurberg MB, Eijsink VG, Nes IF. Functional analysis of promoters involved in quorum sensing-based regulation of bacteriocin production in Lactobacillus. Mol. Microbiol. 37: 619-628 (2000)
    • (2000) Mol. Microbiol , vol.37 , pp. 619-628
    • Risoen, P.A.1    Brurberg, M.B.2    Eijsink, V.G.3    Nes, I.F.4
  • 171
    • 34547842488 scopus 로고    scopus 로고
    • Straume D, Kjos M, Nes IF, Diep DB. Quorum-sensing based bacteriocin production is down-regulated by N-terminally truncated species of gene activators. Md. Genet. Genomics 278: 283-293 (2007)
    • Straume D, Kjos M, Nes IF, Diep DB. Quorum-sensing based bacteriocin production is down-regulated by N-terminally truncated species of gene activators. Md. Genet. Genomics 278: 283-293 (2007)
  • 172
    • 0037011936 scopus 로고    scopus 로고
    • Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction
    • Haas W, Shepard BD, Gilmore MS. Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction. Nature 415: 84-87 (2002)
    • (2002) Nature , vol.415 , pp. 84-87
    • Haas, W.1    Shepard, B.D.2    Gilmore, M.S.3
  • 173
    • 0035110702 scopus 로고    scopus 로고
    • McAuliffe O, O'Keeffe T, Hill C, Ross RP. Regulation of immunity to the two-component lantibiotic, lacticin 3147, by the transcriptional repressor LtnR. Md. Microbiol. 39: 982-993 (2001)
    • McAuliffe O, O'Keeffe T, Hill C, Ross RP. Regulation of immunity to the two-component lantibiotic, lacticin 3147, by the transcriptional repressor LtnR. Md. Microbiol. 39: 982-993 (2001)
  • 174
    • 0029796450 scopus 로고    scopus 로고
    • Rgg is a positive transcriptional regulator of the Streptococcus gordonii gtfG gene
    • Sulavik MC, Clewell DB. Rgg is a positive transcriptional regulator of the Streptococcus gordonii gtfG gene. J. Bacteriol. 178: 5826-5830 (1996)
    • (1996) J. Bacteriol , vol.178 , pp. 5826-5830
    • Sulavik, M.C.1    Clewell, D.B.2
  • 175
    • 0026708281 scopus 로고    scopus 로고
    • Sulavik MC, Tardif G, Clewell DB. Identification of a gene, rgg, which, regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis. J. Bacteriol. 174: 3577-3586 (1992)
    • Sulavik MC, Tardif G, Clewell DB. Identification of a gene, rgg, which, regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis. J. Bacteriol. 174: 3577-3586 (1992)
  • 176
    • 0034059449 scopus 로고    scopus 로고
    • Purification, characterization, and molecular analysis of the gene encoding glucosyltransferase from Streptococcus oralis
    • Fujiwara T, Hoshino T, Ooshima T, Sobue S, Hamada S. Purification, characterization, and molecular analysis of the gene encoding glucosyltransferase from Streptococcus oralis. Infect. Immun. 68: 2475-2483 (2000)
    • (2000) Infect. Immun , vol.68 , pp. 2475-2483
    • Fujiwara, T.1    Hoshino, T.2    Ooshima, T.3    Sobue, S.4    Hamada, S.5
  • 177
    • 0033041979 scopus 로고    scopus 로고
    • The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production
    • Chaussee MS, Ajdic D, Ferretti JJ. The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production. Infect. Immun. 67: 1715-1722 (1999)
    • (1999) Infect. Immun , vol.67 , pp. 1715-1722
    • Chaussee, M.S.1    Ajdic, D.2    Ferretti, J.J.3
  • 178
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an rgg-like regulator in the transcription, secretion, and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon WR, Gibson CM, Caparon MG. A role for trigger factor and an rgg-like regulator in the transcription, secretion, and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17: 6263-6275 (1998)
    • (1998) EMBO J , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 179
    • 0033051428 scopus 로고    scopus 로고
    • Functional analyses of the promoters in the lantibiotic mutacin II biosynthetic locus in Streptococcus mutans
    • Qi F, Chen P, Caufield PW. Functional analyses of the promoters in the lantibiotic mutacin II biosynthetic locus in Streptococcus mutans. Appl. Environ. Microb. 65: 652-658 (1999)
    • (1999) Appl. Environ. Microb , vol.65 , pp. 652-658
    • Qi, F.1    Chen, P.2    Caufield, P.W.3
  • 180
    • 0025872592 scopus 로고
    • Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45
    • Mortvedt CI, Nissen-Meyer J, Sletten K, Nes IF. Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45. Appl. Environ. Microb. 57: 1829-1834 (1991)
    • (1991) Appl. Environ. Microb , vol.57 , pp. 1829-1834
    • Mortvedt, C.I.1    Nissen-Meyer, J.2    Sletten, K.3    Nes, I.F.4
  • 181
    • 0036151988 scopus 로고    scopus 로고
    • Identification, characterization, and expression of a second, bicistronic, operon involved in the production of lactocin S in Lactobacillus sakei L45
    • Skaugen M, Andersen EL, Christie VH, Nes IF. Identification, characterization, and expression of a second, bicistronic, operon involved in the production of lactocin S in Lactobacillus sakei L45. Appl. Environ. Microb. 68: 720-727 (2002)
    • (2002) Appl. Environ. Microb , vol.68 , pp. 720-727
    • Skaugen, M.1    Andersen, E.L.2    Christie, V.H.3    Nes, I.F.4
  • 182
    • 0036589212 scopus 로고    scopus 로고
    • Rawlinson EL, Nes IF, Skaugen M. LasX, a transcriptional regulator of the lactocin S biosynthetic genes in Lactobacillus sakei LAS, acts both as an activator and a repressor. Biochimie 84: 559-567 (2002)
    • Rawlinson EL, Nes IF, Skaugen M. LasX, a transcriptional regulator of the lactocin S biosynthetic genes in Lactobacillus sakei LAS, acts both as an activator and a repressor. Biochimie 84: 559-567 (2002)
  • 183
    • 33646431460 scopus 로고    scopus 로고
    • Regulation of toxin and bacteriocin gene expression in Clostridiumby interchangeable RNA polymerase sigma factors
    • Dupuy B, Raffestin S, Matamouros S, Mani N, Popoff MR, Sonenshein AL. Regulation of toxin and bacteriocin gene expression in Clostridiumby interchangeable RNA polymerase sigma factors. Mol. Microbiol. 60: 1044-1057 (2006)
    • (2006) Mol. Microbiol , vol.60 , pp. 1044-1057
    • Dupuy, B.1    Raffestin, S.2    Matamouros, S.3    Mani, N.4    Popoff, M.R.5    Sonenshein, A.L.6
  • 184
    • 0022873043 scopus 로고
    • Characterization of a bacteriocinogenic plasmid from Clostridium perfringens and molecular genetic analysis of the bacteriocin-encoding gene
    • Gamier T, Cole ST. Characterization of a bacteriocinogenic plasmid from Clostridium perfringens and molecular genetic analysis of the bacteriocin-encoding gene. J. Bacteriol. 168: 1189-1196 (1986)
    • (1986) J. Bacteriol , vol.168 , pp. 1189-1196
    • Gamier, T.1    Cole, S.T.2
  • 185
    • 34250622074 scopus 로고    scopus 로고
    • Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salnarius UCC118
    • Corr SC, Li Y, Riedel CU, O'Toole PW, Hill C, Gahan CG. Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salnarius UCC118. P. Natl. Acad. Sci. USA 104: 7617-7621 (2007)
    • (2007) P. Natl. Acad. Sci. USA , vol.104 , pp. 7617-7621
    • Corr, S.C.1    Li, Y.2    Riedel, C.U.3    O'Toole, P.W.4    Hill, C.5    Gahan, C.G.6
  • 186
    • 34548293678 scopus 로고    scopus 로고
    • Development of innovativepediocin PA-1 by DNA shuffling among class IIa bacteriocins
    • Tominaga T, Hatakeyama Y. Development of innovativepediocin PA-1 by DNA shuffling among class IIa bacteriocins. Appl. Environ. Microb. 73: 5292-5299 (2007)
    • (2007) Appl. Environ. Microb , vol.73 , pp. 5292-5299
    • Tominaga, T.1    Hatakeyama, Y.2
  • 187
    • 33846913393 scopus 로고    scopus 로고
    • Bacteriocin diversity in Streptococcus and Enterococcus
    • Nes IF, Diep DB, Holo H. Bacteriocin diversity in Streptococcus and Enterococcus. J. Bacteriol. 189: 1189-1198 (2007)
    • (2007) J. Bacteriol , vol.189 , pp. 1189-1198
    • Nes, I.F.1    Diep, D.B.2    Holo, H.3
  • 188
    • 1842664393 scopus 로고    scopus 로고
    • Exploration of antimicrobial potential in LAB by genomics
    • Nes IF, Johnsborg O. Exploration of antimicrobial potential in LAB by genomics. Curr. Opin. Biotechnol. 15: 100-104 (2004)
    • (2004) Curr. Opin. Biotechnol , vol.15 , pp. 100-104
    • Nes, I.F.1    Johnsborg, O.2
  • 190
    • 0036301056 scopus 로고    scopus 로고
    • Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus
    • Netz DJ, Pohl R, Beck-Sickinger AQ Selmer T, Pierik AJ, Bastos Mdo C, Sahl HG, Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus. J. Mol. Biol. 319: 745-756 (2002)
    • (2002) J. Mol. Biol , vol.319 , pp. 745-756
    • Netz, D.J.1    Pohl, R.2    Beck-Sickinger, A.Q.3    Selmer, T.4    Pierik, A.J.5    Bastos Mdo, C.6    Sahl, H.G.7
  • 191
    • 0035979791 scopus 로고    scopus 로고
    • Netz DJ, Sahl HG, Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. J. Mol. Biol. 311: 939-949 (2001)
    • Netz DJ, Sahl HG, Marcelino R, dos Santos Nascimento J, de Oliveira SS, Soares MB, do Carmo de Freire Bastos M. Molecular characterisation of aureocin A70, a multi-peptide bacteriocin isolated from Staphylococcus aureus. J. Mol. Biol. 311: 939-949 (2001)
  • 192
    • 0031767745 scopus 로고    scopus 로고
    • Purification and genetic characterization of enterocin I from Enterococcus faecium 6T1a, a novel antilisterial plasmid-encoded bacteriocin which does not belong to the pediocin family of bacteriocins
    • Floriano B, Ruiz-Barba JL, Jimenez-Diaz R. Purification and genetic characterization of enterocin I from Enterococcus faecium 6T1a, a novel antilisterial plasmid-encoded bacteriocin which does not belong to the pediocin family of bacteriocins. Appl. Environ. Microb. 64: 4883-4890 (1998)
    • (1998) Appl. Environ. Microb , vol.64 , pp. 4883-4890
    • Floriano, B.1    Ruiz-Barba, J.L.2    Jimenez-Diaz, R.3
  • 193
    • 34248172307 scopus 로고    scopus 로고
    • Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of Gram-positive bacteria
    • Fujita K, Ichimasa S, Zendo T, Koga S, Yoneyama F, Nakayama J, Sonomoto K. Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of Gram-positive bacteria. Appl. Environ. Microb. 73: 2871-2877 (2007)
    • (2007) Appl. Environ. Microb , vol.73 , pp. 2871-2877
    • Fujita, K.1    Ichimasa, S.2    Zendo, T.3    Koga, S.4    Yoneyama, F.5    Nakayama, J.6    Sonomoto, K.7
  • 194
    • 0142136196 scopus 로고    scopus 로고
    • Purification and characterization of a novel bacteriocin produced by Enterococcus faecalis strain RJ-11
    • Yamamoto Y, Togawa Y, Shimosaka M, Okazaki M. Purification and characterization of a novel bacteriocin produced by Enterococcus faecalis strain RJ-11. Appl. Environ. Microb. 69: 5746-5753 (2003)
    • (2003) Appl. Environ. Microb , vol.69 , pp. 5746-5753
    • Yamamoto, Y.1    Togawa, Y.2    Shimosaka, M.3    Okazaki, M.4
  • 196
    • 0036286488 scopus 로고    scopus 로고
    • An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii
    • Faye T, Brede DA, Langsrud T, Nes IF, Holo H. An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii. J. Bacteriol. 184: 3649-3656 (2002)
    • (2002) J. Bacteriol , vol.184 , pp. 3649-3656
    • Faye, T.1    Brede, D.A.2    Langsrud, T.3    Nes, I.F.4    Holo, H.5
  • 198
    • 0030893398 scopus 로고    scopus 로고
    • Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: Evidence in support of the widespread occurrence of bacteriocin-like activity among ruminai isolates of B. fibrisolvens
    • Kalmokoff ML, Teather RM. Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: Evidence in support of the widespread occurrence of bacteriocin-like activity among ruminai isolates of B. fibrisolvens. Appl. Environ. Microb. 63: 394-402 (1997)
    • (1997) Appl. Environ. Microb , vol.63 , pp. 394-402
    • Kalmokoff, M.L.1    Teather, R.M.2
  • 199


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