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Volumn 31, Issue 2, 2007, Pages 134-167

The biology of lantibiotics from the lacticin 481 group is coming of age

Author keywords

Lacticin 481; Lantibiotic; Mutacin II; Nukacin ISK 1; Salivaricin; Streptococcin A FF22

Indexed keywords

BACTERIOCIN; BUTYRIVIBRIOCIN; CYTOLYSIN; LACTICIN; LANTHIONINE; LANTIBIOTIC; MACEDOCIN; MERSACIDIN; MUTACIN 2; NUKACIN; OROTIC ACID; RUMINOCOCCIN A; SALIVARICIN A; SALIVARICIN B; STEPTOCOCCIN; UNCLASSIFIED DRUG; VARIACIN;

EID: 33846863326     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1111/j.1574-6976.2006.00045.x     Document Type: Review
Times cited : (113)

References (261)
  • 1
    • 33645471937 scopus 로고    scopus 로고
    • Akçelik O, Tükel Ç , Özcengiz & Akçelik M (2006) Characterization of bacteriocins from two Lactococcus lactis subsp. lactis isolates. Mol Nutr Food Res 50: 306-313.
    • Akçelik O, Tükel Ç , Özcengiz & Akçelik M (2006) Characterization of bacteriocins from two Lactococcus lactis subsp. lactis isolates. Mol Nutr Food Res 50: 306-313.
  • 2
    • 0034120975 scopus 로고    scopus 로고
    • Biosynthesis of the lantibiotic mersacidin: Organization of a type B lantibiotic gene cluster
    • Altena K, Guder A, Cramer C & Bierbaum G (2000) Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster. Appl Environ Microbiol 66: 2565-2571.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2565-2571
    • Altena, K.1    Guder, A.2    Cramer, C.3    Bierbaum, G.4
  • 3
    • 13244264842 scopus 로고    scopus 로고
    • Inactivation of Staphylococcus aureus in raw milk cheese by combinations of high-pressure treatments and bacteriocin-producing lactic acid bacteria
    • Arqúes JL, Rodríguez E, Gaya P, Medina M, Guamis B & Nuñez M (2005a) Inactivation of Staphylococcus aureus in raw milk cheese by combinations of high-pressure treatments and bacteriocin-producing lactic acid bacteria. J Appl Microbiol 98: 254-260.
    • (2005) J Appl Microbiol , vol.98 , pp. 254-260
    • Arqúes, J.L.1    Rodríguez, E.2    Gaya, P.3    Medina, M.4    Guamis, B.5    Nuñez, M.6
  • 4
    • 19744366484 scopus 로고    scopus 로고
    • Effect of combinations of high-pressure treatment and bacteriocin-producing lactic acid bacteria on the survival of Listeria monocytogenes in raw milk cheese
    • Arqúes JL, Rodríguez E, Gaya P, Medina M & Nuñez M (2005b) Effect of combinations of high-pressure treatment and bacteriocin-producing lactic acid bacteria on the survival of Listeria monocytogenes in raw milk cheese. Int Dairy J 15: 893-900.
    • (2005) Int Dairy J , vol.15 , pp. 893-900
    • Arqúes, J.L.1    Rodríguez, E.2    Gaya, P.3    Medina, M.4    Nuñez, M.5
  • 5
  • 6
    • 12444307516 scopus 로고    scopus 로고
    • Heterologous expression and functional analysis of the gene cluster for the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1
    • Aso Y, Nagao J, Koga H, Okuda K, Kanemasa Y, Sashihara T, Nakayama J & Sonomoto K (2004a) Heterologous expression and functional analysis of the gene cluster for the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1. J Biosci Bioeng 98: 429-436.
    • (2004) J Biosci Bioeng , vol.98 , pp. 429-436
    • Aso, Y.1    Nagao, J.2    Koga, H.3    Okuda, K.4    Kanemasa, Y.5    Sashihara, T.6    Nakayama, J.7    Sonomoto, K.8
  • 7
    • 4644234612 scopus 로고    scopus 로고
    • Characterization of a gene cluster of Staphylococcus warneri ISK-1 encoding the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1
    • Aso Y, Sashihara T, Nagao J et al. (2004b) Characterization of a gene cluster of Staphylococcus warneri ISK-1 encoding the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1. Biosci Biotechnol Biochem 68: 1663-1671.
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 1663-1671
    • Aso, Y.1    Sashihara, T.2    Nagao, J.3
  • 8
    • 14544281061 scopus 로고    scopus 로고
    • Description of complete DNA sequence of two plasmids from the nukacin ISK-1 producer, Staphylococcus warneri ISK-1
    • Aso Y, Koga H, Sashihara T, Nagao J, Kanemasa Y, Nakayama J & Sonomoto K (2005a) Description of complete DNA sequence of two plasmids from the nukacin ISK-1 producer, Staphylococcus warneri ISK-1. Plasmid 53: 164-178.
    • (2005) Plasmid , vol.53 , pp. 164-178
    • Aso, Y.1    Koga, H.2    Sashihara, T.3    Nagao, J.4    Kanemasa, Y.5    Nakayama, J.6    Sonomoto, K.7
  • 11
    • 11844280314 scopus 로고    scopus 로고
    • Influence of a bacteriocin-producing lactic culture on proteolysis and texture of Hispánico cheese
    • Ávila M, Garde S, Gaya P, Medina M & Nuñez M (2005a) Influence of a bacteriocin-producing lactic culture on proteolysis and texture of Hispánico cheese. Int Dairy J 15: 145-153.
    • (2005) Int Dairy J , vol.15 , pp. 145-153
    • Ávila, M.1    Garde, S.2    Gaya, P.3    Medina, M.4    Nuñez, M.5
  • 12
    • 18444398069 scopus 로고    scopus 로고
    • Effect of milk inoculation with bacteriocin-producing lactic acid bacteria on a Lactobacillus helveticus adjunct cheese culture
    • Ávila M, Garde S, Medina M & Nuñez M (2005b) Effect of milk inoculation with bacteriocin-producing lactic acid bacteria on a Lactobacillus helveticus adjunct cheese culture. J Food Prot 68: 1026-1033.
    • (2005) J Food Prot , vol.68 , pp. 1026-1033
    • Ávila, M.1    Garde, S.2    Medina, M.3    Nuñez, M.4
  • 13
    • 33644536705 scopus 로고    scopus 로고
    • Effect of high-pressure treatment and a bacteriocin-producing lactic culture on the odor and aroma of Hispánico cheese: Correlation of volatile compounds and sensory analysis
    • Ávila M, Garde S, Ferńandez-García E, Medina M & Nuñez M (2006) Effect of high-pressure treatment and a bacteriocin-producing lactic culture on the odor and aroma of Hispánico cheese: correlation of volatile compounds and sensory analysis. J Agric Food Chem 54: 382-389.
    • (2006) J Agric Food Chem , vol.54 , pp. 382-389
    • Ávila, M.1    Garde, S.2    Ferńandez-García, E.3    Medina, M.4    Nuñez, M.5
  • 14
    • 0023890534 scopus 로고
    • Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic
    • Banerjee S & Hansen JN (1988) Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. J Biol Chem 263: 9508-9514.
    • (1988) J Biol Chem , vol.263 , pp. 9508-9514
    • Banerjee, S.1    Hansen, J.N.2
  • 15
    • 0028007534 scopus 로고
    • Construction of an expression system for engineering of the lantibiotic Pep5
    • Bierbaum G, Reis M, Szekat C & Sahl HG (1994) Construction of an expression system for engineering of the lantibiotic Pep5. Appl Environ Microbiol 60: 4332-4338.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4332-4338
    • Bierbaum, G.1    Reis, M.2    Szekat, C.3    Sahl, H.G.4
  • 16
    • 0028929222 scopus 로고
    • Cloning, sequencing and production of the lantibiotic mersacidin
    • Bierbaum G, Brötz H, Koller KP & Sahl HG (1995) Cloning, sequencing and production of the lantibiotic mersacidin. FEMS Microbiol Lett 127: 121-126.
    • (1995) FEMS Microbiol Lett , vol.127 , pp. 121-126
    • Bierbaum, G.1    Brötz, H.2    Koller, K.P.3    Sahl, H.G.4
  • 19
    • 33645779735 scopus 로고    scopus 로고
    • Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies
    • Bonelli RR, Schneider T, Sahl HG & Wiedemann I (2006) Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies. Antimicrob Agents Chemother 50: 1449-1457.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1449-1457
    • Bonelli, R.R.1    Schneider, T.2    Sahl, H.G.3    Wiedemann, I.4
  • 20
    • 29144508806 scopus 로고    scopus 로고
    • Development and characterization of a subtilin-regulated expression system in Bacillus subtilis: Strict control of gene expression by addition of subtilin
    • Bongers RS, Veening JW, Van Wieringen M, Kuipers OP & Kleerebezem M (2005) Development and characterization of a subtilin-regulated expression system in Bacillus subtilis: strict control of gene expression by addition of subtilin. Appl Environ Microbiol 71: 8818-8824.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8818-8824
    • Bongers, R.S.1    Veening, J.W.2    Van Wieringen, M.3    Kuipers, O.P.4    Kleerebezem, M.5
  • 21
    • 0029786349 scopus 로고    scopus 로고
    • Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic
    • Booth MC, Bogie CP, Sahl HG, Siezen RJ, Hatter KL & Gilmore MS (1996) Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic. Mol Microbiol 21: 1175-1184.
    • (1996) Mol Microbiol , vol.21 , pp. 1175-1184
    • Booth, M.C.1    Bogie, C.P.2    Sahl, H.G.3    Siezen, R.J.4    Hatter, K.L.5    Gilmore, M.S.6
  • 22
    • 0028952641 scopus 로고
    • Mode of action of the lantibiotic mersacidin: Inhibition of peptidoglycan biosynthesis via a novel mechanism?
    • Brötz H, Bierbaum G, Markus A, Molitor E & Sahl HG (1995) Mode of action of the lantibiotic mersacidin: inhibition of peptidoglycan biosynthesis via a novel mechanism? Antimicrob Agents Chemother 39: 714-719.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 714-719
    • Brötz, H.1    Bierbaum, G.2    Markus, A.3    Molitor, E.4    Sahl, H.G.5
  • 23
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • Brötz H, Bierbaum G, Reynolds PE & Sahl HG (1997) The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation. Eur J Biochem 246: 193-199.
    • (1997) Eur J Biochem , vol.246 , pp. 193-199
    • Brötz, H.1    Bierbaum, G.2    Reynolds, P.E.3    Sahl, H.G.4
  • 25
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • Brötz H, Josten M, Wiedemann I, Schneider U, Götz F, Bierbaum G & Sahl HG (1998b) Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol Microbiol 30: 317-327.
    • (1998) Mol Microbiol , vol.30 , pp. 317-327
    • Brötz, H.1    Josten, M.2    Wiedemann, I.3    Schneider, U.4    Götz, F.5    Bierbaum, G.6    Sahl, H.G.7
  • 26
    • 33748490494 scopus 로고    scopus 로고
    • A lesson in efficient killing from two-component lantibiotics
    • Breukink E (2006) A lesson in efficient killing from two-component lantibiotics. Mol Microbiol 61: 271-273.
    • (2006) Mol Microbiol , vol.61 , pp. 271-273
    • Breukink, E.1
  • 27
  • 30
    • 0023806662 scopus 로고
    • Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic
    • Buchman GW, Banerjee S & Hansen JN (1988) Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic. J Biol Chem 263: 16260-16266.
    • (1988) J Biol Chem , vol.263 , pp. 16260-16266
    • Buchman, G.W.1    Banerjee, S.2    Hansen, J.N.3
  • 31
    • 25144518888 scopus 로고    scopus 로고
    • The rationale and potential for the reduction of oral malodour using Streptococcus salivarius probiotics
    • Burton JP, Chilcott CN & Tagg JR (2005) The rationale and potential for the reduction of oral malodour using Streptococcus salivarius probiotics. Oral Dis 11: 29-31.
    • (2005) Oral Dis , vol.11 , pp. 29-31
    • Burton, J.P.1    Chilcott, C.N.2    Tagg, J.R.3
  • 32
    • 33645099061 scopus 로고    scopus 로고
    • A preliminary study of the effect of probiotic Streptococcus salivarius K12 on oral malodour parameters
    • Burton JP, Chilcott CN, Moore CJ, Speiser G & Tagg JR (2006a) A preliminary study of the effect of probiotic Streptococcus salivarius K12 on oral malodour parameters. J Appl Microbiol 100: 754-764.
    • (2006) J Appl Microbiol , vol.100 , pp. 754-764
    • Burton, J.P.1    Chilcott, C.N.2    Moore, C.J.3    Speiser, G.4    Tagg, J.R.5
  • 34
    • 0036007382 scopus 로고    scopus 로고
    • Cross-inhibition among wild strains of Lactococcus lactis isolated from the same ecological niche
    • Centeno JA, Gaya P, Medina M & Nuñez M (2002) Cross-inhibition among wild strains of Lactococcus lactis isolated from the same ecological niche. J Food Prot 65: 205-210.
    • (2002) J Food Prot , vol.65 , pp. 205-210
    • Centeno, J.A.1    Gaya, P.2    Medina, M.3    Nuñez, M.4
  • 36
    • 0036428648 scopus 로고    scopus 로고
    • Characterization of the promoter regions involved in galactose- and nisin-mediated induction of the nisA gene in Lactococcus lactis ATCC 11454
    • Chandrapati S & O'Sullivan DJ (2002) Characterization of the promoter regions involved in galactose- and nisin-mediated induction of the nisA gene in Lactococcus lactis ATCC 11454. Mol Microbiol 46: 467-477.
    • (2002) Mol Microbiol , vol.46 , pp. 467-477
    • Chandrapati, S.1    O'Sullivan, D.J.2
  • 38
  • 39
    • 0141960369 scopus 로고    scopus 로고
    • Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes
    • Chaussee MS, Somerville GA, Reitzer L & Musser JM (2003) Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes. J Bacteriol 185: 6016-6024.
    • (2003) J Bacteriol , vol.185 , pp. 6016-6024
    • Chaussee, M.S.1    Somerville, G.A.2    Reitzer, L.3    Musser, J.M.4
  • 40
    • 0031842742 scopus 로고    scopus 로고
    • Structure-activity study of the lantibiotic mutacin II from Streptococcus mutans T8 by a gene replacement strategy
    • Chen P, Novak J, Kirk M, Barnes S, Qi F & Caufield PW (1998a) Structure-activity study of the lantibiotic mutacin II from Streptococcus mutans T8 by a gene replacement strategy. Appl Environ Microbiol 64: 2335-2340.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2335-2340
    • Chen, P.1    Novak, J.2    Kirk, M.3    Barnes, S.4    Qi, F.5    Caufield, P.W.6
  • 41
    • 0031963001 scopus 로고    scopus 로고
    • Diacylglycerol kinase is involved in regulation of expression of the lantibiotic mutacin II of Streptococcus mutans
    • Chen P, Novak J, Qi F & Caufield PW (1998b) Diacylglycerol kinase is involved in regulation of expression of the lantibiotic mutacin II of Streptococcus mutans. J Bacteriol 180: 167-170.
    • (1998) J Bacteriol , vol.180 , pp. 167-170
    • Chen, P.1    Novak, J.2    Qi, F.3    Caufield, P.W.4
  • 42
    • 0032985875 scopus 로고    scopus 로고
    • The specific genes for lantibiotic mutacin II biosynthesis in Streptococcus mutans T8 are clustered and can be transferred en bloc
    • Chen P, Qi F, Novak J & Caufield PW (1999) The specific genes for lantibiotic mutacin II biosynthesis in Streptococcus mutans T8 are clustered and can be transferred en bloc. Appl Environ Microbiol 65: 1356-1360.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1356-1360
    • Chen, P.1    Qi, F.2    Novak, J.3    Caufield, P.W.4
  • 43
    • 0035916407 scopus 로고    scopus 로고
    • Effect of amino acid substitutions in conserved residues in the leader peptide on biosynthesis of the lantibiotic mutacin II
    • Chen P, Qi F, Novak J, Krull RE & Caufield PW (2001) Effect of amino acid substitutions in conserved residues in the leader peptide on biosynthesis of the lantibiotic mutacin II. FEMS Microbiol Lett 195: 139-144.
    • (2001) FEMS Microbiol Lett , vol.195 , pp. 139-144
    • Chen, P.1    Qi, F.2    Novak, J.3    Krull, R.E.4    Caufield, P.W.5
  • 46
    • 0141725789 scopus 로고    scopus 로고
    • The Enterococcus faecalis cytolysin: A novel toxin active against eukaryotic and prokaryotic cells
    • Coburn PS & Gilmore MS (2003) The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells. Cell Microbiol 5: 661-669.
    • (2003) Cell Microbiol , vol.5 , pp. 661-669
    • Coburn, P.S.1    Gilmore, M.S.2
  • 47
    • 0032967758 scopus 로고    scopus 로고
    • A novel means of self-protection, unrelated to toxin activation, confers immunity to the bactericidal effects of the Enterococcus faecalis cytolysin
    • Coburn PS, Hancock LE, Booth MC & Gilmore MS (1999) A novel means of self-protection, unrelated to toxin activation, confers immunity to the bactericidal effects of the Enterococcus faecalis cytolysin. Infect Immun 67: 3339-3347.
    • (1999) Infect Immun , vol.67 , pp. 3339-3347
    • Coburn, P.S.1    Hancock, L.E.2    Booth, M.C.3    Gilmore, M.S.4
  • 48
    • 11144287200 scopus 로고    scopus 로고
    • Enterococcus faecalis senses target cells and in response expresses cytolysin
    • Coburn PS, Pillar CM, Jett BD, Haas W & Gilmore MS (2004) Enterococcus faecalis senses target cells and in response expresses cytolysin. Science 306: 2270-2272.
    • (2004) Science , vol.306 , pp. 2270-2272
    • Coburn, P.S.1    Pillar, C.M.2    Jett, B.D.3    Haas, W.4    Gilmore, M.S.5
  • 49
    • 0344837858 scopus 로고    scopus 로고
    • Activation of subtilin precursors by Bacillus subtilis extracellular serine proteases subtilisin (AprE), WprA, and Vpr
    • Corvey C, Stein T, Düsterhus S, Karas M & Entian KD (2003) Activation of subtilin precursors by Bacillus subtilis extracellular serine proteases subtilisin (AprE), WprA, and Vpr. Biochem Biophys Res Commun 304: 48-54.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 48-54
    • Corvey, C.1    Stein, T.2    Düsterhus, S.3    Karas, M.4    Entian, K.D.5
  • 50
    • 13844314218 scopus 로고    scopus 로고
    • Bacterial lantibiotics: Strategies to improve therapeutic potential
    • Cotter PD, Hill C & Ross RP (2005a) Bacterial lantibiotics: strategies to improve therapeutic potential. Curr Protein Pept Sci 6: 61-75.
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 61-75
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 51
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter PD, Hill C & Ross RP (2005b) Bacteriocins: developing innate immunity for food. Nat Rev Microbiol 3: 777-788.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 52
    • 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 (2005c) Posttranslational conversion of L-serines to D-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147. Proc Natl Acad Sci USA 102: 18584-18589.
    • (2005) Proc 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
  • 53
    • 33846851726 scopus 로고    scopus 로고
    • What's in a name? Class distinction for bacteriocins
    • doi:10.1038/nrmicro1273-c2
    • Cotter PD, Hill C & Ross RP (2006) What's in a name? Class distinction for bacteriocins. Nat Rev Microbiol 4: 2. doi:10.1038/nrmicro1273-c2.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 2
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 55
    • 18044400091 scopus 로고    scopus 로고
    • Ruminococcin A, a new lantibiotic produced by a Ruminococcus gnavus strain isolated from human feces
    • Dabard J, Bridonneau C, Philippe C et al. (2001) Ruminococcin A, a new lantibiotic produced by a Ruminococcus gnavus strain isolated from human feces. Appl Environ Microbiol 67: 4111-4118.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4111-4118
    • Dabard, J.1    Bridonneau, C.2    Philippe, C.3
  • 57
    • 0030047564 scopus 로고    scopus 로고
    • Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study
    • Demel RA, Peelen T, Siezen RJ, de Kruijff B & Kuipers OP (1996) Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity. A monolayer study. Eur J Biochem 235: 267-274.
    • (1996) Eur J Biochem , vol.235 , pp. 267-274
    • Demel, R.A.1    Peelen, T.2    Siezen, R.J.3    de Kruijff, B.4    Kuipers, O.P.5
  • 58
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis using the foodgrade inducer nisin
    • de Ruyter PGGA, Kuipers OP & de Vos WM (1996) Controlled gene expression systems for Lactococcus lactis using the foodgrade inducer nisin. Appl Environ Microbiol 62: 3662-3667.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3662-3667
    • de Ruyter, P.G.G.A.1    Kuipers, O.P.2    de Vos, W.M.3
  • 59
    • 0029028865 scopus 로고
    • Maturation pathway of nisin and other lantibiotics: Posttranslationally modified antimicrobial peptides exported by Gram-positive bacteria
    • de Vos WM, Kuipers OP, van der Meer JR & Siezen RJ (1995) Maturation pathway of nisin and other lantibiotics: posttranslationally modified antimicrobial peptides exported by Gram-positive bacteria. Mol Microbiol 17: 427-437.
    • (1995) Mol Microbiol , vol.17 , pp. 427-437
    • de Vos, W.M.1    Kuipers, O.P.2    van der Meer, J.R.3    Siezen, R.J.4
  • 60
    • 0025356864 scopus 로고
    • Analysis of the genetic determinant for production of the peptide antibiotic nisin
    • Dodd HM, Horn N & Gasson MJ (1990) Analysis of the genetic determinant for production of the peptide antibiotic nisin. J Gen Microbiol 136: 555-566.
    • (1990) J Gen Microbiol , vol.136 , pp. 555-566
    • Dodd, H.M.1    Horn, N.2    Gasson, M.J.3
  • 61
    • 0031842606 scopus 로고    scopus 로고
    • Sequence and analysis of the 60 kb conjugative, bacteriocin-producing plasmid pMRC01 from Lactococcus lactis DPC3147
    • Dougherty BA, Hill C, Weidman JF, Richardson DR, Venter JC & Ross RP (1998) Sequence and analysis of the 60 kb conjugative, bacteriocin-producing plasmid pMRC01 from Lactococcus lactis DPC3147. Mol Microbiol 29: 1029-1038.
    • (1998) Mol Microbiol , vol.29 , pp. 1029-1038
    • Dougherty, B.A.1    Hill, C.2    Weidman, J.F.3    Richardson, D.R.4    Venter, J.C.5    Ross, R.P.6
  • 63
    • 0026055403 scopus 로고
    • Plasmid-encoded determinants for bacteriocin production and immunity in a Lactococcus lactis strain and purification of the inhibitory peptide
    • Dufour A, Thuault D, Boulliou A, Bourgeois CM & Le Pennec J-P (1991) Plasmid-encoded determinants for bacteriocin production and immunity in a Lactococcus lactis strain and purification of the inhibitory peptide. J Gen Microbiol 137: 2423-2429.
    • (1991) J Gen Microbiol , vol.137 , pp. 2423-2429
    • Dufour, A.1    Thuault, D.2    Boulliou, A.3    Bourgeois, C.M.4    Le Pennec, J.-P.5
  • 64
    • 0033797550 scopus 로고    scopus 로고
    • IS1675, a novel lactococcal insertion element, forms a transposon-like structure including the lacticin 481 lantibiotic operon
    • Dufour A, Rincé A, Uguen P & Le Pennec J-P (2000) IS1675, a novel lactococcal insertion element, forms a transposon-like structure including the lacticin 481 lantibiotic operon. J Bacteriol 182: 5600-5605.
    • (2000) J Bacteriol , vol.182 , pp. 5600-5605
    • Dufour, A.1    Rincé, A.2    Uguen, P.3    Le Pennec, J.-P.4
  • 65
    • 33846854389 scopus 로고    scopus 로고
    • Dufour A, Rincé A, Hindré T, Haras H & Le Pennec J-P (2003) Lacticin 481: an antimicrobial peptide of the lantibiotic family produced by Lactococcus lactis. Recent Res Devel Bacteriol 1: 219-234.
    • Dufour A, Rincé A, Hindré T, Haras H & Le Pennec J-P (2003) Lacticin 481: an antimicrobial peptide of the lantibiotic family produced by Lactococcus lactis. Recent Res Devel Bacteriol 1: 219-234.
  • 66
    • 0036418802 scopus 로고    scopus 로고
    • Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication
    • Eijsink VGH, Axelsson L, Diep DB, Håvarstein LS, Holo H & Nes IF (2002) Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication. Antonie Leeuwenhoek 81: 639-654.
    • (2002) Antonie Leeuwenhoek , vol.81 , pp. 639-654
    • Eijsink, V.G.H.1    Axelsson, L.2    Diep, D.B.3    Håvarstein, L.S.4    Holo, H.5    Nes, I.F.6
  • 67
    • 0026442521 scopus 로고
    • Biosynthesis of the lantibiotic nisin: Genomic organization and membrane localization of the NisB protein
    • Engelke G, Gutowski-Eckel Z, Hammelmann M & Entian KD (1992) Biosynthesis of the lantibiotic nisin: genomic organization and membrane localization of the NisB protein. Appl Environ Microbiol 58: 3730-3743.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3730-3743
    • Engelke, G.1    Gutowski-Eckel, Z.2    Hammelmann, M.3    Entian, K.D.4
  • 69
    • 0030024926 scopus 로고    scopus 로고
    • Genetics of subtilin and nisin biosyntheses
    • Entian KD & de Vos WM (1996) Genetics of subtilin and nisin biosyntheses. Antonie Leeuwenhoek 69: 109-117.
    • (1996) Antonie Leeuwenhoek , vol.69 , pp. 109-117
    • Entian, K.D.1    de Vos, W.M.2
  • 70
    • 0033605727 scopus 로고    scopus 로고
    • Membrane topology of the lactococcal bacteriocin ATP-binding cassette transporter protein LcnC
    • Franke CM, Tiemersma J, Venema G & Kok J (1999) Membrane topology of the lactococcal bacteriocin ATP-binding cassette transporter protein LcnC. J Biol Chem 274: 8484-8490.
    • (1999) J Biol Chem , vol.274 , pp. 8484-8490
    • Franke, C.M.1    Tiemersma, J.2    Venema, G.3    Kok, J.4
  • 72
    • 0035135834 scopus 로고    scopus 로고
    • PCR detection of the structural genes of nisin Z and lacticin 481 in Lactococcus lactis subsp. lactis INIA 415, a strain isolated from raw milk Manchego cheese
    • Garde S, Rodríguez E, Gaya P, Medina M & Nuñez M (2001) PCR detection of the structural genes of nisin Z and lacticin 481 in Lactococcus lactis subsp. lactis INIA 415, a strain isolated from raw milk Manchego cheese. Biotechnol Lett 23: 85-89.
    • (2001) Biotechnol Lett , vol.23 , pp. 85-89
    • Garde, S.1    Rodríguez, E.2    Gaya, P.3    Medina, M.4    Nuñez, M.5
  • 73
    • 0037032188 scopus 로고    scopus 로고
    • Volatile compounds in Hispánico cheese manufactured using a mesophilic starter, a thermophilic starter, and bacteriocin-producing Lactococcus lactis subsp. lactis INIA 415
    • Garde S, Carbonell M, Fernández-García E, Medina M & Nuñez M (2002a) Volatile compounds in Hispánico cheese manufactured using a mesophilic starter, a thermophilic starter, and bacteriocin-producing Lactococcus lactis subsp. lactis INIA 415. J Agric Food Chem 50: 6752-6757.
    • (2002) J Agric Food Chem , vol.50 , pp. 6752-6757
    • Garde, S.1    Carbonell, M.2    Fernández-García, E.3    Medina, M.4    Nuñez, M.5
  • 74
    • 0037023956 scopus 로고    scopus 로고
    • Proteolysis in Hispánico cheese manufactured using a mesophilic starter, a thermophilic starter, and bacteriocin-producing Lactococcus lactis subsp. lactis INIA 415 adjunct culture
    • Garde S, Tomillo J, Gaya P, Medina M & Nuñez M (2002b) Proteolysis in Hispánico cheese manufactured using a mesophilic starter, a thermophilic starter, and bacteriocin-producing Lactococcus lactis subsp. lactis INIA 415 adjunct culture. J Agric Food Chem 50: 3479-3485.
    • (2002) J Agric Food Chem , vol.50 , pp. 3479-3485
    • Garde, S.1    Tomillo, J.2    Gaya, P.3    Medina, M.4    Nuñez, M.5
  • 75
    • 33744971911 scopus 로고    scopus 로고
    • Proteolysis of Hispánico cheese manufactured using lacticin 481-producing Lactococcus lactis subsp. lactis INIA 639
    • Garde S, Ávila M, Gaya P, Medina M & Nuñez M (2006) Proteolysis of Hispánico cheese manufactured using lacticin 481-producing Lactococcus lactis subsp. lactis INIA 639. J Dairy Sci 89: 840-849.
    • (2006) J Dairy Sci , vol.89 , pp. 840-849
    • Garde, S.1    Ávila, M.2    Gaya, P.3    Medina, M.4    Nuñez, M.5
  • 79
    • 3142549206 scopus 로고    scopus 로고
    • Colicins and microcins: The next generation antimicrobials
    • Gillor O, Kirkup BC & Riley MA (2004) Colicins and microcins: the next generation antimicrobials. Adv Appl Microbiol 54: 129-146.
    • (2004) Adv Appl Microbiol , vol.54 , pp. 129-146
    • Gillor, O.1    Kirkup, B.C.2    Riley, M.A.3
  • 80
    • 0025608122 scopus 로고
    • An HlyB-type function is required for expression of the Enterococcus faecalis hemolysin/ bacteriocin
    • Gilmore MS, Segarra RA & Booth MC (1990) An HlyB-type function is required for expression of the Enterococcus faecalis hemolysin/ bacteriocin. Infect Immun 58: 3914-3923.
    • (1990) Infect Immun , vol.58 , pp. 3914-3923
    • Gilmore, M.S.1    Segarra, R.A.2    Booth, M.C.3
  • 81
    • 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 (1994) Genetic structure of the Enterococcus faecalis plasmid pAD1-encoded cytolytic toxin system and its relationship to lantibiotic determinants. J Bacteriol 176: 7335-7344.
    • (1994) J Bacteriol , 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
  • 82
    • 0030042458 scopus 로고    scopus 로고
    • Enterococcus faecalis cytolysin and lactocin S of Lactobacillus sake
    • Gilmore MS, Skaugen SK & Nes I (1996) Enterococcus faecalis cytolysin and lactocin S of Lactobacillus sake. Antonie Leeuwenhoek 69: 129-138.
    • (1996) Antonie Leeuwenhoek , vol.69 , pp. 129-138
    • Gilmore, M.S.1    Skaugen, S.K.2    Nes, I.3
  • 83
    • 0036134754 scopus 로고    scopus 로고
    • Trypsin mediates growth phase-dependent transcriptional regulation of genes involved in biosynthesis of ruminococcin A, a lantibiotic produced by a Ruminococcus gnavus strain from a human intestinal microbiota
    • Gomez A, Laridé M, Marcille F & Fons M (2002) Trypsin mediates growth phase-dependent transcriptional regulation of genes involved in biosynthesis of ruminococcin A, a lantibiotic produced by a Ruminococcus gnavus strain from a human intestinal microbiota. J Bacteriol 184: 18-28.
    • (2002) J Bacteriol , vol.184 , pp. 18-28
    • Gomez, A.1    Laridé, M.2    Marcille, F.3    Fons, M.4
  • 84
    • 0015933308 scopus 로고
    • The number and nature of α, β-unsaturated amino acids in subtilin
    • Gross E & Kiltz HH (1973) The number and nature of α, β-unsaturated amino acids in subtilin. Biochem Biophys Res Commun 50: 559-565.
    • (1973) Biochem Biophys Res Commun , vol.50 , pp. 559-565
    • Gross, E.1    Kiltz, H.H.2
  • 85
    • 0015215446 scopus 로고
    • The structure of nisin
    • Gross E & Morell JL (1971) The structure of nisin. J Am Chem Soc 93: 4634-4635.
    • (1971) J Am Chem Soc , vol.93 , pp. 4634-4635
    • Gross, E.1    Morell, J.L.2
  • 86
    • 0033851437 scopus 로고    scopus 로고
    • Posttranslationally modified bacteriocins-the lantibiotics
    • Guder A, Wiedemann I & Sahl HG (2000) Posttranslationally modified bacteriocins-the lantibiotics. Biopolymers 55: 62-73.
    • (2000) Biopolymers , vol.55 , pp. 62-73
    • Guder, A.1    Wiedemann, I.2    Sahl, H.G.3
  • 87
    • 0036136736 scopus 로고    scopus 로고
    • Role of the single regulator MrsR1 and the two-component system MrsR2/K2 in the regulation of mersacidin production and immunity
    • Guder A, Schmitter T, Wiedemann I, Sahl HG & Bierbaum G (2002) Role of the single regulator MrsR1 and the two-component system MrsR2/K2 in the regulation of mersacidin production and immunity. Appl Environ Microbiol 68: 106-113.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 106-113
    • Guder, A.1    Schmitter, T.2    Wiedemann, I.3    Sahl, H.G.4    Bierbaum, G.5
  • 88
    • 20444503846 scopus 로고    scopus 로고
    • Microbial solutions to microbial problems; lactococcal bacteriocins for the control of undesirable biota in food
    • Guinane CM, Cotter PD, Hill C & Ross RP (2005) Microbial solutions to microbial problems; lactococcal bacteriocins for the control of undesirable biota in food. J Appl Microbiol 98: 1316-1325.
    • (2005) J Appl Microbiol , vol.98 , pp. 1316-1325
    • Guinane, C.M.1    Cotter, P.D.2    Hill, C.3    Ross, R.P.4
  • 89
    • 0028144184 scopus 로고
    • Growth phase-dependent regulation and membrane localization of SpaB, a protein involved in biosynthesis of the lantibiotic subtilin
    • Gutowski-Eckel Z, Klein C, Siegers K, Bohm K, Hammelmann M & Entian KD (1994) Growth phase-dependent regulation and membrane localization of SpaB, a protein involved in biosynthesis of the lantibiotic subtilin. Appl Environ Microbiol 60: 1-11.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1-11
    • Gutowski-Eckel, Z.1    Klein, C.2    Siegers, K.3    Bohm, K.4    Hammelmann, M.5    Entian, K.D.6
  • 90
    • 0037011936 scopus 로고    scopus 로고
    • Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction
    • Haas W, Shepard BD & Gilmore MS (2002) Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction. Nature 415: 84-87.
    • (2002) Nature , vol.415 , pp. 84-87
    • Haas, W.1    Shepard, B.D.2    Gilmore, M.S.3
  • 91
    • 4444277132 scopus 로고    scopus 로고
    • Assembly and stability of nisin-lipid II pores
    • Hasper HE, de Kruijff B & Breukink E (2004) Assembly and stability of nisin-lipid II pores. Biochemistry 43: 11567-11575.
    • (2004) Biochemistry , vol.43 , pp. 11567-11575
    • Hasper, H.E.1    de Kruijff, B.2    Breukink, E.3
  • 92
    • 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
    • Håvarstein LS, Holo H & Nes IF (1994) 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) Microbiology , vol.140 , pp. 2383-2389
    • Håvarstein, L.S.1    Holo, H.2    Nes, I.F.3
  • 93
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrate concomitant with export
    • Håvarstein LS, Diep DB & Nes IF (1995) A family of bacteriocin ABC transporters carry out proteolytic processing of their substrate concomitant with export. Mol Microbiol 16: 229-240.
    • (1995) Mol Microbiol , vol.16 , pp. 229-240
    • Håvarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 94
    • 0036589242 scopus 로고    scopus 로고
    • Mode of action of modified and unmodified bacteriocins from Gram-positive bacteria
    • Héchard Y & Sahl HG (2002) Mode of action of modified and unmodified bacteriocins from Gram-positive bacteria. Biochimie 84: 545-557.
    • (2002) Biochimie , vol.84 , pp. 545-557
    • Héchard, Y.1    Sahl, H.G.2
  • 95
    • 0031665461 scopus 로고    scopus 로고
    • Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analysis of its biosynthetic gene cluster
    • Heidrich C, Pag U, Josten M, Metzger JW, Jack RW, Bierbaum G, Jung G & Sahl HG (1998) Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analysis of its biosynthetic gene cluster. Appl Environ Microbiol 64: 3140-3146.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3140-3146
    • Heidrich, C.1    Pag, U.2    Josten, M.3    Metzger, J.W.4    Jack, R.W.5    Bierbaum, G.6    Jung, G.7    Sahl, H.G.8
  • 96
    • 33846851726 scopus 로고    scopus 로고
    • What's in a name? Class distinction for bacteriocins
    • doi:10.1038/nrmicro1273-c1
    • Heng NCK & Tagg JR (2006) What's in a name? Class distinction for bacteriocins. Nat Rev Microbiol 4: 2. doi:10.1038/nrmicro1273-c1.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 2
    • Heng, N.C.K.1    Tagg, J.R.2
  • 97
    • 0035292812 scopus 로고    scopus 로고
    • Dual role of GdmH in producer immunity and secretion of the staphylococcal lantibiotics gallidermin and epidermin
    • Hille M, Kies S, Götz F & Peschel A (2001) Dual role of GdmH in producer immunity and secretion of the staphylococcal lantibiotics gallidermin and epidermin. Appl Environ Microbiol 67: 1380-1383.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1380-1383
    • Hille, M.1    Kies, S.2    Götz, F.3    Peschel, A.4
  • 98
    • 0037313204 scopus 로고    scopus 로고
    • Bacteriocin detection from whole bacteria by matrix-assisted laser desorption ionization-time of flight mass spectrometry
    • Hindré T, Didelot S, Le Pennec J-P, Haras D, Dufour A & Vallée-Réhel K (2003) Bacteriocin detection from whole bacteria by matrix-assisted laser desorption ionization-time of flight mass spectrometry. Appl Environ Microbiol 69: 1051-1058.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 1051-1058
    • Hindré, T.1    Didelot, S.2    Le Pennec, J.-P.3    Haras, D.4    Dufour, A.5    Vallée-Réhel, K.6
  • 99
    • 1342279427 scopus 로고    scopus 로고
    • Regulation of lantibiotic lacticin 481 production at the transcriptional level by acid pH
    • Hindré T, Le Pennec J-P, Haras D & Dufour A (2004) Regulation of lantibiotic lacticin 481 production at the transcriptional level by acid pH. FEMS Microbiol Lett 231: 291-298.
    • (2004) FEMS Microbiol Lett , vol.231 , pp. 291-298
    • Hindré, T.1    Le Pennec, J.-P.2    Haras, D.3    Dufour, A.4
  • 100
    • 2942554929 scopus 로고    scopus 로고
    • Localization and functional analysis of PepI, the immunity peptide of Pep5-producing Staphylococcus epidermidis strain 5
    • Hoffmann A, Schneider T, Pag U & Sahl HG (2004) Localization and functional analysis of PepI, the immunity peptide of Pep5-producing Staphylococcus epidermidis strain 5. Appl Environ Microbiol 70: 3263-3271.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3263-3271
    • Hoffmann, A.1    Schneider, T.2    Pag, U.3    Sahl, H.G.4
  • 101
    • 0037699956 scopus 로고    scopus 로고
    • NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity
    • Hsu ST, Breukink E, Bierbaum G, Sahl HG, de Kruijff B, Kaptein R, van Nuland NA & Bonvin AM (2003) NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity. J Biol Chem 278: 13110-13117.
    • (2003) J Biol Chem , vol.278 , pp. 13110-13117
    • Hsu, S.T.1    Breukink, E.2    Bierbaum, G.3    Sahl, H.G.4    de Kruijff, B.5    Kaptein, R.6    van Nuland, N.A.7    Bonvin, A.M.8
  • 103
    • 0030176383 scopus 로고    scopus 로고
    • Bacteriocin J46, a new bacteriocin produced by Lactococcus lactis subsp. cremoris J46: Isolation and characterization of the protein and its gene
    • Huot E, Meghrous J, Barrena-Gonzalez C & Petitdemange H (1996) Bacteriocin J46, a new bacteriocin produced by Lactococcus lactis subsp. cremoris J46: isolation and characterization of the protein and its gene. Anaerobe 2: 137-145.
    • (1996) Anaerobe , vol.2 , pp. 137-145
    • Huot, E.1    Meghrous, J.2    Barrena-Gonzalez, C.3    Petitdemange, H.4
  • 104
    • 0029438170 scopus 로고
    • A response regulator gene controls production of the lantibiotic streptococcin A-FF22
    • Hynes WL & Ferretti JJ (1995) A response regulator gene controls production of the lantibiotic streptococcin A-FF22. Dev Biol Stand 85: 635-637.
    • (1995) Dev Biol Stand , vol.85 , pp. 635-637
    • Hynes, W.L.1    Ferretti, J.J.2
  • 105
    • 0027246560 scopus 로고
    • Cloning of the gene encoding streptococcin A-FF22, a novel lantibiotic produced by Streptococcus pyogenes, and determination of its nucleotide sequence
    • Hynes WL, Ferretti JJ & Tagg JR (1993) Cloning of the gene encoding streptococcin A-FF22, a novel lantibiotic produced by Streptococcus pyogenes, and determination of its nucleotide sequence. Appl Environ Microbiol 59: 1969-1971.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1969-1971
    • Hynes, W.L.1    Ferretti, J.J.2    Tagg, J.R.3
  • 106
    • 0028036571 scopus 로고
    • Duplication of the lantibiotic structural gene in M-type 49 group A Streptococcus strains producing streptococcin A-M49
    • Hynes WL, Friend VL & Ferretti JJ (1994) Duplication of the lantibiotic structural gene in M-type 49 group A Streptococcus strains producing streptococcin A-M49. Appl Environ Microbiol 60: 4207-4209.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4207-4209
    • Hynes, W.L.1    Friend, V.L.2    Ferretti, J.J.3
  • 107
    • 0025128648 scopus 로고
    • Genetic analysis of the pAD1 hemolysin/bacteriocin determinant in Enterococcus faecalis: Tn917 insertional mutagenesis and cloning
    • Ike Y, Clewell DB, Segarra RA & Gilmore MS (1990) Genetic analysis of the pAD1 hemolysin/bacteriocin determinant in Enterococcus faecalis: Tn917 insertional mutagenesis and cloning. J Bacteriol 172: 155-163.
    • (1990) J Bacteriol , vol.172 , pp. 155-163
    • Ike, Y.1    Clewell, D.B.2    Segarra, R.A.3    Gilmore, M.S.4
  • 108
    • 0028144487 scopus 로고
    • The mode of action of SA-FF22, a lantibiotic isolated from Streptococcus pyogenes strain FF22
    • Jack R, Benz R, Tagg J & Sahl H-G (1994a) The mode of action of SA-FF22, a lantibiotic isolated from Streptococcus pyogenes strain FF22. Eur J Biochem 219: 699-705.
    • (1994) Eur J Biochem , vol.219 , pp. 699-705
    • Jack, R.1    Benz, R.2    Tagg, J.3    Sahl, H.-G.4
  • 109
    • 0028211139 scopus 로고
    • Elucidation of the structure of SA-FF22, a lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22
    • Jack RW, Carne A, Metzger J, Stefanović S, Sahl H-G, Jung G & Tagg J (1994b) Elucidation of the structure of SA-FF22, a lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22. Eur J Biochem 220: 455-462.
    • (1994) Eur J Biochem , vol.220 , pp. 455-462
    • Jack, R.W.1    Carne, A.2    Metzger, J.3    Stefanović, S.4    Sahl, H.-G.5    Jung, G.6    Tagg, J.7
  • 110
    • 0028990155 scopus 로고
    • Bacteriocins of Gram-positive bacteria
    • Jack RW, Tagg JR & Ray B (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
  • 111
    • 0003148144 scopus 로고
    • Lantibiotics: A survey
    • Jung G & Sahl H-G, eds, pp, ESCOM, Leiden
    • Jung G (1991) Lantibiotics: a survey. Nisin and Novel Lantibiotics (Jung G & Sahl H-G, eds), pp. 1-34. ESCOM, Leiden.
    • (1991) Nisin and Novel Lantibiotics , pp. 1-34
    • Jung, G.1
  • 112
    • 0024590316 scopus 로고
    • Nisin, a peptide antibiotic: Cloning and sequencing of the nisA gene and posttranslational processing of its peptide product
    • Kaletta C & Entian KD (1989) Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product. J Bacteriol 171: 1597-1601.
    • (1989) J Bacteriol , vol.171 , pp. 1597-1601
    • Kaletta, C.1    Entian, K.D.2
  • 114
    • 0025831674 scopus 로고
    • Prepeptide sequence of cinnamycin (Ro09-0198): The first structural gene of a duramycin-type lantibiotic
    • Kaletta C, Entian KD & Jung G (1991) Prepeptide sequence of cinnamycin (Ro09-0198): the first structural gene of a duramycin-type lantibiotic. Eur J Biochem 199: 411-415.
    • (1991) Eur J Biochem , vol.199 , pp. 411-415
    • Kaletta, C.1    Entian, K.D.2    Jung, G.3
  • 115
    • 0032901289 scopus 로고    scopus 로고
    • Evidence for production of a new lantibiotic (butyrivibriocin OR79A) by the ruminal anaerobe Butyrivibrio fibrisolvens OR79: Characterization of the structural gene encoding butyrivibriocin OR79A
    • Kalmokoff ML, Lu D, Whitford MF & Teather RM (1999) Evidence for production of a new lantibiotic (butyrivibriocin OR79A) by the ruminal anaerobe Butyrivibrio fibrisolvens OR79: characterization of the structural gene encoding butyrivibriocin OR79A. Appl Environ Microbiol 65: 2128-2135.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2128-2135
    • Kalmokoff, M.L.1    Lu, D.2    Whitford, M.F.3    Teather, R.M.4
  • 117
    • 0038330697 scopus 로고    scopus 로고
    • Control of antimicrobial peptide synthesis by the agr quorum sensing system in Staphylococcus epidermidis: Activity of the lantibiotic epidermin is regulated at the level of precursor peptide processing
    • Kies S, Vuong C, Hille M, Peschel A, Meyer C, Götz F & Otto M (2003) Control of antimicrobial peptide synthesis by the agr quorum sensing system in Staphylococcus epidermidis: activity of the lantibiotic epidermin is regulated at the level of precursor peptide processing. Peptides 24: 329-338.
    • (2003) Peptides , vol.24 , pp. 329-338
    • Kies, S.1    Vuong, C.2    Hille, M.3    Peschel, A.4    Meyer, C.5    Götz, F.6    Otto, M.7
  • 119
    • 0031171919 scopus 로고    scopus 로고
    • A bacteriocin of strain Pediococcus sp. ISK-1 isolated from Nukadoko, bed of fermented rice bran
    • Kimura H, Nagano R, Matsusaki H, Sonomoto K & Ishizaki A (1997) A bacteriocin of strain Pediococcus sp. ISK-1 isolated from Nukadoko, bed of fermented rice bran. Biosci Biotech Biochem 61: 1049-1051.
    • (1997) Biosci Biotech Biochem , vol.61 , pp. 1049-1051
    • Kimura, H.1    Nagano, R.2    Matsusaki, H.3    Sonomoto, K.4    Ishizaki, A.5
  • 120
    • 0001288165 scopus 로고    scopus 로고
    • Purification and partial identification of bacteriocin ISK-1, a new lantibiotic produced by Pediococcus sp. ISK-1
    • Kimura H, Matsusaki H, Sashihara T, Sonomoto K & Ishizaki A (1998) Purification and partial identification of bacteriocin ISK-1, a new lantibiotic produced by Pediococcus sp. ISK-1. Biosci Biotechnol Biochem 62: 2341-2345.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 2341-2345
    • Kimura, H.1    Matsusaki, H.2    Sashihara, T.3    Sonomoto, K.4    Ishizaki, A.5
  • 121
    • 0023926266 scopus 로고
    • Bacteriocins of lactic acid bacteria
    • Klaenhammer TR (1988) Bacteriocins of lactic acid bacteria. Biochimie 70: 337-349.
    • (1988) Biochimie , vol.70 , pp. 337-349
    • Klaenhammer, T.R.1
  • 122
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer TR (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
  • 123
    • 4544251455 scopus 로고    scopus 로고
    • Quorum sensing control of lantibiotic production; nisin and subtilin autoregulate their own biosynthesis
    • Kleerebezem M (2004) Quorum sensing control of lantibiotic production; nisin and subtilin autoregulate their own biosynthesis. Peptides 25: 1405-1414.
    • (2004) Peptides , vol.25 , pp. 1405-1414
    • Kleerebezem, M.1
  • 124
    • 0034832026 scopus 로고    scopus 로고
    • Peptide pheromone-dependent regulation of antimicrobial peptide production in Gram-positive bacteria: A case of multicellular behaviour
    • Kleerebezem M & Quadri LE (2001) Peptide pheromone-dependent regulation of antimicrobial peptide production in Gram-positive bacteria: a case of multicellular behaviour. Peptides 22: 1579-1596.
    • (2001) Peptides , vol.22 , pp. 1579-1596
    • Kleerebezem, M.1    Quadri, L.E.2
  • 125
    • 0030721749 scopus 로고    scopus 로고
    • Controlled gene expression systems for lactic acid bacteria: Transferable nisin-inducible expression cassettes for Lactococcus, Leuconostoc and Lactobacillus ssp
    • Kleerebezem M, Beerthuyzen MM, Vaughan EE, de Vos WM & Kuipers OP (1997) Controlled gene expression systems for lactic acid bacteria: transferable nisin-inducible expression cassettes for Lactococcus, Leuconostoc and Lactobacillus ssp. Appl Environ Microbiol 63: 4581-4584.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4581-4584
    • Kleerebezem, M.1    Beerthuyzen, M.M.2    Vaughan, E.E.3    de Vos, W.M.4    Kuipers, O.P.5
  • 126
    • 0028037950 scopus 로고
    • Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633
    • Klein C & Entian KD (1994) Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633. Appl Environ Microbiol 60: 2793-2801.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2793-2801
    • Klein, C.1    Entian, K.D.2
  • 127
    • 0026530785 scopus 로고
    • Analysis of genes involved in biosynthesis of the lantibiotic subtilin
    • Klein C, Kaletta C, Schnell N & Entian KD (1992) Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Appl Environ Microbiol 58: 132-142.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 132-142
    • Klein, C.1    Kaletta, C.2    Schnell, N.3    Entian, K.D.4
  • 128
    • 0027392580 scopus 로고
    • Biosynthesis of the lantibiotic subtilin is regulated by a histidine kinase/response regulator system
    • Klein C, Kaletta C & Entian KD (1993) Biosynthesis of the lantibiotic subtilin is regulated by a histidine kinase/response regulator system. Appl Environ Microbiol 59: 296-303.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 296-303
    • Klein, C.1    Kaletta, C.2    Entian, K.D.3
  • 130
    • 0036855378 scopus 로고    scopus 로고
    • NisB is required for the dehydration and NisC for the lanthionine formation in the post-translational modification of nisin
    • Koponen O, Tolonen M, Qiao M, Wahlström G, Helin J & Saris PEJ (2002) NisB is required for the dehydration and NisC for the lanthionine formation in the post-translational modification of nisin. Microbiology 148: 3561-3568.
    • (2002) Microbiology , vol.148 , pp. 3561-3568
    • Koponen, O.1    Tolonen, M.2    Qiao, M.3    Wahlström, G.4    Helin, J.5    Saris, P.E.J.6
  • 133
    • 0027162304 scopus 로고
    • Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity
    • Kuipers OP, Beerthuyzen MM, Siezen RJ & de Vos WM (1993) Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity. Eur J Biochem 216: 281-291.
    • (1993) Eur J Biochem , vol.216 , pp. 281-291
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3    de Vos, W.M.4
  • 136
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • Kuipers A, de Boef E, Rink R, Fekken S, Kluskens LD, Driessen AJM, Leenhouts K, Kuipers OP & Moll GN (2004) NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides. J Biol Chem 279: 22176-22182.
    • (2004) J Biol Chem , vol.279 , pp. 22176-22182
    • Kuipers, A.1    de Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.M.6    Leenhouts, K.7    Kuipers, O.P.8    Moll, G.N.9
  • 137
    • 0029864280 scopus 로고    scopus 로고
    • Expression, purification and characterization of EpiC, an enzyme involved in the biosynthesis of the lantibiotic epidermin, and sequence analysis of Staphylococcus epidermidis epiC mutants
    • Kupke T & Götz F (1996) Expression, purification and characterization of EpiC, an enzyme involved in the biosynthesis of the lantibiotic epidermin, and sequence analysis of Staphylococcus epidermidis epiC mutants. J Bacteriol 178: 1335-1340.
    • (1996) J Bacteriol , vol.178 , pp. 1335-1340
    • Kupke, T.1    Götz, F.2
  • 138
    • 0031040532 scopus 로고    scopus 로고
    • The enethiolate anion reaction products of EpiD. pKa value of the enethiol side chain is lower than that of the thiol side chain of peptides
    • Kupke T & Götz F (1997) The enethiolate anion reaction products of EpiD. pKa value of the enethiol side chain is lower than that of the thiol side chain of peptides. J Biol Chem 272: 4759-4762.
    • (1997) J Biol Chem , vol.272 , pp. 4759-4762
    • Kupke, T.1    Götz, F.2
  • 139
    • 0028142446 scopus 로고
    • Mass spectroscopic analysis of a novel enzymatic reaction. Oxidative decarboxylation of the lantibiotic precursor peptide EpiA catalyzed by the flavoprotein EpiD
    • Kupke T, Kempter C, Gnau V, Jung G & Götz F (1994) Mass spectroscopic analysis of a novel enzymatic reaction. Oxidative decarboxylation of the lantibiotic precursor peptide EpiA catalyzed by the flavoprotein EpiD. J Biol Chem 269: 5653-5659.
    • (1994) J Biol Chem , vol.269 , pp. 5653-5659
    • Kupke, T.1    Kempter, C.2    Gnau, V.3    Jung, G.4    Götz, F.5
  • 140
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • Li B, Yu JPJ, Brunzelle JS, Moll GN, van der Donk WA & Nair SK (2006) Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science 311: 1464-1467.
    • (2006) Science , vol.311 , pp. 1464-1467
    • Li, B.1    Yu, J.P.J.2    Brunzelle, J.S.3    Moll, G.N.4    van der Donk, W.A.5    Nair, S.K.6
  • 141
    • 0037379390 scopus 로고    scopus 로고
    • The stress-responsive dgk gene from Streptococcus mutans encodes a putative undecaprenol kinase activity
    • Lis M & Kuramitsu HK (2003) The stress-responsive dgk gene from Streptococcus mutans encodes a putative undecaprenol kinase activity. Infect Immun 71: 1938-1943.
    • (2003) Infect Immun , vol.71 , pp. 1938-1943
    • Lis, M.1    Kuramitsu, H.K.2
  • 142
    • 0026491208 scopus 로고
    • Enhancement of the chemical and antimicrobial properties of subtilin by site-directed mutagenesis
    • Liu W & Hansen JN (1992) Enhancement of the chemical and antimicrobial properties of subtilin by site-directed mutagenesis. J Biol Chem 267: 25078-25085.
    • (1992) J Biol Chem , vol.267 , pp. 25078-25085
    • Liu, W.1    Hansen, J.N.2
  • 143
    • 0032931983 scopus 로고    scopus 로고
    • Molecular characterization of the pH-inducible and growth phase-dependent promoter P170 of Lactococcus lactis
    • Madsen SM, Arnau J, Vrang A, Givskov M & Israelsen H (1999) Molecular characterization of the pH-inducible and growth phase-dependent promoter P170 of Lactococcus lactis. Mol Microbiol 32: 75-87.
    • (1999) Mol Microbiol , vol.32 , pp. 75-87
    • Madsen, S.M.1    Arnau, J.2    Vrang, A.3    Givskov, M.4    Israelsen, H.5
  • 144
    • 17644397319 scopus 로고    scopus 로고
    • Two acid-inducible promoters from Lactococcus lactis require the cis-acting ACiD-box and the transcription regulator RcfB
    • Madsen SM, Hindré T, Le Pennec JP, Israelsen H & Dufour A (2005) Two acid-inducible promoters from Lactococcus lactis require the cis-acting ACiD-box and the transcription regulator RcfB. Mol Microbiol 56: 735-746.
    • (2005) Mol Microbiol , vol.56 , pp. 735-746
    • Madsen, S.M.1    Hindré, T.2    Le Pennec, J.P.3    Israelsen, H.4    Dufour, A.5
  • 145
    • 0036178887 scopus 로고    scopus 로고
    • The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin
    • Majer F, Schmid DG, Altena K, Bierbaum G & Kupke T (2002) The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidin. J Bacteriol 184: 1234-1243.
    • (2002) J Bacteriol , vol.184 , pp. 1234-1243
    • Majer, F.1    Schmid, D.G.2    Altena, K.3    Bierbaum, G.4    Kupke, T.5
  • 146
    • 0037474279 scopus 로고    scopus 로고
    • Cinnamycin (Ro 09-0198) promotes cell binding and toxicity by inducing transbilayer lipid movement
    • Makino A, Baba T, Fujimoto K et al. (2003) Cinnamycin (Ro 09-0198) promotes cell binding and toxicity by inducing transbilayer lipid movement. J Biol Chem 278: 3204-3209.
    • (2003) J Biol Chem , vol.278 , pp. 3204-3209
    • Makino, A.1    Baba, T.2    Fujimoto, K.3
  • 147
    • 0036300803 scopus 로고    scopus 로고
    • Distribution of genes encoding the trypsin-dependent lantibiotic ruminococcin A among bacteria isolated from human fecal microbiota
    • Marcille F, Gomez A, Joubert P, Ladiré M, Veau G, Clara A, Gavini F, Willems A & Fons M (2002) Distribution of genes encoding the trypsin-dependent lantibiotic ruminococcin A among bacteria isolated from human fecal microbiota. Appl Environ Microbiol 68: 3424-3431.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3424-3431
    • Marcille, F.1    Gomez, A.2    Joubert, P.3    Ladiré, M.4    Veau, G.5    Clara, A.6    Gavini, F.7    Willems, A.8    Fons, M.9
  • 149
    • 0031890703 scopus 로고    scopus 로고
    • Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential
    • McAuliffe O, Ryan MP, Ross RP, Hill C, Breeuwer P & Abee T (1998) Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential. Appl Environ Microbiol 64: 439-445.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 439-445
    • McAuliffe, O.1    Ryan, M.P.2    Ross, R.P.3    Hill, C.4    Breeuwer, P.5    Abee, T.6
  • 150
    • 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 (2000a) Each peptide of the two-component lantibiotic lacticin 3147 requires a separate modification enzyme for activity. Microbiology 146: 2147-2154.
    • (2000) Microbiology , vol.146 , pp. 2147-2154
    • McAuliffe, O.1    Hill, C.2    Ross, R.P.3
  • 151
    • 0033967119 scopus 로고    scopus 로고
    • Identification and overexpression of ltnI, a novel gene which confers immunity to the two-component lantibiotic lacticin 3147
    • McAuliffe O, Hill C & Ross RP (2000b) Identification and overexpression of ltnI, a novel gene which confers immunity to the two-component lantibiotic lacticin 3147. Microbiology 146: 129-138.
    • (2000) Microbiology , vol.146 , pp. 129-138
    • McAuliffe, O.1    Hill, C.2    Ross, R.P.3
  • 152
    • 0035004672 scopus 로고    scopus 로고
    • Lantibiotics: Structure, biosynthesis and mode of action
    • McAuliffe O, Ross RP & Hill C (2001a) Lantibiotics: structure, biosynthesis and mode of action. FEMS Microbiol Rev 25: 285-308.
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 285-308
    • McAuliffe, O.1    Ross, R.P.2    Hill, C.3
  • 153
    • 0035110702 scopus 로고    scopus 로고
    • Regulation of immunity to the two-component lantibiotic, lacticin 3147, by the transcriptional repressor LtnR
    • McAuliffe O, O'Keeffe T, Hill C & Ross RP (2001b) Regulation of immunity to the two-component lantibiotic, lacticin 3147, by the transcriptional repressor LtnR. Mol Microbiol 39: 982-993.
    • (2001) Mol Microbiol , vol.39 , pp. 982-993
    • McAuliffe, O.1    O'Keeffe, T.2    Hill, C.3    Ross, R.P.4
  • 154
    • 0032782007 scopus 로고    scopus 로고
    • Nucleotide sequence of the streptococcin A-FF22 lantibiotic regulon: Model for production of the lantibiotic SA-FF22 by strains of Streptococcus pyogenes
    • McLaughlin RE, Ferretti JJ & Hynes WL (1999) Nucleotide sequence of the streptococcin A-FF22 lantibiotic regulon: model for production of the lantibiotic SA-FF22 by strains of Streptococcus pyogenes. FEMS Microbiol Lett 175: 171-177.
    • (1999) FEMS Microbiol Lett , vol.175 , pp. 171-177
    • McLaughlin, R.E.1    Ferretti, J.J.2    Hynes, W.L.3
  • 155
    • 0029115380 scopus 로고
    • Nucleotide sequence of the lantibiotic Pep5 biosynthesis gene cluster and functional analysis of PepP and PepC: Evidence for a role of PepC in thioether formation
    • Meyer C, Bierbaum G, Heidrich C, Reis M, Suling J, Iglesias-Wind MI, Kempter C, Molitor E & Sahl HG (1995) Nucleotide sequence of the lantibiotic Pep5 biosynthesis gene cluster and functional analysis of PepP and PepC: evidence for a role of PepC in thioether formation. Eur J Biochem 232: 478-489.
    • (1995) Eur J Biochem , vol.232 , pp. 478-489
    • Meyer, C.1    Bierbaum, G.2    Heidrich, C.3    Reis, M.4    Suling, J.5    Iglesias-Wind, M.I.6    Kempter, C.7    Molitor, E.8    Sahl, H.G.9
  • 156
    • 32244446657 scopus 로고    scopus 로고
    • The dehydratase activity of lacticin 481 synthetase is highly processive
    • Miller LM, Chatterjee C, van der Donk WA & Kelleher NL (2006) The dehydratase activity of lacticin 481 synthetase is highly processive. J Am Chem Soc 128: 1420-1421.
    • (2006) J Am Chem Soc , vol.128 , pp. 1420-1421
    • Miller, L.M.1    Chatterjee, C.2    van der Donk, W.A.3    Kelleher, N.L.4
  • 157
    • 0036165901 scopus 로고    scopus 로고
    • Use of lacticin 481 to facilitate delivery of the bacteriophage resistance plasmid, pCBG104 to cheese starters
    • Mills S, Coffey A, O'Sullivan L, Strokes D, Hill C, Fitzgerald GF & Ross RP (2002) Use of lacticin 481 to facilitate delivery of the bacteriophage resistance plasmid, pCBG104 to cheese starters. J Appl Microbiol 92: 238-246.
    • (2002) J Appl Microbiol , vol.92 , pp. 238-246
    • Mills, S.1    Coffey, A.2    O'Sullivan, L.3    Strokes, D.4    Hill, C.5    Fitzgerald, G.F.6    Ross, R.P.7
  • 159
    • 23844460885 scopus 로고    scopus 로고
    • Purification and characterization of warnericin RB4, anti-Alicyclobacillus bacteriocin, produced by Staphylococcus warneri RB4
    • Minamikawa M, Kawai Y, Inoue N & Yamazaki K (2005) Purification and characterization of warnericin RB4, anti-Alicyclobacillus bacteriocin, produced by Staphylococcus warneri RB4. Curr Microbiol 51: 22-26.
    • (2005) Curr Microbiol , vol.51 , pp. 22-26
    • Minamikawa, M.1    Kawai, Y.2    Inoue, N.3    Yamazaki, K.4
  • 160
    • 21444431674 scopus 로고    scopus 로고
    • Sequential actions of the two component peptides of the lantibiotic 3147 explain its antimicrobial activity at nanomolar concentrations
    • Morgan SM, O'Connor PM, Cotter PD, Ross RP & Hill C (2005) Sequential actions of the two component peptides of the lantibiotic 3147 explain its antimicrobial activity at nanomolar concentrations. Antimicrob Agents Chemother 49: 2606-2611.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2606-2611
    • Morgan, S.M.1    O'Connor, P.M.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 162
    • 24644468692 scopus 로고    scopus 로고
    • Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli
    • Nagao J, Harada Y, Shioya K, Aso Y, Zendo T, Nakayama J & Sonomoto K (2005b) Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli. Biochem Biophys Res Commun 336: 507-513.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 507-513
    • Nagao, J.1    Harada, Y.2    Shioya, K.3    Aso, Y.4    Zendo, T.5    Nakayama, J.6    Sonomoto, K.7
  • 163
    • 0038480005 scopus 로고    scopus 로고
    • Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution
    • Nakagawa I, Kurokawa K, Yamashita A et al. (2003) Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution. Genome Res 13: 1042-1055.
    • (2003) Genome Res , vol.13 , pp. 1042-1055
    • Nakagawa, I.1    Kurokawa, K.2    Yamashita, A.3
  • 165
    • 0028306988 scopus 로고
    • Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans
    • Novák J, Caufield PW & Miller EJ (1994) Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans. J Bacteriol 176: 4316-4320.
    • (1994) J Bacteriol , vol.176 , pp. 4316-4320
    • Novák, J.1    Caufield, P.W.2    Miller, E.J.3
  • 166
    • 0036165760 scopus 로고    scopus 로고
    • Halocins and sulfolobicins: The emerging story of archaeal protein and peptide antibiotics
    • O'Connor EM & Shand RF (2002) Halocins and sulfolobicins: the emerging story of archaeal protein and peptide antibiotics. J Ind Microbiol Biotechnol 28: 23-31.
    • (2002) J Ind Microbiol Biotechnol , vol.28 , pp. 23-31
    • O'Connor, E.M.1    Shand, R.F.2
  • 167
    • 0344823660 scopus 로고    scopus 로고
    • SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins
    • Okeley NM, Paul M, Stasser JP, Blackburn N & van der Donk WA (2003) SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins. Biochemistry 42: 13613-13624.
    • (2003) Biochemistry , vol.42 , pp. 13613-13624
    • Okeley, N.M.1    Paul, M.2    Stasser, J.P.3    Blackburn, N.4    van der Donk, W.A.5
  • 168
    • 23744455185 scopus 로고    scopus 로고
    • Characterization of functional domains of lantibiotic-binding immunity protein, NukH, from Staphylococcus warneri ISK-1
    • Okuda K, Aso Y, Nagao J, Shioya K, Kanemasa Y, Nakayama J & Sonomoto K (2005) Characterization of functional domains of lantibiotic-binding immunity protein, NukH, from Staphylococcus warneri ISK-1. FEMS Microbiol Lett 250: 19-25.
    • (2005) FEMS Microbiol Lett , vol.250 , pp. 19-25
    • Okuda, K.1    Aso, Y.2    Nagao, J.3    Shioya, K.4    Kanemasa, Y.5    Nakayama, J.6    Sonomoto, K.7
  • 169
    • 0035122347 scopus 로고    scopus 로고
    • The application of a fermented food ingredient containing 'variacin', a novel antimicrobial produced by Kocuria varians, to control the growth of Bacillus cereus in chilled dairy products
    • O'Mahony T, Rekhif N, Cavadini C & Fitzgerald GF (2001) The application of a fermented food ingredient containing 'variacin', a novel antimicrobial produced by Kocuria varians, to control the growth of Bacillus cereus in chilled dairy products. J Appl Microbiol 90: 106-114.
    • (2001) J Appl Microbiol , vol.90 , pp. 106-114
    • O'Mahony, T.1    Rekhif, N.2    Cavadini, C.3    Fitzgerald, G.F.4
  • 170
    • 0036725885 scopus 로고    scopus 로고
    • Elevated enzyme release from lactococcal starter cultures on exposure to the lantibiotic lacticin 481, produced by Lactococcus lactis DPC5552
    • O'Sullivan L, Morgan SM, Ross RP & Hill C (2002) Elevated enzyme release from lactococcal starter cultures on exposure to the lantibiotic lacticin 481, produced by Lactococcus lactis DPC5552. J Dairy Sci 85: 2130-2140.
    • (2002) J Dairy Sci , vol.85 , pp. 2130-2140
    • O'Sullivan, L.1    Morgan, S.M.2    Ross, R.P.3    Hill, C.4
  • 171
    • 0345599202 scopus 로고    scopus 로고
    • A lacticin 481-producing adjunct cultures increases starter lysis while inhibiting non-starter lactic acid bacteria proliferation during Cheddar cheese ripening
    • O'Sullivan L, Ross RP & Hill C (2003a) A lacticin 481-producing adjunct cultures increases starter lysis while inhibiting non-starter lactic acid bacteria proliferation during Cheddar cheese ripening. J Appl Microbiol 95: 1235-1241.
    • (2003) J Appl Microbiol , vol.95 , pp. 1235-1241
    • O'Sullivan, L.1    Ross, R.P.2    Hill, C.3
  • 172
    • 0037640011 scopus 로고    scopus 로고
    • Generation of food-grade lactococcal starters which produce the lantibiotics lacticin 3147 and lacticin 481
    • O'Sullivan L, Ryan MP, Ross RP & Hill C (2003b) Generation of food-grade lactococcal starters which produce the lantibiotics lacticin 3147 and lacticin 481. Appl Environ Microbiol 69: 3681-3685.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3681-3685
    • O'Sullivan, L.1    Ryan, M.P.2    Ross, R.P.3    Hill, C.4
  • 174
    • 0032529910 scopus 로고    scopus 로고
    • Producer self-protection against the lantibiotic epidermin by the ABC transporter EpiFEG of Staphylococcus epidermidis Tu3298
    • Otto M, Peschel A & Götz F (1998) Producer self-protection against the lantibiotic epidermin by the ABC transporter EpiFEG of Staphylococcus epidermidis Tu3298. FEMS Microbiol Lett 166: 203-211.
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 203-211
    • Otto, M.1    Peschel, A.2    Götz, F.3
  • 175
    • 0035143188 scopus 로고    scopus 로고
    • The effects of cultivating lactic starter cultures with bacteriocin-producing lactic acid bacteria
    • Oumer A, Garde S, Gaya P, Medina M & Nuñez M (2001) The effects of cultivating lactic starter cultures with bacteriocin-producing lactic acid bacteria. J Food Prot 64: 81-86.
    • (2001) J Food Prot , vol.64 , pp. 81-86
    • Oumer, A.1    Garde, S.2    Gaya, P.3    Medina, M.4    Nuñez, M.5
  • 176
    • 0032974997 scopus 로고    scopus 로고
    • Molecular analysis of expression of the lantibiotic Pep5 immunity phenotype
    • Pag U, Heidrich C, Bierbaum G & Sahl HG (1999) Molecular analysis of expression of the lantibiotic Pep5 immunity phenotype. Appl Environ Microbiol 65: 591-598.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 591-598
    • Pag, U.1    Heidrich, C.2    Bierbaum, G.3    Sahl, H.G.4
  • 179
    • 0025228365 scopus 로고
    • Preliminary characterization of four bacteriocins from Streptococcus mutans
    • Parrot M, Caufield PW & Lavoie MC (1990) Preliminary characterization of four bacteriocins from Streptococcus mutans. Can J Microbiol 36: 123-130.
    • (1990) Can J Microbiol , vol.36 , pp. 123-130
    • Parrot, M.1    Caufield, P.W.2    Lavoie, M.C.3
  • 180
    • 25144458128 scopus 로고    scopus 로고
    • New developments in lantibiotic biosynthesis and mode of action
    • Patton GC & van der Donk WA (2005) New developments in lantibiotic biosynthesis and mode of action. Curr Opin Microbiol 8: 543-551.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 543-551
    • Patton, G.C.1    van der Donk, W.A.2
  • 181
    • 0030058860 scopus 로고    scopus 로고
    • Analysis of the Staphylococcus epidermidis genes epiF, -E, and -G involved in epidermin immunity
    • Peschel A & Götz F (1996) Analysis of the Staphylococcus epidermidis genes epiF, -E, and -G involved in epidermin immunity. J Bacteriol 178: 531-536.
    • (1996) J Bacteriol , vol.178 , pp. 531-536
    • Peschel, A.1    Götz, F.2
  • 183
    • 0030983728 scopus 로고    scopus 로고
    • Secretion of the lantibiotics epidermin and gallidermin: Sequence analysis of the genes gdmT and gdmH, their influence on epidermin production and their regulation by EpiQ
    • Peschel A, Schnell N, Hille M, Entian KD & Götz F (1997) Secretion of the lantibiotics epidermin and gallidermin: sequence analysis of the genes gdmT and gdmH, their influence on epidermin production and their regulation by EpiQ. Mol Gen Genet 254: 312-318.
    • (1997) Mol Gen Genet , vol.254 , pp. 312-318
    • Peschel, A.1    Schnell, N.2    Hille, M.3    Entian, K.D.4    Götz, F.5
  • 185
    • 0026543167 scopus 로고
    • Purification and partial characterization of lacticin 481, a lanthionine-containing bacteriocin produced by Lactococcus lactis subsp. lactis CNRZ 481
    • Piard J-C, Muriana PM, Desmazeaud MJ & Klaenhammer TR (1992) Purification and partial characterization of lacticin 481, a lanthionine-containing bacteriocin produced by Lactococcus lactis subsp. lactis CNRZ 481. Appl Environ Microbiol 58: 279-284.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 279-284
    • Piard, J.-C.1    Muriana, P.M.2    Desmazeaud, M.J.3    Klaenhammer, T.R.4
  • 186
    • 0027290908 scopus 로고
    • Conjugal transfer of the determinants for bacteriocin (lacticin 481) production and immunity in Lactococcus lactis subsp. lactis CNRZ 481
    • Piard J-C, Delorme C, Novel M, Desmazeaud M & Novel G (1993a) Conjugal transfer of the determinants for bacteriocin (lacticin 481) production and immunity in Lactococcus lactis subsp. lactis CNRZ 481. FEMS Microbiol Lett 112: 313-318.
    • (1993) FEMS Microbiol Lett , vol.112 , pp. 313-318
    • Piard, J.-C.1    Delorme, C.2    Novel, M.3    Desmazeaud, M.4    Novel, G.5
  • 187
    • 0027327107 scopus 로고
    • Structure, organization, and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis
    • Piard J-C, Kuipers OP, Rollema HS, Desmazeaud MJ & de Vos WM (1993b) Structure, organization, and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis. J Biol Chem 268: 16361-16368.
    • (1993) J Biol Chem , vol.268 , pp. 16361-16368
    • Piard, J.-C.1    Kuipers, O.P.2    Rollema, H.S.3    Desmazeaud, M.J.4    de Vos, W.M.5
  • 188
    • 0034485941 scopus 로고    scopus 로고
    • Efficacy of four conjugal lactococcal phage resistance plasmids against phage in commercial Lactococcus lactis subsp. cremoris cheese starter strains
    • Pillidge CJ, Collins LJ, Ward LJH, Cantillon BM, Shaw BD, Timmins MJ, Heap HA & Polzin KM (2000) Efficacy of four conjugal lactococcal phage resistance plasmids against phage in commercial Lactococcus lactis subsp. cremoris cheese starter strains. Int Dairy J 10: 617-625.
    • (2000) Int Dairy J , vol.10 , pp. 617-625
    • Pillidge, C.J.1    Collins, L.J.2    Ward, L.J.H.3    Cantillon, B.M.4    Shaw, B.D.5    Timmins, M.J.6    Heap, H.A.7    Polzin, K.M.8
  • 189
    • 0029974631 scopus 로고    scopus 로고
    • Variacin, a new lanthionine-containing bacteriocin produced by Micrococcus varians: Comparison to lacticin 481 of Lactococcus lactis
    • Pridmore D, Rekhif N, Pittet A-C, Suri B & Mollet B (1996) Variacin, a new lanthionine-containing bacteriocin produced by Micrococcus varians: comparison to lacticin 481 of Lactococcus lactis. Appl Environ Microbiol 62: 1799-1802.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1799-1802
    • Pridmore, D.1    Rekhif, N.2    Pittet, A.-C.3    Suri, B.4    Mollet, B.5
  • 190
    • 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 (1999) Functional analyses of the promoters in the lantibiotic mutacin II biosynthetic locus in Streptococcus mutans. Appl Environ Microbiol 65: 652-658.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 652-658
    • Qi, F.1    Chen, P.2    Caufield, P.W.3
  • 191
    • 0029094989 scopus 로고
    • The cellular location and effect on nisin immunity of the NisI protein from Lactococcus lactis N8 expressed in Escherichia coli and L. lactis
    • Qiao M, Immonen T, Koponen O & Saris PEJ (1995) The cellular location and effect on nisin immunity of the NisI protein from Lactococcus lactis N8 expressed in Escherichia coli and L. lactis. FEMS Microbiol Lett 131: 75-80.
    • (1995) FEMS Microbiol Lett , vol.131 , pp. 75-80
    • Qiao, M.1    Immonen, T.2    Koponen, O.3    Saris, P.E.J.4
  • 192
    • 0027209995 scopus 로고
    • Trypsin-dependent production of an antibacterial substance by a human Peptostreptococcus strain in gnotobiotic rats and in vitro
    • Ramare F, Nicoli J, Dabard J, Corring T, Ladire M, Gueugneau AM & Raibaud P (1993) Trypsin-dependent production of an antibacterial substance by a human Peptostreptococcus strain in gnotobiotic rats and in vitro. Appl Environ Microbiol 59: 2876-2883.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2876-2883
    • Ramare, F.1    Nicoli, J.2    Dabard, J.3    Corring, T.4    Ladire, M.5    Gueugneau, A.M.6    Raibaud, P.7
  • 193
    • 0036589212 scopus 로고    scopus 로고
    • LasX, a transcriptional regulator of the lactocin S biosynthetic genes in Lactobacillus sakei L45, acts both as an activator and a repressor
    • Rawlinson EL, Nes IF & Skaugen M (2002) LasX, a transcriptional regulator of the lactocin S biosynthetic genes in Lactobacillus sakei L45, acts both as an activator and a repressor. Biochimie 84: 559-567.
    • (2002) Biochimie , vol.84 , pp. 559-567
    • Rawlinson, E.L.1    Nes, I.F.2    Skaugen, M.3
  • 194
    • 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 (2005) Identification of the DNA-binding site of the Rgg-like regulator LasX within the lactocin S promoter region. Microbiology 151: 813-823.
    • (2005) Microbiology , vol.151 , pp. 813-823
    • Rawlinson, E.L.1    Nes, I.F.2    Skaugen, M.3
  • 195
    • 0027931272 scopus 로고
    • Producer immunity towards the lantibiotic Pep5: Identification of the immunity gene pepI and localization and functional analysis of its gene product
    • Reis M, Eschbach-Bludau M, Iglesias-Wind MI, Kupke T & Sahl HG (1994) Producer immunity towards the lantibiotic Pep5: identification of the immunity gene pepI and localization and functional analysis of its gene product. Appl Environ Microbiol 60: 2876-2883.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2876-2883
    • Reis, M.1    Eschbach-Bludau, M.2    Iglesias-Wind, M.I.3    Kupke, T.4    Sahl, H.G.5
  • 197
    • 0036589206 scopus 로고    scopus 로고
    • Bacteriocin diversity: Ecological and evolutionary perspectives
    • Riley MA & Wertz JE (2002) Bacteriocin diversity: ecological and evolutionary perspectives. Biochimie 84: 357-364.
    • (2002) Biochimie , vol.84 , pp. 357-364
    • Riley, M.A.1    Wertz, J.E.2
  • 198
    • 0028293918 scopus 로고
    • Cloning, expression, and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from Lactococcus lactis subsp. lactis
    • Rincé A, Dufour A, Le Pogam S, Thuault D, Bourgeois CM & Le Pennec J-P (1994) Cloning, expression, and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from Lactococcus lactis subsp. lactis. Appl Environ Microbiol 60: 1652-1657.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1652-1657
    • Rincé, A.1    Dufour, A.2    Le Pogam, S.3    Thuault, D.4    Bourgeois, C.M.5    Le Pennec, J.-P.6
  • 199
    • 0030712222 scopus 로고    scopus 로고
    • Characterization of the lacticin 481 operon: The Lactococcus lactis genes lctF, lctE, and lctG encode a putative ABC transporter involved in bacteriocin immunity
    • Rincé A, Dufour A, Uguen P, Le Pennec J-P & Haras D (1997) Characterization of the lacticin 481 operon: the Lactococcus lactis genes lctF, lctE, and lctG encode a putative ABC transporter involved in bacteriocin immunity. Appl Environ Microbiol 63: 4252-4260.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4252-4260
    • Rincé, A.1    Dufour, A.2    Uguen, P.3    Le Pennec, J.-P.4    Haras, D.5
  • 200
  • 201
    • 0039205887 scopus 로고    scopus 로고
    • Diversity of bacteriocins produced by lactic acid bacteria isolated from raw milk
    • Rodríguez E, González B, Gaya P, Nuñez M & Medina M (2000) Diversity of bacteriocins produced by lactic acid bacteria isolated from raw milk. Int Dairy J 10: 7-15.
    • (2000) Int Dairy J , vol.10 , pp. 7-15
    • Rodríguez, E.1    González, B.2    Gaya, P.3    Nuñez, M.4    Medina, M.5
  • 202
    • 22144435219 scopus 로고    scopus 로고
    • Combined effect of high-pressure treatments and bacteriocin-producing lactic acid bacteria on the inactivation of Escherichia coli O157:H7 in raw-milk cheese
    • Rodriguez E, Arques JL, Nuñez M, Gaya P & Medina M (2005) Combined effect of high-pressure treatments and bacteriocin-producing lactic acid bacteria on the inactivation of Escherichia coli O157:H7 in raw-milk cheese. Appl Environ Microbiol 71: 3399-3404.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3399-3404
    • Rodriguez, E.1    Arques, J.L.2    Nuñez, M.3    Gaya, P.4    Medina, M.5
  • 203
    • 0029093410 scopus 로고
    • Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering
    • Rollema HS, Kuipers OP, Both P, de Vos WM & Siezen RJ (1995) Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering. Appl Environ Microbiol 61: 2873-2878.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2873-2878
    • Rollema, H.S.1    Kuipers, O.P.2    Both, P.3    de Vos, W.M.4    Siezen, R.J.5
  • 204
    • 0027279657 scopus 로고
    • Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3
    • Ross KF, Ronson CW & Tagg JR (1993) Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3. Appl Environ Microbiol 59: 2014-2021.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2014-2021
    • Ross, K.F.1    Ronson, C.W.2    Tagg, J.R.3
  • 205
    • 0037113945 scopus 로고    scopus 로고
    • Preservation and fermentation: Past, present and future
    • Ross RP, Morgan S & Hill C (2002) Preservation and fermentation: past, present and future. Int J Food Microbiol 79: 3-16.
    • (2002) Int J Food Microbiol , vol.79 , pp. 3-16
    • Ross, R.P.1    Morgan, S.2    Hill, C.3
  • 206
    • 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 (1985) 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 Chemother 27: 841-845.
    • (1985) Antimicrob Agents Chemother , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 208
    • 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 (1999) Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. J Biol Chem 274: 37544-37550.
    • (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
  • 209
    • 0021807335 scopus 로고
    • Influence of the staphylococcin-like peptide Pep5 on membrane potential of bacterial cells and cytoplasmic membrane vesicles
    • Sahl HG (1985) Influence of the staphylococcin-like peptide Pep5 on membrane potential of bacterial cells and cytoplasmic membrane vesicles. J Bacteriol 162: 833-836.
    • (1985) J Bacteriol , vol.162 , pp. 833-836
    • Sahl, H.G.1
  • 210
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria
    • Sahl HG & Bierbaum G (1998) Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria. Annu Rev Microbiol 52: 41-79.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 41-79
    • Sahl, H.G.1    Bierbaum, G.2
  • 211
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • Sahl HG, Jack RW & Bierbaum G (1995) Biosynthesis and biological activities of lantibiotics with unique post-translational modifications. Eur J Biochem 230: 827-853.
    • (1995) Eur J Biochem , vol.230 , pp. 827-853
    • Sahl, H.G.1    Jack, R.W.2    Bierbaum, G.3
  • 212
    • 0034330091 scopus 로고    scopus 로고
    • A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: Cloning of the structural gene and identification of the structure
    • Sashihara T, Kimura H, Higuchi T, Adachi A, Matsusaki H, Sonomoto K & Ishizaki A (2000) A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: cloning of the structural gene and identification of the structure. Biosci Biotechnol Biochem 64: 2420-2428.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2420-2428
    • Sashihara, T.1    Kimura, H.2    Higuchi, T.3    Adachi, A.4    Matsusaki, H.5    Sonomoto, K.6    Ishizaki, A.7
  • 214
    • 0024373046 scopus 로고
    • The peptide antibiotic subtilin acts by formation of voltage-dependent multi-state pores in bacterial and artificial membranes
    • Schüller F, Benz R & Sahl HG (1989) The peptide antibiotic subtilin acts by formation of voltage-dependent multi-state pores in bacterial and artificial membranes. Eur J Biochem 182: 181-186.
    • (1989) Eur J Biochem , vol.182 , pp. 181-186
    • Schüller, F.1    Benz, R.2    Sahl, H.G.3
  • 215
    • 0023912839 scopus 로고
    • Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings
    • Schnell N, Entian KD, Schneider U, Götz F, Zahner H, Kellner R & Jung G (1988) Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings. Nature 333: 276-278.
    • (1988) Nature , vol.333 , pp. 276-278
    • Schnell, N.1    Entian, K.D.2    Schneider, U.3    Götz, F.4    Zahner, H.5    Kellner, R.6    Jung, G.7
  • 216
    • 0024654855 scopus 로고
    • Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic
    • Schnell N, Entian KD, Götz F, Hörner T, Kellner R & Jung G (1989) Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic. FEMS Microbiol Lett 58: 263-268.
    • (1989) FEMS Microbiol Lett , vol.58 , pp. 263-268
    • Schnell, N.1    Entian, K.D.2    Götz, F.3    Hörner, T.4    Kellner, R.5    Jung, G.6
  • 219
    • 0028966278 scopus 로고
    • Genes involved in immunity to the lantibiotic nisin produced by Lactococcus lactis 6F3
    • Siegers K & Entian KD (1995) Genes involved in immunity to the lantibiotic nisin produced by Lactococcus lactis 6F3. Appl Environ Microbiol 61: 1082-1089.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1082-1089
    • Siegers, K.1    Entian, K.D.2
  • 220
    • 15844418684 scopus 로고    scopus 로고
    • Biosynthesis of lantibiotic nisin. Post-translational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex
    • Siegers K, Heinzmann S & Entian KD (1996) Biosynthesis of lantibiotic nisin. Post-translational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex. J Biol Chem 271: 12294-12301.
    • (1996) J Biol Chem , vol.271 , pp. 12294-12301
    • Siegers, K.1    Heinzmann, S.2    Entian, K.D.3
  • 221
    • 0030046733 scopus 로고    scopus 로고
    • Comparison of lantibiotic gene clusters and encoded proteins
    • Siezen RJ, Kuipers OP & de Vos WM (1996) Comparison of lantibiotic gene clusters and encoded proteins. Antonie Leeuwenhoek 69: 171-184.
    • (1996) Antonie Leeuwenhoek , vol.69 , pp. 171-184
    • Siezen, R.J.1    Kuipers, O.P.2    de Vos, W.M.3
  • 223
    • 0030964778 scopus 로고    scopus 로고
    • Organization and expression of a gene cluster involved in the biosynthesis of the lantibiotic lactocin S
    • Skaugen M, Abildgaard CIM & Nes IF (1997) Organization and expression of a gene cluster involved in the biosynthesis of the lantibiotic lactocin S. Mol Gen Genet 253: 674-686.
    • (1997) Mol Gen Genet , vol.253 , pp. 674-686
    • Skaugen, M.1    Abildgaard, C.I.M.2    Nes, I.F.3
  • 224
    • 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 (2002) Identification, characterization, and expression of a second, bicistronic, operon involved in the production of lactocin S in Lactobacillus sakei L45. Appl Environ Microbiol 68: 720-727.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 720-727
    • Skaugen, M.1    Andersen, E.L.2    Christie, V.H.3    Nes, I.F.4
  • 225
    • 0036006594 scopus 로고    scopus 로고
    • Maturation of the lantibiotic subtilin: Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to monitor precursors and their proteolytic processing in crude bacterial cultures
    • Stein T & Entian KD (2002) Maturation of the lantibiotic subtilin: matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to monitor precursors and their proteolytic processing in crude bacterial cultures. Rapid Commun Mass Spectrom 16: 103-110.
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 103-110
    • Stein, T.1    Entian, K.D.2
  • 227
    • 0037414778 scopus 로고    scopus 로고
    • Function of Lactococcus lactis nisin immunity genes nisI and nisFEG after coordinated expression in the surrogate host Bacillus subtilis
    • Stein T, Heinzmann S, Solovieva I & Entian KD (2003) Function of Lactococcus lactis nisin immunity genes nisI and nisFEG after coordinated expression in the surrogate host Bacillus subtilis. J Biol Chem 278: 89-94.
    • (2003) J Biol Chem , vol.278 , pp. 89-94
    • Stein, T.1    Heinzmann, S.2    Solovieva, I.3    Entian, K.D.4
  • 228
    • 13244258308 scopus 로고    scopus 로고
    • Expression and functional analysis of the subtilin immunity genes spaIFEG in the subtilin-sensitive host Bacillus subtilis MO1099
    • Stein T, Heinzmann S, Düsterhus S, Borchert S & Entian KD (2005) Expression and functional analysis of the subtilin immunity genes spaIFEG in the subtilin-sensitive host Bacillus subtilis MO1099. J Bacteriol 187: 822-828.
    • (2005) J Bacteriol , vol.187 , pp. 822-828
    • Stein, T.1    Heinzmann, S.2    Düsterhus, S.3    Borchert, S.4    Entian, K.D.5
  • 230
    • 8744303083 scopus 로고    scopus 로고
    • Is autoinducer-2 a universal signal for interspecies communication: A comparative genomic and phylogenic analysis of the synthesis and signal transduction pathways
    • Sun J, Daniel R, Wagner-Dobler I & Zeng AP (2004) Is autoinducer-2 a universal signal for interspecies communication: a comparative genomic and phylogenic analysis of the synthesis and signal transduction pathways. BMC Evol Biol 4: 36.
    • (2004) BMC Evol Biol , vol.4 , pp. 36
    • Sun, J.1    Daniel, R.2    Wagner-Dobler, I.3    Zeng, A.P.4
  • 231
    • 0038155138 scopus 로고    scopus 로고
    • Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin
    • Szekat C, Jack RW, Skutlarek D, Färber H & Bierbaum G (2003) Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin. Appl Environ Microbiol 69: 3777-3783.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3777-3783
    • Szekat, C.1    Jack, R.W.2    Skutlarek, D.3    Färber, H.4    Bierbaum, G.5
  • 232
    • 0345060796 scopus 로고    scopus 로고
    • Chemical communication among bacteria
    • Taga ME & Bassler BL (2003) Chemical communication among bacteria. Proc Natl Acad Sci USA 100(Suppl 2): 14549-14554.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.SUPPL. 2 , pp. 14549-14554
    • Taga, M.E.1    Bassler, B.L.2
  • 233
    • 3442892702 scopus 로고    scopus 로고
    • Prevention of streptococcal pharyngitis by anti-Streptococcus pyogenes bacteriocins-like inhibitory substances (BLIS) produced by Streptococcus salivarius
    • Tagg JR (2004) Prevention of streptococcal pharyngitis by anti-Streptococcus pyogenes bacteriocins-like inhibitory substances (BLIS) produced by Streptococcus salivarius. Indian J Med Res 119(Suppl): 13-16.
    • (2004) Indian J Med Res , vol.119 , Issue.SUPPL. , pp. 13-16
    • Tagg, J.R.1
  • 234
    • 0038242658 scopus 로고
    • Bacteriocin production by group A streptococci
    • Tagg JR, Read RSD & McGiven AR (1971) Bacteriocin production by group A streptococci. Pathology 3: 277-278.
    • (1971) Pathology , vol.3 , pp. 277-278
    • Tagg, J.R.1    Read, R.S.D.2    McGiven, A.R.3
  • 235
    • 0015668810 scopus 로고
    • Bacteriocin of a group A streptococcus: Partial purification and properties
    • Tagg JR, Read RSD & McGiven AR (1973) Bacteriocin of a group A streptococcus: partial purification and properties. Antimicrob Agents Chemother 4: 214-221.
    • (1973) Antimicrob Agents Chemother , vol.4 , pp. 214-221
    • Tagg, J.R.1    Read, R.S.D.2    McGiven, A.R.3
  • 237
    • 0032964297 scopus 로고    scopus 로고
    • Blast 2 sequences-a new tool for comparing protein and nucleotide sequences
    • Tatusova TA & Madden TL (1999) Blast 2 sequences-a new tool for comparing protein and nucleotide sequences. FEMS Microbiol Lett 174: 247-250.
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 238
    • 0026148683 scopus 로고
    • Inhibition of Clostridium tyrobutyricum by bacteriocin-like substances produced by lactic acid bacteria
    • Thuault D, Beliard E, Le Guern J & Bourgeois C-M (1991) Inhibition of Clostridium tyrobutyricum by bacteriocin-like substances produced by lactic acid bacteria. J Dairy Sci 74: 1145-1150.
    • (1991) J Dairy Sci , vol.74 , pp. 1145-1150
    • Thuault, D.1    Beliard, E.2    Le Guern, J.3    Bourgeois, C.-M.4
  • 240
    • 0036692989 scopus 로고    scopus 로고
    • Lantibiotics produced by lactic acid bacteria: Structure, function and applications
    • Twomey D, Ross RP, Ryan M, Meaney B & Hill C (2002) Lantibiotics produced by lactic acid bacteria: structure, function and applications. Antonie Leeuwenhoek 82: 165-185.
    • (2002) Antonie Leeuwenhoek , vol.82 , pp. 165-185
    • Twomey, D.1    Ross, R.P.2    Ryan, M.3    Meaney, B.4    Hill, C.5
  • 241
    • 0032931853 scopus 로고    scopus 로고
    • Influence of osmolarity and the presence of an osmoprotectant on Lactococcus lactis growth and bacteriocin production
    • Uguen P, Hamelin J, Le Pennec J-P & Blanco C (1999) Influence of osmolarity and the presence of an osmoprotectant on Lactococcus lactis growth and bacteriocin production. Appl Environ Microbiol 65: 291-293.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 291-293
    • Uguen, P.1    Hamelin, J.2    Le Pennec, J.-P.3    Blanco, C.4
  • 242
    • 0033811439 scopus 로고    scopus 로고
    • Lantibiotic biosynthesis: Interactions between prelacticin 481 and its putative modification enzyme, LctM
    • Uguen P, Le Pennec J-P & Dufour A (2000) Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM. J Bacteriol 182: 5262-5266.
    • (2000) J Bacteriol , vol.182 , pp. 5262-5266
    • Uguen, P.1    Le Pennec, J.-P.2    Dufour, A.3
  • 244
    • 0034967239 scopus 로고    scopus 로고
    • Intra-and interspecies signaling between Streptococcus salivarius and Streptococcus pyogenes mediated by SalA and SalA1 lantibiotic peptides
    • Upton M, Tagg JR, Wescombe P & Jenkinson HF (2001) Intra-and interspecies signaling between Streptococcus salivarius and Streptococcus pyogenes mediated by SalA and SalA1 lantibiotic peptides. J Bacteriol 183: 3931-3938.
    • (2001) J Bacteriol , vol.183 , pp. 3931-3938
    • Upton, M.1    Tagg, J.R.2    Wescombe, P.3    Jenkinson, H.F.4
  • 245
    • 33644760393 scopus 로고    scopus 로고
    • Streptococcus macedonicus ACA-DC 198 produces the lantibiotic, macedocin, at temperature and pH conditions that prevail during cheese manufacture
    • Van den Berghe E, Skourtas G, Tsakalidou E & De Vuyst L (2006) Streptococcus macedonicus ACA-DC 198 produces the lantibiotic, macedocin, at temperature and pH conditions that prevail during cheese manufacture. Int J Food Microbiol 107: 138-147.
    • (2006) Int J Food Microbiol , vol.107 , pp. 138-147
    • Van den Berghe, E.1    Skourtas, G.2    Tsakalidou, E.3    De Vuyst, L.4
  • 247
    • 0027309021 scopus 로고
    • Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis
    • van der Meer JR, Polman J, Beerthuyzen MM, Siezen RJ, Kuipers OP & de Vos WM (1993) Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis. J Bacteriol 175: 2578-2588.
    • (1993) J Bacteriol , vol.175 , pp. 2578-2588
    • van der Meer, J.R.1    Polman, J.2    Beerthuyzen, M.M.3    Siezen, R.J.4    Kuipers, O.P.5    de Vos, W.M.6
  • 249
    • 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 (2001) Proteins of the lactococcin A secretion system: lcnD encodes two in-frame proteins. FEMS Microbiol Lett 204: 259-263.
    • (2001) FEMS Microbiol Lett , vol.204 , pp. 259-263
    • Varcamonti, M.1    Nicastro, G.2    Venema, G.3    Kok, J.4
  • 250
    • 0141539309 scopus 로고    scopus 로고
    • Bacteriocin-like inhibitory substance (BLIS) production by the normal flora of the nasopharynx: Potential to protect against otitis media?
    • Walls T, Power D & Tagg J (2003) Bacteriocin-like inhibitory substance (BLIS) production by the normal flora of the nasopharynx: potential to protect against otitis media? J Med Microbiol 52: 829-833.
    • (2003) J Med Microbiol , vol.52 , pp. 829-833
    • Walls, T.1    Power, D.2    Tagg, J.3
  • 251
    • 0038220969 scopus 로고    scopus 로고
    • Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes
    • Wescombe PA & Tagg JR (2003) Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes. Appl Environ Microbiol 69: 2737-2747.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2737-2747
    • Wescombe, P.A.1    Tagg, J.R.2
  • 253
    • 33144480519 scopus 로고    scopus 로고
    • Production of the lantibiotic salivaricin A and its variants by oral streptococci and use of a specific induction assay to detect their presence in human saliva
    • Wescombe PA, Upton M, Dierksen KP et al. (2006b) Production of the lantibiotic salivaricin A and its variants by oral streptococci and use of a specific induction assay to detect their presence in human saliva. Appl Environ Microbiol 72: 1459-1466.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1459-1466
    • Wescombe, P.A.1    Upton, M.2    Dierksen, K.P.3
  • 255
    • 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 (2001) 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) 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
  • 256
    • 33748506881 scopus 로고    scopus 로고
    • The mode of action of the lantibiotic lacticin 3147 - a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II
    • Wiedemann I, Böttiger T, Bonelli RR et al. (2006a) The mode of action of the lantibiotic lacticin 3147 - a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II. Mol Microbiol 61: 285-296.
    • (2006) Mol Microbiol , vol.61 , pp. 285-296
    • Wiedemann, I.1    Böttiger, T.2    Bonelli, R.R.3
  • 258
    • 0032484693 scopus 로고    scopus 로고
    • Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans
    • Woodruff WA, Novak J & Caufield PW (1998) Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans. Gene 206: 37-43.
    • (1998) Gene , vol.206 , pp. 37-43
    • Woodruff, W.A.1    Novak, J.2    Caufield, P.W.3
  • 259
    • 4644372683 scopus 로고    scopus 로고
    • Post-translational modifications during lantibiotic biosynthesis
    • Xie L & van der Donk WA (2004) Post-translational modifications during lantibiotic biosynthesis. Curr Opin Chem Biol 8: 498-507.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 498-507
    • Xie, L.1    van der Donk, W.A.2
  • 261
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


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