메뉴 건너뛰기




Volumn 84, Issue 5-6, 2002, Pages 545-557

Mode of action of modified and unmodified bacteriocins from Gram-positive bacteria

Author keywords

Antibacterial; Bacteriocin; Lantibiotic; Pore

Indexed keywords

ACTAGARDIN; BACTERIOCIN; BAVARICIN MN; DIVERCIN V41; DURAMYCIN; ENTEROCIN P; EPIDERMIN; LACTACIN F; LACTOCOCCIN G; LANTHIOPEPTIN; LANTIBIOTIC; LEUCOCIN A; LIPID; MANNOSE PERMEASE; MERSACIDIN; MESENTERICIN Y105; NISIN; PEDIOCIN JD; PEDIOCIN PA 1; PEPTIDOGLYCAN; PERMEASE; PHEROMONE; PHOSPHOETHANOLAMINE; PHOSPHOLIPASE A2; PHOSPHOTRANSFERASE; PLANTARICIN A; PLANTARICIN EF; PLANTARICIN JK; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; UNINDEXED DRUG; ANTIINFECTIVE AGENT; DRUG DERIVATIVE; MURAMYL NAC (PENTAPEPTIDE)PYROPHOSPHORYL UNDECAPRENOL; MURAMYL-NAC-(PENTAPEPTIDE)PYROPHOSPHORYL-UNDECAPRENOL; PEPTIDE; PHOSPHATIDYLETHANOLAMINE; URIDINE DIPHOSPHATE N ACETYLMURAMIC ACID;

EID: 0036589242     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(02)01417-7     Document Type: Review
Times cited : (264)

References (87)
  • 2
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • T.R. Klaenhammer, Genetics of bacteriocins produced by lactic acid bacteria, FEMS Microbiol. Rev. 12 (1993) 39-85.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-85
    • Klaenhammer, T.R.1
  • 3
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • H.G. Sahl, R.W. Jack, J. Bierbaum, Biosynthesis and biological activities of lantibiotics with unique post-translational modifications, Eur. J. Biochem. 230 (1995) 827-853.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 827-853
    • Sahl, H.G.1    Jack, R.W.2    Bierbaum, J.3
  • 4
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics - Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria
    • H.G. Sahl, G. Bierbaum, Lantibiotics - Biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria, Annu. Rev. Microbiol. 52 (1998) 41-47.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-47
    • Sahl, H.G.1    Bierbaum, G.2
  • 5
    • 0033851437 scopus 로고    scopus 로고
    • Posttranslationally modified bacteriocins-the lantibiotics
    • A. Guder, I. Wiedemann, H.G. Sahl, Posttranslationally modified bacteriocins-the lantibiotics, Biopolymers 55 (2000) 62-73.
    • (2000) Biopolymers , vol.55 , pp. 62-73
    • Guder, A.1    Wiedemann, I.2    Sahl, H.G.3
  • 6
    • 0025817859 scopus 로고
    • Lantibiotics-ribosomally synthesized biologically active polypeptides containing sulfide bridges and didehydroamino acids
    • G. Jung, Lantibiotics-ribosomally synthesized biologically active polypeptides containing sulfide bridges and didehydroamino acids, Angewandte Chemie, Int. Ed. Engl. 30 (1991) 1051-1068.
    • (1991) Angewandte Chemie, Int. Ed. Engl. , vol.30 , pp. 1051-1068
    • Jung, G.1
  • 9
    • 0027509839 scopus 로고
    • The antimicrobial effect of a structural variant of subtilin against outgrowing Bacillus cereus T spores and vegetative cells occurs by different mechanisms
    • W. Liu, J.N. Hansen, The antimicrobial effect of a structural variant of subtilin against outgrowing Bacillus cereus T spores and vegetative cells occurs by different mechanisms, Appl. Environ. Microbiol. 59 (1993) 648-651.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 648-651
    • Liu, W.1    Hansen, J.N.2
  • 10
    • 34250970043 scopus 로고
    • Die Wirkung von Nisin auf Clostridium butyricum
    • H.R. Ramseier, Die Wirkung von Nisin auf Clostridium butyricum, Arch. Mikrobiol. 37 (1960) 57-94.
    • (1960) Arch. Mikrobiol. , vol.37 , pp. 57-94
    • Ramseier, H.R.1
  • 11
    • 0015663984 scopus 로고
    • Additional antibiotic inhibitors of peptidoglycan synthesis
    • P.E. Linnett, J.L. Strominger, Additional antibiotic inhibitors of peptidoglycan synthesis, Antimicrob. Agents Chemother. 4 (1973) 231-236.
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 231-236
    • Linnett, P.E.1    Strominger, J.L.2
  • 13
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin: Influence on the membrane potential of bacterial cells and on cytoplasmic and artificial membrane vesicles
    • E. Ruhr, H.G. Sahl, Mode of action of the peptide antibiotic nisin: influence on the membrane potential of bacterial cells and on cytoplasmic and artificial membrane vesicles, Antimicrob. Agents Chemother. 27 (1985) 841-845.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 14
    • 0023491341 scopus 로고
    • Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin
    • H.G. Sahl, M. Kordel, R. Benz, Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin, Arch. Microbiol. 149 (1987) 120-124.
    • (1987) Arch. Microbiol. , vol.149 , pp. 120-124
    • Sahl, H.G.1    Kordel, M.2    Benz, R.3
  • 15
    • 0019951817 scopus 로고
    • Mode of action of the staphylococcin-like peptide Pep5 and culture conditions effecting its activity
    • H.G. Sahl, H. Brandis, Mode of action of the staphylococcin-like peptide Pep5 and culture conditions effecting its activity, Zbl. Bakt. Hyg. 252 (1982) 166-175.
    • (1982) Zbl. Bakt. Hyg. , vol.252 , pp. 166-175
    • Sahl, H.G.1    Brandis, H.2
  • 16
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • H. Brötz, M. Josten, I. Wiedemann, U. Schneider, F. Götz, G. Bierbaum, et al., Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics, Mol. Microbiol. 30 (1998) 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
  • 18
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • I. Wiedemann, E. Breukink, C. van Kraaij, O.P. Kuipers, G. Bierbaum, B. de Kruijff, et al., Specific binding of nisin to the peptidglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity, J. Biol. Chem. 276 (2001) 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
  • 20
    • 0021905348 scopus 로고
    • Induction of autolysis of staphylococci by the basic peptide antibiotic Pep5 and nisin and their influence on the activity of autolytic enzymes
    • G. Bierbaum, H.G. Sahl, Induction of autolysis of staphylococci by the basic peptide antibiotic Pep5 and nisin and their influence on the activity of autolytic enzymes, Arch. Microbiol. 141 (1985) 249-254.
    • (1985) Arch. Microbiol. , vol.141 , pp. 249-254
    • Bierbaum, G.1    Sahl, H.G.2
  • 21
    • 0023547233 scopus 로고
    • Autolytic system of Staphylococcus simulans 22: Influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase
    • G. Bierbaum, H.G. Sahl, Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase, J. Bacteriol. 169 (1987) 5452-5458.
    • (1987) J. Bacteriol. , vol.169 , pp. 5452-5458
    • Bierbaum, G.1    Sahl, H.G.2
  • 22
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphiphatic, alpha-helical antimicrobial peptides
    • Z. Oren, Y. Shai, Mode of action of linear amphiphatic, alpha-helical antimicrobial peptides, Biopolymers 47 (1998) 451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 23
    • 0003123005 scopus 로고
    • Mechanism of channel-formation by lantibiotics in black lipid membranes
    • in: G. Jung, H.-G. Sahl (Eds.); Escom, Leiden
    • R. Benz, G. Jung, H.G. Sahl, Mechanism of channel-formation by lantibiotics in black lipid membranes, in: G. Jung, H.-G. Sahl (Eds.), Nisin and Novel Lantibiotics, Escom, Leiden, 1991, pp. 359-372.
    • (1991) Nisin and Novel Lantibiotics , pp. 359-372
    • Benz, R.1    Jung, G.2    Sahl, H.G.3
  • 24
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • G. Boheim, Statistical analysis of alamethicin channels in black lipid membranes, J. Membr. Biol. 19 (1974) 277-303.
    • (1974) J. Membr. Biol. , vol.19 , pp. 277-303
    • Boheim, G.1
  • 25
    • 0023251067 scopus 로고
    • Alamethicin incorporation in lipid bilayers: A thermodynamic study
    • V. Rizzo, S. Stankowski, G. Schwarz, Alamethicin incorporation in lipid bilayers: a thermodynamic study, Biochemistry 19 (1987) 2751-2759.
    • (1987) Biochemistry , vol.19 , pp. 2751-2759
    • Rizzo, V.1    Stankowski, S.2    Schwarz, G.3
  • 26
    • 0030059436 scopus 로고    scopus 로고
    • Three-dimensional structure of the lantibiotic nisin in the presence of membrane-mimetic micelles of dodecylphosphocholine and of sodium dodecylsulphate
    • H.W. van den Hooven, C.C.M. Doeland, M. van de Kamp, R.N.H. Konings, C.W. Hilbers, F.J.M. van de Ven, Three-dimensional structure of the lantibiotic nisin in the presence of membrane-mimetic micelles of dodecylphosphocholine and of sodium dodecylsulphate, Eur. J. Biochem. 235 (1996) 382-393.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 382-393
    • Van Den Hooven, H.W.1    Doeland, C.C.M.2    Van De Kamp, M.3    Konings, R.N.H.4    Hilbers, C.W.5    Van De Ven, F.J.M.6
  • 27
    • 0030067073 scopus 로고    scopus 로고
    • Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphophocholine and of sodium dodecylsulphate
    • H.W. van den Hooven, C.A.E.M. Spronk, M. van de Kamp, R.N.H. Konings, C.W. Hilbers, F.J.M. van de Ven, Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphophocholine and of sodium dodecylsulphate, Eur. J. Biochem. 235 (1996) 394-403.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 394-403
    • Van Den Hooven, H.W.1    Spronk, C.A.E.M.2    Van De Kamp, M.3    Konings, R.N.H.4    Hilbers, C.W.5    Van De Ven, F.J.M.6
  • 29
    • 0026594411 scopus 로고
    • Solution structures of nisin and its two major degradation products determined by NMR
    • L.Y. Lian, W.C. Chan, S.D. Morley, G.C.K. Roberts, B.W. Bycroft, D. Jackson, Solution structures of nisin and its two major degradation products determined by NMR, Biochem. J. 283 (1991) 413-420.
    • (1991) Biochem. J. , vol.283 , pp. 413-420
    • Lian, L.Y.1    Chan, W.C.2    Morley, S.D.3    Roberts, G.C.K.4    Bycroft, B.W.5    Jackson, D.6
  • 31
    • 0030047564 scopus 로고    scopus 로고
    • Z nisin, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity - A monolayer study
    • R.A. Demel, T. Peelen, R.J. Siezen, B. de Kruijff, O.P. Kuipers, Z Nisin, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity - a monolayer study, Eur. J. Biochem. 235 (1996) 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
  • 32
    • 0030923340 scopus 로고    scopus 로고
    • The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane
    • E. Breukink, C. van Kraaij, R.A. Demel, R.J. Siezen, O.P. Kuipers, B. de Kruijff, The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane, Biochemistry 36 (1997) 6968-6976.
    • (1997) Biochemistry , vol.36 , pp. 6968-6976
    • Breukink, E.1    Van Kraaij, C.2    Demel, R.A.3    Siezen, R.J.4    Kuipers, O.P.5    De Kruijff, B.6
  • 33
    • 0032542055 scopus 로고    scopus 로고
    • Pore formation by nisin involves translocation of its C-terminal part across the membranes
    • C. vanKraaij, E. Breukink, M.A. Noordermeer, R.A. Demel, R.J. Siezen, O.P. Kuipers, et al., Pore formation by nisin involves translocation of its C-terminal part across the membranes, Biochemistry 37 (1998) 16033-16040.
    • (1998) Biochemistry , vol.37 , pp. 16033-16040
    • Vankraaij, C.1    Breukink, E.2    Noordermeer, M.A.3    Demel, R.A.4    Siezen, R.J.5    Kuipers, O.P.6
  • 34
    • 0029984783 scopus 로고    scopus 로고
    • Interaction of nisin with planar lipid bilayers monitored by fluorescence recovery after photobleaching
    • C.J. Giffard, S. Ladha, A.R. Mackie, D.C. Clark, D. Sanders, Interaction of nisin with planar lipid bilayers monitored by fluorescence recovery after photobleaching. J. Membr. Biol. 151 (1996) 293-300.
    • (1996) J. Membr. Biol. , vol.151 , pp. 293-300
    • Giffard, C.J.1    Ladha, S.2    Mackie, A.R.3    Clark, D.C.4    Sanders, D.5
  • 35
    • 0029664334 scopus 로고    scopus 로고
    • Physicochemical characterization of the nisin-membrane interaction with liposomes derived from Listeria monocytogenes
    • K. Winkowski, R.D. Ludescher, T.J. Montville, Physicochemical characterization of the nisin-membrane interaction with liposomes derived from Listeria monocytogenes, Appl. Environ. Microbiol. 62 (1996) 323-327.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 323-327
    • Winkowski, K.1    Ludescher, R.D.2    Montville, T.J.3
  • 36
    • 0030597972 scopus 로고    scopus 로고
    • Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin
    • W.C. Chan, M.L. Leyland, J. Clark, H.M. Dodd, L.Y. Lian, M.J. Gasson, et al., Structure-activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin, FEBS Lett. 390 (1996) 129-132.
    • (1996) FEBS Lett. , vol.390 , pp. 129-132
    • Chan, W.C.1    Leyland, M.L.2    Clark, J.3    Dodd, H.M.4    Lian, L.Y.5    Gasson, M.J.6
  • 37
    • 0017083591 scopus 로고
    • Gardimycin, a new antibiotic from Actinoplanes, III. Biological properties
    • V. Arioli, M. Berti, L.G. Silvestri, Gardimycin, a new antibiotic from Actinoplanes, III. Biological properties, J. Antibiot. 29 (1976) 511-515.
    • (1976) J. Antibiot. , vol.29 , pp. 511-515
    • Arioli, V.1    Berti, M.2    Silvestri, L.G.3
  • 38
    • 0002377291 scopus 로고
    • Chemotherapeutic properties of mersacidin in vitro and in vivo
    • in: G. Jung, H.-G. Sahl (Eds.); Escom, Leiden
    • M. Limbert, D. Isert, N. Klesel, A. Markus, G. Seibert, S. Chatterjee, et al., Chemotherapeutic properties of mersacidin in vitro and in vivo, in: G. Jung, H.-G. Sahl (Eds.), Nisin and Novel Lantibiotics, Escom, Leiden, 1991, pp. 448-456.
    • (1991) Nisin and Novel Lantibiotics , pp. 448-456
    • Limbert, M.1    Isert, D.2    Klesel, N.3    Markus, A.4    Seibert, G.5    Chatterjee, S.6
  • 39
    • 0025903443 scopus 로고
    • Activity of mersacidin, a novel peptide, compared with that of vancomycin, teicoplanin, and daptomycin
    • W.W. Niu, H.C. Neu, Activity of mersacidin, a novel peptide, compared with that of vancomycin, teicoplanin, and daptomycin, Antimicrob. Agents Chemother. 35 (1991) 998-1000.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 998-1000
    • Niu, W.W.1    Neu, H.C.2
  • 40
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • H. Brötz, G. Bierbaum, P.E. Reynolds, H.G. Sahl, The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation, Eur. J. Biochem. 246 (1997) 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
  • 42
    • 0028955428 scopus 로고
    • The tetracycline lantibiotic actagardine: 1H-NMR and 13C-NMR assignments and revised primary structure
    • N. Zimmermann, J.W. Metzger, G. Jung, The tetracycline lantibiotic actagardine: 1H-NMR and 13C-NMR assignments and revised primary structure, Eur. J. Biochem. 228 (1995) 786-797.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 786-797
    • Zimmermann, N.1    Metzger, J.W.2    Jung, G.3
  • 43
    • 0021347761 scopus 로고
    • Stimulation of glycolysis by placental polypeptides and inhibition by duramycin
    • E. Racker, C. Riegler, M. Abdel-Ghany, Stimulation of glycolysis by placental polypeptides and inhibition by duramycin, Cancer 44 (1983) 1364-1367.
    • (1983) Cancer , vol.44 , pp. 1364-1367
    • Racker, E.1    Riegler, C.2    Abdel-Ghany, M.3
  • 44
    • 0023178756 scopus 로고
    • Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles
    • L.L. Chen, P.C. Tai, Effects of antibiotics and other inhibitors on ATP-dependent protein translocation into membrane vesicles, J. Bacteriol. 169 (1987) 2372-2379.
    • (1987) J. Bacteriol. , vol.169 , pp. 2372-2379
    • Chen, L.L.1    Tai, P.C.2
  • 45
    • 0022003139 scopus 로고
    • Interaction of duramycin with artificial and natural membranes
    • J. Navarro, J. Chabot, K. Sherril, R. Aneja, S.A. Zahler, Interaction of duramycin with artificial and natural membranes, Biochemistry 24 (1985) 4645-4650.
    • (1985) Biochemistry , vol.24 , pp. 4645-4650
    • Navarro, J.1    Chabot, J.2    Sherril, K.3    Aneja, R.4    Zahler, S.A.5
  • 46
    • 0002297866 scopus 로고
    • Duramycin B and C, two new lanthionine-containing antibiotics as inhibitors of phospholipase A2, and structural revision of duramycin and cinnamycin
    • in: G. Jung, H.-G. Sahl (Eds.); Escom, Leiden
    • A. Fredenhagen, F. Märki, G. Fendrich, W. Märki, J. Gruner, J. van Oostrum, et al., Duramycin B and C, two new lanthionine-containing antibiotics as inhibitors of phospholipase A2, and structural revision of duramycin and cinnamycin, in: G. Jung, H.-G. Sahl (Eds.), Nisin and Novel Lantibiotics, Escom, Leiden, 1991, pp. 131-140.
    • (1991) Nisin and Novel Lantibiotics , pp. 131-140
    • Fredenhagen, A.1    Märki, F.2    Fendrich, G.3    Märki, W.4    Gruner, J.5    Van Oostrum, J.6
  • 47
    • 0030041310 scopus 로고    scopus 로고
    • Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophophatidylethanolamine by 1H-NMR
    • K. Hosoda, M. Ohya, T. Kohno, T. Maeda, S. Endo, W. Wakamatsu, Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophophatidylethanolamine by 1H-NMR, J. Biochem. 119 (1996) 226-230.
    • (1996) J. Biochem. , vol.119 , pp. 226-230
    • Hosoda, K.1    Ohya, M.2    Kohno, T.3    Maeda, T.4    Endo, S.5    Wakamatsu, W.6
  • 49
    • 0026091089 scopus 로고
    • Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2
    • F. Märki, E. Hänni, A. Fredenhagen, J. van Oostrum, Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2, Biochem. Pharmacol. 42 (1991) 2027-2031.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 2027-2031
    • Märki, F.1    Hänni, E.2    Fredenhagen, A.3    Van Oostrum, J.4
  • 50
    • 0033857685 scopus 로고    scopus 로고
    • Class II antimicrobial peptides from lactic acid bacteria
    • I.F. Nes, H. Holo, Class II antimicrobial peptides from lactic acid bacteria, Biopolymers 55 (2000) 50-61.
    • (2000) Biopolymers , vol.55 , pp. 50-61
    • Nes, I.F.1    Holo, H.2
  • 52
    • 0025960702 scopus 로고
    • Mode of action of pediocin AcH from Pediococcus acidilactici H on sensitive bacterial strains
    • A.K. Bhunia, M.C. Johnson, B. Ray, N. Kalchayanand, Mode of action of pediocin AcH from Pediococcus acidilactici H on sensitive bacterial strains, J. Appl. Bacteriol. 70 (1991) 25-33.
    • (1991) J. Appl. Bacteriol. , vol.70 , pp. 25-33
    • Bhunia, A.K.1    Johnson, M.C.2    Ray, B.3    Kalchayanand, N.4
  • 53
    • 0027424936 scopus 로고
    • Pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0, forms hydrophilic pores in the cytoplasmic membrane of target cells
    • M.L. Chikindas, M.J. Garcia-Garcera, A.J. Driessen, A.M. Ledeboer, J. Nissen-Meyer, I.F. Nes, et al., Pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0, forms hydrophilic pores in the cytoplasmic membrane of target cells, Appl. Environ. Microbiol. 59 (1993) 3577-3584.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3577-3584
    • Chikindas, M.L.1    Garcia-Garcera, M.J.2    Driessen, A.J.3    Ledeboer, A.M.4    Nissen-Meyer, J.5    Nes, I.F.6
  • 54
    • 0030999249 scopus 로고    scopus 로고
    • Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein-receptor and its relationship to a predicted tertiary structure
    • Y. Chen, R. Shapira, M. Eisenstein, T.J. Montville, Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein-receptor and its relationship to a predicted tertiary structure, Appl. Environ. Microbiol. 63 (1997) 524-531.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 524-531
    • Chen, Y.1    Shapira, R.2    Eisenstein, M.3    Montville, T.J.4
  • 55
    • 0031717018 scopus 로고    scopus 로고
    • Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles
    • Y. Chen, R.D. Ludescher, T.J. Montville, Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles, Appl. Environ. Microbiol. 64 (1998) 3530-3532.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3530-3532
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 56
    • 0030833912 scopus 로고    scopus 로고
    • Electrostatic interactions, but not the YGNGV consensus motif, govern the binding of pediocin PA-1 and its fragments to phospholipid vesicles
    • Y. Chen, R.D. Ludescher, T.J. Montville, Electrostatic interactions, but not the YGNGV consensus motif, govern the binding of pediocin PA-1 and its fragments to phospholipid vesicles, Appl. Environ. Microbiol. 63 (1997) 4770-4777.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4770-4777
    • Chen, Y.1    Ludescher, R.D.2    Montville, T.J.3
  • 57
    • 0031793223 scopus 로고    scopus 로고
    • The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C terminus
    • G. Fimland, R. Jack, G. Jung, I.F. Nes, I. Nissen-Meyer, The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C terminus, Appl. Environ. Microbiol. 64 (1998) 5057-5060.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 5057-5060
    • Fimland, G.1    Jack, R.2    Jung, G.3    Nes, I.F.4    Nissen-Meyer, I.5
  • 58
    • 0026786899 scopus 로고
    • Collapse of the proton motive force in Listeria monocytogenes caused by a bacteriocin produced by Pediococcus acidilactici
    • D.P. Christensen, R.W. Hutkins, Collapse of the proton motive force in Listeria monocytogenes caused by a bacteriocin produced by Pediococcus acidilactici, Appl. Environ. Microbiol. 58 (1992) 3312-3315.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3312-3315
    • Christensen, D.P.1    Hutkins, R.W.2
  • 59
    • 0031708535 scopus 로고    scopus 로고
    • Bacteriocins inhibit glucose PEP:PTS activity in Listeria monocytogenes by induced efflux of intracellular metabolites
    • B.L. Waite, R.W. Hutkins, Bacteriocins inhibit glucose PEP:PTS activity in Listeria monocytogenes by induced efflux of intracellular metabolites, J. Appl. Microbiol. 85 (1998) 287-292.
    • (1998) J. Appl. Microbiol. , vol.85 , pp. 287-292
    • Waite, B.L.1    Hutkins, R.W.2
  • 60
    • 0031802188 scopus 로고    scopus 로고
    • Bacteriocin inhibition of two glucose transport systems in Listeria monocytogenes
    • B.L. Waite, G.R. Siragusa, R.W. Hutkins, Bacteriocin inhibition of two glucose transport systems in Listeria monocytogenes, J. Appl. Microbiol. 84 (1998) 715-721.
    • (1998) J. Appl. Microbiol. , vol.84 , pp. 715-721
    • Waite, B.L.1    Siragusa, G.R.2    Hutkins, R.W.3
  • 61
    • 0029908370 scopus 로고    scopus 로고
    • Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles
    • A.L. Kaiser, T.J. Montville, Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles, Appl. Environ. Microbiol. 62 (1996) 4529-4535.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4529-4535
    • Kaiser, A.L.1    Montville, T.J.2
  • 62
    • 0032975054 scopus 로고    scopus 로고
    • Delineation of key amino acid side chains and peptide domains for antimicrobial properties of divercin V41, a pediocin-like bacteriocin secreted by Carnobacterium divergens V41
    • P. Bhugaloo-Vial, J.P. Douliez, D. Moll, X. Dousset, P. Boyaval, D. Marion, Delineation of key amino acid side chains and peptide domains for antimicrobial properties of divercin V41, a pediocin-like bacteriocin secreted by Carnobacterium divergens V41, Appl. Environ. Microbiol. 65 (1999) 2895-2900.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2895-2900
    • Bhugaloo-Vial, P.1    Douliez, J.P.2    Moll, D.3    Dousset, X.4    Boyaval, P.5    Marion, D.6
  • 63
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • N.L. Fregeau Gallagher, M. Sailer, W.P. Niemczura, T.T. Nakashima, M.E. Stiles, J.C. Vederas, Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria, Biochemistry 36 (1997) 15062-15072.
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Fregeau Gallagher, N.L.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 65
    • 0027298849 scopus 로고
    • Membrane permeabilization of Listeria monocytogenes and mitochondria by the bacteriocin mesentericin Y105
    • A. Maftah, D. Renault, C. Vignoles, Y. Hechard, P. Bressollier, M.H. Ratinaud, et al., Membrane permeabilization of Listeria monocytogenes and mitochondria by the bacteriocin mesentericin Y105, J. Bacteriol. 175 (1993) 3232-3235.
    • (1993) J. Bacteriol. , vol.175 , pp. 3232-3235
    • Maftah, A.1    Renault, D.2    Vignoles, C.3    Hechard, Y.4    Bressollier, P.5    Ratinaud, M.H.6
  • 66
    • 0029891059 scopus 로고    scopus 로고
    • Covalent structure, synthesis, and structure-function studies of mesentericin Y 105(37), a defensive peptide from Gram-positive bacteria Leuconostoc mesenteroides
    • Y. Fleury, M.A. Dayem, J.J. Montagne, E. Chaboisseau, J.P. Le Caer, P. Nicolas, et al., Covalent structure, synthesis, and structure-function studies of mesentericin Y 105(37), a defensive peptide from Gram-positive bacteria Leuconostoc mesenteroides, J. Biol. Chem. 271 (1996) 14421-14429.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14421-14429
    • Fleury, Y.1    Dayem, M.A.2    Montagne, J.J.3    Chaboisseau, E.4    Le Caer, J.P.5    Nicolas, P.6
  • 67
    • 0030613798 scopus 로고    scopus 로고
    • The rpoN (sigma54) gene from Listeria monocytogenes is involved in resistance to mesentericin Y105, an antibacterial peptide from Leuconostoc mesenteroides
    • D. Robichon, E. Gouin, M. Débarbouillé, P. Cossart, Y. Cenatiempo, Y. Héchard, The rpoN (sigma54) gene from Listeria monocytogenes is involved in resistance to mesentericin Y105, an antibacterial peptide from Leuconostoc mesenteroides, J. Bacteriol. 1979 (1997) 7591-7594.
    • (1997) J. Bacteriol. , vol.179 , pp. 7591-7594
    • Robichon, D.1    Gouin, E.2    Débarbouillé, M.3    Cossart, P.4    Cenatiempo, Y.5    Héchard, Y.6
  • 68
    • 0033661296 scopus 로고    scopus 로고
    • The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins
    • K. Dalet, C. Briand, Y. Cenatiempo, Y. Hechard The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins, Curr. Microbiol. 41 (2000) 441-443.
    • (2000) Curr. Microbiol. , vol.41 , pp. 441-443
    • Dalet, K.1    Briand, C.2    Cenatiempo, Y.3    Hechard, Y.4
  • 69
    • 0035216679 scopus 로고    scopus 로고
    • A sigma(54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105
    • K. Dalet, Y. Cenatiempo, P. Cossart, Y. Hechard, A sigma(54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105, Microbiology 147 (2001) 3263-3269.
    • (2001) Microbiology , vol.147 , pp. 3263-3269
    • Dalet, K.1    Cenatiempo, Y.2    Cossart, P.3    Hechard, Y.4
  • 70
    • 0034969179 scopus 로고    scopus 로고
    • Analysis of sigma(54)-dependent genes in Enterococcus faecalis: A mannose PTS permease (EII(Man) is involved in sensitivity to a bacteriocin, mesentericin Y105
    • Y. Hechard, C. Pelletier, Y. Cenatiempo, J. Frere, Analysis of sigma(54)-dependent genes in Enterococcus faecalis: a mannose PTS permease (EII(Man) is involved in sensitivity to a bacteriocin, mesentericin Y105, Microbiology 147 (2001) 1575-1580.
    • (2001) Microbiology , vol.147 , pp. 1575-1580
    • Hechard, Y.1    Pelletier, C.2    Cenatiempo, Y.3    Frere, J.4
  • 71
    • 0033930978 scopus 로고    scopus 로고
    • Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • M. Ramnath, M. Beukes, K. Tamura, J.W. Hastings, Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Appl. Environ. Microbiol. 66 (2000) 3098-3101.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3098-3101
    • Ramnath, M.1    Beukes, M.2    Tamura, K.3    Hastings, J.W.4
  • 72
    • 0034736095 scopus 로고    scopus 로고
    • Analogues of bacteriocins: Antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives
    • L.Z. Yan, A.C. Gibbs, M.E. Stiles, D.S. Wishart, J.C. Vederas, Analogues of bacteriocins: antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives, J. Med. Chem. 43 (2000) 4579-4581.
    • (2000) J. Med. Chem. , vol.43 , pp. 4579-4581
    • Yan, L.Z.1    Gibbs, A.C.2    Stiles, M.E.3    Wishart, D.S.4    Vederas, J.C.5
  • 73
    • 0030698620 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum
    • L.M. Cintas, P. Casaus, L.S. Havarstein, P.E. Hernandez, I.F. Nes, Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum, Appl. Environ. Microbiol. 63 (1997) 4321-4330.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4321-4330
    • Cintas, L.M.1    Casaus, P.2    Havarstein, L.S.3    Hernandez, P.E.4    Nes, I.F.5
  • 76
    • 0028222975 scopus 로고
    • Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane
    • T. Abee, T.R. Klaenhammer, L. Letellier, Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane, Appl. Environ. Microbiol. 60 (1994) 1006-1013.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1006-1013
    • Abee, T.1    Klaenhammer, T.R.2    Letellier, L.3
  • 77
    • 0032865690 scopus 로고    scopus 로고
    • Complementary and overlapping selectivity of the two-peptide bacteriocins plantaricin EF and JK
    • G.N. Moll, E. van den Akker, H.H. Hauge, J. Nissen-Meyer, I.F. Nes, W.N. Konings, et al., Complementary and overlapping selectivity of the two-peptide bacteriocins plantaricin EF and JK, J. Bacteriol. 181 (1999) 4848-4852.
    • (1999) J. Bacteriol. , vol.181 , pp. 4848-4852
    • Moll, G.N.1    Van Den Akker, E.2    Hauge, H.H.3    Nissen-Meyer, J.4    Nes, I.F.5    Konings, W.N.6
  • 78
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • J. Nissen-Meyer, H. Holo, L.S. Havarstein, K. Sletten, I.F. Nes, A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides, J. Bacteriol. 174 (1992) 5686-5692.
    • (1992) J. Bacteriol. , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Havarstein, L.S.3    Sletten, K.4    Nes, I.F.5
  • 81
    • 0032541965 scopus 로고    scopus 로고
    • Plantaricin A is an amphiphilic alpha-helical bacteriocin-like pheromone which exerts antimicrobial and pheromone activities through different mechanisms
    • H.H. Hauge, D. Mantzilas, G.N. Moll, W.N. Konings, A.J. Driessen, V.G. Eijsink, et al., Plantaricin A is an amphiphilic alpha-helical bacteriocin-like pheromone which exerts antimicrobial and pheromone activities through different mechanisms, Biochemistry 37 (1998) 16026-16032.
    • (1998) Biochemistry , vol.37 , pp. 16026-16032
    • Hauge, H.H.1    Mantzilas, D.2    Moll, G.N.3    Konings, W.N.4    Driessen, A.J.5    Eijsink, V.G.6
  • 82
    • 0026332723 scopus 로고
    • The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner
    • M.J. Van Belkum, J. Kok, G. Venema, H. Holo, I.F. Nes, W.N. Konings, et al., The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner, J. Bacteriol. 173 (1991) 7934-7941.
    • (1991) J. Bacteriol. , vol.173 , pp. 7934-7941
    • Van Belkum, M.J.1    Kok, J.2    Venema, G.3    Holo, H.4    Nes, I.F.5    Konings, W.N.6
  • 83
    • 0029742984 scopus 로고    scopus 로고
    • Lactococcin 972: A homodimeric lactococcal bacteriocin whose primary target is not the plasma membrane
    • B. Martinez, J.E. Suarez, A. Rodriguez, Lactococcin 972: a homodimeric lactococcal bacteriocin whose primary target is not the plasma membrane, Microbiology 142 (1996) 2393-2398.
    • (1996) Microbiology , vol.142 , pp. 2393-2398
    • Martinez, B.1    Suarez, J.E.2    Rodriguez, A.3
  • 84
    • 0042824986 scopus 로고    scopus 로고
    • Synthesis of lactococcin 972, a bacteriocin produced by Lactococcus lactis IPLA 972, depends on the expression of a plasmid-encoded bicistronic operon
    • B. Martinez, M. Fernandez, J.E. Suarez, A. Rodriguez, Synthesis of lactococcin 972, a bacteriocin produced by Lactococcus lactis IPLA 972, depends on the expression of a plasmid-encoded bicistronic operon, Microbiology 145 (1999) 3155-3161.
    • (1999) Microbiology , vol.145 , pp. 3155-3161
    • Martinez, B.1    Fernandez, M.2    Suarez, J.E.3    Rodriguez, A.4
  • 85
    • 0040516199 scopus 로고    scopus 로고
    • Lactococcin 972, a bacteriocin that inhibits septum formation in lactococci
    • B. Martinez, A. Rodriguez, J.E. Suarez, Lactococcin 972, a bacteriocin that inhibits septum formation in lactococci, Microbiology 146 (2000) 949-955.
    • (2000) Microbiology , vol.146 , pp. 949-955
    • Martinez, B.1    Rodriguez, A.2    Suarez, J.E.3
  • 86
    • 0032824975 scopus 로고    scopus 로고
    • Bacteriocins: Mechanism of membrane insertion and pore formation
    • G.N. Moll, W.N. Konings, A.J. Driessen, Bacteriocins: mechanism of membrane insertion and pore formation, Antonie Van Leeuwenhoek 76 (1999) 185-198.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 185-198
    • Moll, G.N.1    Konings, W.N.2    Driessen, A.J.3
  • 87
    • 0031771680 scopus 로고    scopus 로고
    • Variations in tolerance of Listeria monocytogenes to nisin, pediocin PA-1 and bavaricin A
    • M. Rasch, S. Knochel, Variations in tolerance of Listeria monocytogenes to nisin, pediocin PA-1 and bavaricin A, Lett. Appl. Microbiol. 27 (1998) 275-278.
    • (1998) Lett. Appl. Microbiol. , vol.27 , pp. 275-278
    • Rasch, M.1    Knochel, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.