메뉴 건너뛰기




Volumn 54, Issue 7, 2011, Pages 2399-2408

Structure-activity relationships of an antimicrobial peptide plantaricin s from two-peptide class IIb bacteriocins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCIN; PLANTARICIN S; UNCLASSIFIED DRUG;

EID: 79953770908     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm101540e     Document Type: Article
Times cited : (34)

References (56)
  • 1
    • 65149100197 scopus 로고    scopus 로고
    • Structure-function relationships of the non-lanthionine-containing peptide (class ii) bacteriocins produced by Gram-positive bacteria
    • Nissen-Meyer, J.; Rogne, P.; Oppegard, C.; Haugen, H. S.; Kristiansen, P. E. Structure-function relationships of the non-lanthionine-containing peptide (class ii) bacteriocins produced by Gram-positive bacteria Curr. Pharm. Biotechnol. 2009, 10, 19-37
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 19-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegard, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 2
    • 27244436751 scopus 로고    scopus 로고
    • Food microbiology: Bacteriocins: Developing innate immunity for food
    • DOI 10.1038/nrmicro1273, PII N1273
    • Cotter, P. D.; Hill, C.; Ross, R. P. Bacteriocins: developing innate immunity for food Nat. Rev. Microbiol. 2005, 3, 777-788 (Pubitemid 41518738)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.10 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 9
    • 0141906358 scopus 로고    scopus 로고
    • Mode of action of lactocin 705, a two-component bacteriocin from Lactobacillus casei CRL705
    • DOI 10.1016/S0168-1605(02)00479-8
    • Castellano, P.; Raya, R.; Vignolo, G. Mode of action of lactocin 705, a two-component bacteriocin from Lactobacillus casei CRL705 Int. J. Food Microbiol. 2003, 85, 35-43 (Pubitemid 37329366)
    • (2003) International Journal of Food Microbiology , vol.85 , Issue.1-2 , pp. 35-43
    • Castellano, P.1    Raya, R.2    Vignolo, G.3
  • 10
    • 0038182634 scopus 로고    scopus 로고
    • Differential roles of the two-component peptides of lactocin 705 in antimicrobial activity
    • DOI 10.1007/s00284-002-3844-0
    • Cuozzo, S. A.; Castellano, P.; Sesma, F. J.; Vignolo, G. M.; Raya, R. R. Differential roles of the two-component peptides of lactocin 705 in antimicrobial activity Curr. Microbiol. 2003, 46, 180-183 (Pubitemid 36919748)
    • (2003) Current Microbiology , vol.46 , Issue.3 , pp. 180-183
    • Cuozzo, S.A.1    Castellano, P.2    Sesma, F.J.M.3    Vignolo, G.M.4    Raya, R.R.5
  • 14
    • 42949144745 scopus 로고    scopus 로고
    • Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G
    • Rogne, P.; Fimland, G.; Nissen-Meyer, J.; Kristiansen, P. E. Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G Biochim. Biophys. Acta 2008, 1784, 543-554
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 543-554
    • Rogne, P.1    Fimland, G.2    Nissen-Meyer, J.3    Kristiansen, P.E.4
  • 16
    • 67849116711 scopus 로고    scopus 로고
    • Three-dimensional structure of the two-peptide bacteriocin plantaricin JK
    • Rogne, P.; Haugen, C.; Fimland, G.; Nissen-Meyer, J.; Kristiansen, P. E. Three-dimensional structure of the two-peptide bacteriocin plantaricin JK Peptides 2009, 30, 1613-1621
    • (2009) Peptides , vol.30 , pp. 1613-1621
    • Rogne, P.1    Haugen, C.2    Fimland, G.3    Nissen-Meyer, J.4    Kristiansen, P.E.5
  • 17
    • 42949148663 scopus 로고    scopus 로고
    • Mutational analysis of putative helix-helix interacting GxxxG-motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G
    • DOI 10.1021/bi800289w
    • Oppegard, C.; Schmidt, J.; Kristiansen, P. E.; Nissen-Meyer, J. Mutational analysis of putative helix-helix interacting GxxxG-Motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G Biochemistry 2008, 47, 5242-5249 (Pubitemid 351620761)
    • (2008) Biochemistry , vol.47 , Issue.18 , pp. 5242-5249
    • Oppegard, C.1    Schmidt, J.2    Kristiansen, P.E.3    Nissen-Meyer, J.4
  • 18
    • 77953181569 scopus 로고    scopus 로고
    • Structure analysis of the two-peptide bacteriocin lactococcin G by introducing d -amino acid residues
    • Oppegard, C.; Rogne, P.; Kristiansen, P. E.; Nissen-Meyer, J. Structure analysis of the two-peptide bacteriocin lactococcin G by introducing d -amino acid residues Microbiology 2010, 156, 1883-1889
    • (2010) Microbiology , vol.156 , pp. 1883-1889
    • Oppegard, C.1    Rogne, P.2    Kristiansen, P.E.3    Nissen-Meyer, J.4
  • 19
    • 0032005933 scopus 로고    scopus 로고
    • Amphiphilic ±-helices are important structural motifs in the a and β peptides that constitute the bacteriocin lactococcin G - Enhancement of helix formation upon ±-β interaction
    • DOI 10.1046/j.1432-1327.1998.2510565.x
    • Hauge, H. H.; Nissen-Meyer, J.; Nes, I. F.; Eijsink, V. G. Amphiphilic alpha-helices are important structural motifs in the alpha and beta peptides that constitute the bacteriocin lactococcin G - enhancement of helix formation upon alpha-beta interaction Eur. J. Biochem. 1998, 251, 565-572 (Pubitemid 28108948)
    • (1998) European Journal of Biochemistry , vol.251 , Issue.3 , pp. 565-572
    • Hauge, H.H.1    Nissen-Meyer, J.2    Nes, I.F.3    Eijsink, V.G.H.4
  • 20
    • 76649116857 scopus 로고    scopus 로고
    • The lactococcin g immunity protein recognizes specific regions in both peptides constituting the two-peptide bacteriocin lactococcin g
    • Oppegard, C.; Emanuelsen, L.; Thorbek, L.; Fimland, G.; Nissen-Meyer, J. The lactococcin g immunity protein recognizes specific regions in both peptides constituting the two-peptide bacteriocin lactococcin g Appl. Environ. Microbiol. 2010, 76, 1267-1273
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 1267-1273
    • Oppegard, C.1    Emanuelsen, L.2    Thorbek, L.3    Fimland, G.4    Nissen-Meyer, J.5
  • 22
    • 0028789406 scopus 로고
    • Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides
    • Jimenez-Diaz, R.; Ruiz-Barba, J. L.; Cathcart, D. P.; Holo, H.; Nes, I. F.; Sletten, K. H.; Warner, P. J. Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides Appl. Environ. Microbiol. 1995, 61, 4459-4463
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4459-4463
    • Jimenez-Diaz, R.1    Ruiz-Barba, J.L.2    Cathcart, D.P.3    Holo, H.4    Nes, I.F.5    Sletten, K.H.6    Warner, P.J.7
  • 23
    • 3142737226 scopus 로고    scopus 로고
    • Dynamic relationships among type IIa bacteriocins: Temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic ± helix as a receptor-binding region
    • DOI 10.1021/bi036018e
    • Kaur, K.; Andrew, L. C.; Wishart, D. S.; Vederas, J. C. Dynamic relationships among type IIa bacteriocins: temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic alpha helix as a receptor-binding region Biochemistry 2004, 43, 9009-9020 (Pubitemid 38924435)
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 9009-9020
    • Kaur, K.1    Andrew, L.C.2    Wishart, D.S.3    Vederas, J.C.4
  • 24
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer, J.; Holo, H.; Havarstein, L. S.; Sletten, K.; Nes, I. F. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides J. Bacteriol. 1992, 174, 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
  • 25
    • 34248158850 scopus 로고    scopus 로고
    • Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis
    • DOI 10.1128/AEM.02718-06
    • Oppegard, C.; Fimland, G.; Thorbaek, L.; Nissen-Meyer, J. Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis Appl. Environ. Microbiol. 2007, 73, 2931-2938 (Pubitemid 46718576)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.9 , pp. 2931-2938
    • Oppegard, C.1    Fimland, G.2    Thorbaek, L.3    Nissen-Meyer, J.4
  • 26
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama, N.; Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 2000, 287, 252-260 (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 27
    • 79953794903 scopus 로고    scopus 로고
    • http://www.ebi.ac.uk/Tools/em-boss/align/index.html.
  • 28
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N.; Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 1997, 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 29
    • 34948877554 scopus 로고    scopus 로고
    • Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins)
    • DOI 10.1016/j.bbamem.2007.05.023, PII S0005273607002003
    • Epand, R. F.; Savage, P. B.; Epand, R. M. Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins) Biochim. Biophys. Acta 2007, 1768, 2500-2509 (Pubitemid 47532031)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.10 , pp. 2500-2509
    • Epand, R.F.1    Savage, P.B.2    Epand, R.M.3
  • 30
    • 33748929313 scopus 로고    scopus 로고
    • Role of membrane lipids in the mechanism of bacterial species selective toxicity by two ±/β-antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.01.018, PII S0005273606000356
    • Epand, R. F.; Schmitt, M. A.; Gellman, S. H.; Epand, R. M. Role of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides Biochim. Biophys. Acta 2006, 1758, 1343-1350 (Pubitemid 44436066)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1343-1350
    • Epand, R.F.1    Schmitt, M.A.2    Gellman, S.H.3    Epand, R.M.4
  • 32
    • 29344464343 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a phosphatidylglycerol membrane
    • DOI 10.1016/j.febslet.2005.11.064, PII S0014579305014365
    • Elmore, D. E. Molecular dynamics simulation of a phosphatidylglycerol membrane FEBS Lett. 2006, 580, 144-148 (Pubitemid 43005327)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 144-148
    • Elmore, D.E.1
  • 33
    • 0032534843 scopus 로고    scopus 로고
    • Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: Molecular dynamics simulations
    • Tieleman, D. P.; Forrest, L. R.; Sansom, M. S.; Berendsen, H. J. Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: molecular dynamics simulations Biochemistry 1998, 37, 17554-17561
    • (1998) Biochemistry , vol.37 , pp. 17554-17561
    • Tieleman, D.P.1    Forrest, L.R.2    Sansom, M.S.3    Berendsen, H.J.4
  • 34
    • 66749128465 scopus 로고    scopus 로고
    • Interaction of an antimicrobial peptide with a model lipid bilayer using molecular dynamics simulation
    • Soliman, W.; Bhattacharjee, S.; Kaur, K. Interaction of an antimicrobial peptide with a model lipid bilayer using molecular dynamics simulation Langmuir 2009, 25, 6591-6595
    • (2009) Langmuir , vol.25 , pp. 6591-6595
    • Soliman, W.1    Bhattacharjee, S.2    Kaur, K.3
  • 35
    • 33847076821 scopus 로고    scopus 로고
    • Effect of NaCl and KCl on fate and growth/no growth interfaces of Listeria monocytogenes Scott A at different pH and nisin concentrations
    • Boziaris, I. S.; Skandamis, P. N.; Anastasiadi, M.; Nychas, G. J. Effect of NaCl and KCl on fate and growth/no growth interfaces of Listeria monocytogenes Scott A at different pH and nisin concentrations J. Appl. Microbiol. 2007, 102, 796-805
    • (2007) J. Appl. Microbiol. , vol.102 , pp. 796-805
    • Boziaris, I.S.1    Skandamis, P.N.2    Anastasiadi, M.3    Nychas, G.J.4
  • 36
    • 34249294472 scopus 로고    scopus 로고
    • Optimum bacteriocin production by Lactobacillus plantarum 17.2b requires absence of NaCl and apparently follows a mixed metabolite kinetics
    • DOI 10.1016/j.jbiotec.2007.01.041, PII S0168165607001605
    • Delgado, A.; Arroyo Lopez, F. N.; Brito, D.; Peres, C.; Fevereiro, P.; Garrido-Fernandez, A. Optimum bacteriocin production by Lactobacillus plantarum 17.2b requires absence of NaCl and apparently follows a mixed metabolite kinetics J. Biotechnol. 2007, 130, 193-201 (Pubitemid 46813172)
    • (2007) Journal of Biotechnology , vol.130 , Issue.2 , pp. 193-201
    • Delgado, A.1    Arroyo Lopez, F.N.2    Brito, D.3    Peres, C.4    Fevereiro, P.5    Garrido-Fernandez, A.6
  • 37
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • DOI 10.1007/S008940100045
    • Lindahl, E.; Hess, B.; van der Spoel, D. GROMACS 3.0: a package for molecular simulation and trajectory analysis J. Mol. Model. 2001, 7, 306-317 (Pubitemid 36153547)
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 40
    • 79953786249 scopus 로고    scopus 로고
    • MSI, Molecular Simulations Inc.
    • MSI, Molecular Simulations Inc., 1998.
    • (1998)
  • 42
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C.; Barber, J. D.; Barton, G. J. The Jpred 3 secondary structure prediction server Nucleic Acids Res. 2008, 36, W197-W201
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 43
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sonnichsen, F. D.; Van Eyk, J. E.; Hodges, R. S.; Sykes, B. D. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide Biochemistry 1992, 31, 8790-8798
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 44
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities from trifluoroethanol titration curves
    • Jasanoff, A.; Fersht, A. R. Quantitative determination of helical propensities from trifluoroethanol titration curves Biochemistry 1994, 33, 2129-2135
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 45
    • 0032890798 scopus 로고    scopus 로고
    • Membrane-mimicking entities induce structuring of the two-peptide bacteriocins plantaricin E/F and plantaricin J/K
    • Hauge, H. H.; Mantzilas, D.; Eijsink, V. G.; Nissen-Meyer, J. Membrane-mimicking entities induce structuring of the two-peptide bacteriocins plantaricin E/F and plantaricin J/K J. Bacteriol. 1999, 181, 740-747 (Pubitemid 29061554)
    • (1999) Journal of Bacteriology , vol.181 , Issue.3 , pp. 740-747
    • Hauge, H.H.1    Mantzilas, D.2    Eijsink, V.G.H.3    Nissen-Meyer, J.4
  • 46
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • DOI 10.1021/bi025856q
    • Fimland, G.; Eijsink, V. G.; Nissen-Meyer, J. Mutational analysis of the role of tryptophan residues in an antimicrobial peptide Biochemistry 2002, 41, 9508-9515 (Pubitemid 34810026)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.H.2    Nissen-Meyer, J.3
  • 47
    • 15744401646 scopus 로고    scopus 로고
    • The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum
    • DOI 10.1074/jbc.M412712200
    • Johnsen, L.; Fimland, G.; Nissen-Meyer, J. The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum J. Biol. Chem. 2005, 280, 9243-9250 (Pubitemid 40409615)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 48
    • 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
    • DOI 10.1021/bi971263h
    • Gallagher, N. L. F.; Sailer, M.; Niemczura, W. P.; Nakashima, T. T.; Stiles, M. E.; Vederas, J. C. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphophocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria Biochemistry 1997, 36, 15062-15072 (Pubitemid 27527970)
    • (1997) Biochemistry , vol.36 , Issue.49 , 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
  • 49
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of Carnobacteriocin B2 and implications for structure-activity relationship among type IIa bacteriocins from lactic acid bacteria
    • Wang, Y. J.; Henz, M. E.; Gallagher, N. L. F.; Chai, S. Y.; Gibbs, A. C.; Yan, L. Z.; Stiles, M. E.; Wishart, D. S.; Vederas, J. C. Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria Biochemistry 1999, 38, 15438-15447 (Pubitemid 129503584)
    • (1999) Biochemistry , vol.38 , Issue.47 , pp. 15438-15447
    • Wang, Y.1    Henz, M.E.2    Fregeau Gallagher, N.L.3    Chai, S.4    Gibbs, A.C.5    Yan, L.Z.6    Stiles, M.E.7    Wishart, D.S.8    Vederas, J.C.9
  • 50
    • 0035923448 scopus 로고    scopus 로고
    • Conformational changes in pediocin AcH upon vesicle binding and approximation of the membrane-bound structure in detergent micelles
    • DOI 10.1021/bi011031p
    • Watson, R. M.; Woody, R. W.; Lewis, R. V.; Bohle, D. S.; Andreotti, A. H.; Ray, B.; Miller, K. W. Conformational changes in pediocin AcH upon vesicle binding and approximation of the membrane-bound structure in detergent micelles Biochemistry 2001, 40, 14037-14046 (Pubitemid 33078875)
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 14037-14046
    • Watson, R.M.1    Woody, R.W.2    Lewis, R.V.3    Scott Bohle, D.4    Andreotti, A.H.5    Ray, B.6    Miller, K.W.7
  • 51
    • 0031782073 scopus 로고    scopus 로고
    • Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a
    • Papathanasopoulos, M. A.; Dykes, G. A.; Revol-Junelles, A. M.; Delfour, A.; von Holy, A.; Hastings, J. W. Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a Microbiology 1998, 144 (Part 5) 1343-1348 (Pubitemid 28233838)
    • (1998) Microbiology , vol.144 , Issue.5 , pp. 1343-1348
    • Papathanasopoulos, M.A.1    Dykes, G.A.2    Revol-Junelles, A.-M.3    Delfour, A.4    Von Holy, A.5    Hastings, J.W.6
  • 52
    • 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
    • Fleury, Y.; Dayem, M. A.; Montagne, J. J.; Chaboisseau, E.; Le Caer, J. P.; Nicolas, P.; Delfour, A. Covalent structure, synthesis, and structure-function studies of mesentericin Y 105(37), a defensive peptide from Gram-positive bacteria Leuconostoc mesenteroides J. Biol. Chem. 1996, 271, 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    Delfour, A.7
  • 53
    • 0031793223 scopus 로고    scopus 로고
    • The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the Center toward the C terminus
    • Fimland, G.; Jack, R.; Jung, G.; Nes, I. F.; Nissen-Meyer, J. The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C terminus Appl. Environ. Microbiol. 1998, 64, 5057-5060 (Pubitemid 28557887)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.12 , pp. 5057-5060
    • Fimland, G.1    Jack, R.2    Jung, G.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 54
    • 69949137695 scopus 로고    scopus 로고
    • Class II one-peptide bacteriocins target a phylogenetically defined subgroup of mannose phosphotransferase systems on sensitive cells
    • Kjos, M.; Nes, I. F.; Diep, D. B. Class II one-peptide bacteriocins target a phylogenetically defined subgroup of mannose phosphotransferase systems on sensitive cells Microbiology 2009, 155, 2949-2961
    • (2009) Microbiology , vol.155 , pp. 2949-2961
    • Kjos, M.1    Nes, I.F.2    Diep, D.B.3
  • 55
    • 4444341230 scopus 로고    scopus 로고
    • Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis
    • Ramnath, M.; Arous, S.; Gravesen, A.; Hastings, J. W.; Hechard, Y. Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis Microbiology 2004, 150, 2663-2668 (Pubitemid 39173269)
    • (2004) Microbiology , vol.150 , Issue.8 , pp. 2663-2668
    • Ramnath, M.1    Arous, S.2    Gravesen, A.3    Hastings, J.W.4    Hechard, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.