메뉴 건너뛰기




Volumn 75, Issue 7, 2009, Pages 1811-1819

Insights into structure-activity relationships in the C-terminal region of divercin V41, a class IIa bacteriocin with high-level antilisterial activity

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; AMINATION; AMINES; AMINO ACIDS; BIOCHEMISTRY; DICHROISM; ELECTROPHORESIS; ESCHERICHIA COLI; GELATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HIGH PRESSURE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; ORGANIC ACIDS; POLYMERS; PROTEINS; SODIUM; SODIUM SULFATE;

EID: 63849304558     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02266-08     Document Type: Article
Times cited : (15)

References (60)
  • 1
    • 0035077071 scopus 로고    scopus 로고
    • Influence of physico-chemical factors on the oligomerization and biological activity of bacteriocin AS-48
    • Abriouel, H., E. Valdivia, A. Galvez, and M. Maqueda. 2001. Influence of physico-chemical factors on the oligomerization and biological activity of bacteriocin AS-48. Curr. Microbiol. 42:89-95.
    • (2001) Curr. Microbiol , vol.42 , pp. 89-95
    • Abriouel, H.1    Valdivia, E.2    Galvez, A.3    Maqueda, M.4
  • 2
    • 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 Camobacterium divergens V41
    • Bhugaloo-Vial, P., J. P. Douliez, D. Moll, X. Dousset, P. Boyaval, and D. Marion. 1999. Delineation of key amino acid side chains and peptide domains for antimicrobial properties of divercin V41. a pediocin-like bacteriocin secreted by Camobacterium divergens V41. Appl. Environ. Microbiol. 65:2895-2900.
    • (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
  • 3
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
    • Buck, M. 1998. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31:297-355.
    • (1998) Q. Rev. Biophys , vol.31 , pp. 297-355
    • Buck, M.1
  • 4
    • 34249080139 scopus 로고    scopus 로고
    • Identification of new genes associated with intermediate resistance of Enterococcus faecalis to divercin V41, a pediocin-like bacteriocin
    • Calvez, S., A. Rincé, Y. Auffray, H. Prévost, and D. Drider. 2007. Identification of new genes associated with intermediate resistance of Enterococcus faecalis to divercin V41, a pediocin-like bacteriocin. Microbiology 153:1609-1618.
    • (2007) Microbiology , vol.153 , pp. 1609-1618
    • Calvez, S.1    Rincé, A.2    Auffray, Y.3    Prévost, H.4    Drider, D.5
  • 5
    • 0036950298 scopus 로고    scopus 로고
    • Selection of Escherichia coli-inhibiting strains of Lactobacillus paracasei subsp. paracasei
    • Caridi, A. 2002. Selection of Escherichia coli-inhibiting strains of Lactobacillus paracasei subsp. paracasei. J. Ind. Microbiol. Biotechnol. 29:303-308.
    • (2002) J. Ind. Microbiol. Biotechnol , vol.29 , pp. 303-308
    • Caridi, A.1
  • 7
    • 0030698620 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum
    • Cintas, L. M., P. Casaus, L. S. Håvarstein, P. E. Hernández, and I. F. Nes. 1997. Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum. Appl. Environ. Microbiol. 63:4321-4330.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 4321-4330
    • Cintas, L.M.1    Casaus, P.2    Håvarstein, L.S.3    Hernández, P.E.4    Nes, I.F.5
  • 9
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D., C. Hill, and R. P. Ross. 2005. 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
  • 10
    • 0035216679 scopus 로고    scopus 로고
    • 54- dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 147:3263-3269.
    • 54- dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 147:3263-3269.
  • 14
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland, G., V. G. Eijsink, and J. Nissen-Meyer. 2002. Mutational analysis of the role of tryptophan residues in an antimicrobial peptide. Biochemistry 41:9508-9515.
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 15
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificitv
    • Fimland, G., O. R. Blingsmo, K. Sletten, G. Jung, I. F. Nes, and J. Nissen-Meyer. 1996. New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: the C-terminal region is important for determining specificitv. Appl. Environ. Microbiol. 62:3313-3318.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.R.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 16
    • 0034005323 scopus 로고    scopus 로고
    • A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum
    • Fimland, G., L. Johnsen, L. Axelsson, M. B. Brurberg, I. F. Nes, V. G. H. Eijsink, and J. Nissen-Meyer. 2000. A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum. J. Bacteriol. 182:2643-2648.
    • (2000) J. Bacteriol , vol.182 , pp. 2643-2648
    • Fimland, G.1    Johnsen, L.2    Axelsson, L.3    Brurberg, M.B.4    Nes, I.F.5    Eijsink, V.G.H.6    Nissen-Meyer, J.7
  • 17
    • 0029891059 scopus 로고    scopus 로고
    • Fleury, Y., M. A. Dayem, J. J. Montagne, E. Chaboisseau, J. P. Le Caer, P. Nicolas, P., and A. Delfour. 1996. Covalent structure, synthesis, and structure-function studies of mesentericin Y105, a defensive peptide from gram-positive bacteria Leuconostoc mesenteroides. J. Biol. Chem. 271:14421-14429.
    • Fleury, Y., M. A. Dayem, J. J. Montagne, E. Chaboisseau, J. P. Le Caer, P. Nicolas, P., and A. Delfour. 1996. Covalent structure, synthesis, and structure-function studies of mesentericin Y105, a defensive peptide from gram-positive bacteria Leuconostoc mesenteroides. J. Biol. Chem. 271:14421-14429.
  • 18
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Fregeau Gallagher, N. L., M. Sailer, W. P. Niemczura, T. T. Nakashima, M. E. Stiles, and J. C. Vederas. 1997. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria. Biochemistry 36:15062-15072.
    • (1997) 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
  • 19
    • 0035955375 scopus 로고    scopus 로고
    • Glaser, P., L. Frangeul, C. Buchrieser, C. Rusniok, A. Amend, F. Baquero, P. Berche, H. Bloecker, P. Brandt, T. Chakraborty, A. Charbit, F. Chetouani, E. Couvé, A. de Daruvar, P. Dehoux, F. Domann, G. Domínguez-Bernal, E. Duchaud, L. Durant, O. Dussurget, K. D. Entian, H. Fsihi, F. García-del Portillo, P. Garrido, L. Gautier, W. Goebel, N. Gómez-López, T. Hain, J. Hauf, D. Jackson, L. M. Jones, U. Kaerst, J. Kreft, M. Kuhn, F. Kunst, G. Kurapkat, F. Madueno, A. Maitournam, J. M. Vicente, E. Ng, H. Nedjari, G. Nordsiek, S. Novella, B. de Pablos, J. C. Pérez-Diaz, R. Purcell, B. Remmel, M. Rose, T. Schlueter, N. Simoes, A. Tierrez, J. A. Vázquez-Boland, H. Voss, J. Wehland, and P. Cossart. 2001. Comparative genomics of Listeria species. Science 294:849-852.
    • Glaser, P., L. Frangeul, C. Buchrieser, C. Rusniok, A. Amend, F. Baquero, P. Berche, H. Bloecker, P. Brandt, T. Chakraborty, A. Charbit, F. Chetouani, E. Couvé, A. de Daruvar, P. Dehoux, F. Domann, G. Domínguez-Bernal, E. Duchaud, L. Durant, O. Dussurget, K. D. Entian, H. Fsihi, F. García-del Portillo, P. Garrido, L. Gautier, W. Goebel, N. Gómez-López, T. Hain, J. Hauf, D. Jackson, L. M. Jones, U. Kaerst, J. Kreft, M. Kuhn, F. Kunst, G. Kurapkat, F. Madueno, A. Maitournam, J. M. Vicente, E. Ng, H. Nedjari, G. Nordsiek, S. Novella, B. de Pablos, J. C. Pérez-Diaz, R. Purcell, B. Remmel, M. Rose, T. Schlueter, N. Simoes, A. Tierrez, J. A. Vázquez-Boland, H. Voss, J. Wehland, and P. Cossart. 2001. Comparative genomics of Listeria species. Science 294:849-852.
  • 20
    • 38349095584 scopus 로고    scopus 로고
    • BACT1BASE: A new web-accessible data base for bacteriocin characterization
    • Hammami, R., A. Zouhir, J. Benhamida, and I. Fliss. 2007. BACT1BASE: a new web-accessible data base for bacteriocin characterization. BMC Microbiol. 7:89.
    • (2007) BMC Microbiol , vol.7 , pp. 89
    • Hammami, R.1    Zouhir, A.2    Benhamida, J.3    Fliss, I.4
  • 21
    • 28944447119 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A
    • Haugen, H. E., G. Fimland, J. Nissen-Meyer, and P. E. Kristiansen. 2005. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A. Biochemistry 44:16149-16157.
    • (2005) Biochemistry , vol.44 , pp. 16149-16157
    • Haugen, H.E.1    Fimland, G.2    Nissen-Meyer, J.3    Kristiansen, P.E.4
  • 22
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Håvarstein, L. S., D. B. Diep, and L F. Nes. 1995. A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates 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, L.F.3
  • 24
    • 0028787147 scopus 로고
    • Tryptophan hydrogen bonding and electric dipole moments: Functional roles in the gramicidin channel and implications for membrane proteins
    • Hu, W., and T. A. Cross. 1995. Tryptophan hydrogen bonding and electric dipole moments: functional roles in the gramicidin channel and implications for membrane proteins. Biochemistry 34:14147-14155.
    • (1995) Biochemistry , vol.34 , pp. 14147-14155
    • Hu, W.1    Cross, T.A.2
  • 25
    • 0028882402 scopus 로고
    • Tryptophan dynamics and structural refinement in a lipid bilayer environment: Solid state NMR of the gramicidin channel
    • Hu, W., N. D. Lazo, and T. A. Cross. 1995. Tryptophan dynamics and structural refinement in a lipid bilayer environment: solid state NMR of the gramicidin channel. Biochemistry 34:14138-14146.
    • (1995) Biochemistry , vol.34 , pp. 14138-14146
    • Hu, W.1    Lazo, N.D.2    Cross, T.A.3
  • 27
    • 0027478576 scopus 로고
    • The role of proline 345 in diphtheria toxin translocation
    • Johnson, V. G., P. J. Nicholls, W. H. Habig, and R. J. Youle. 1993. The role of proline 345 in diphtheria toxin translocation. J. Biol. Chem. 268:3514-3519.
    • (1993) J. Biol. Chem , vol.268 , pp. 3514-3519
    • Johnson, V.G.1    Nicholls, P.J.2    Habig, W.H.3    Youle, R.J.4
  • 28
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 29
    • 0035461360 scopus 로고    scopus 로고
    • Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743
    • Kalmokoff, M. L., S. K. Banerjee, T. Cyr, M. A. Hefford, and T. Gleeson. 2001. Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743. Appl. Environ. Microbiol. 67:4041-4047.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 4041-4047
    • Kalmokoff, M.L.1    Banerjee, S.K.2    Cyr, T.3    Hefford, M.A.4    Gleeson, T.5
  • 30
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer, T. R. 1993. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12:39-85.
    • (1993) FEMS Microbiol. Rev , vol.12 , pp. 39-85
    • Klaenhammer, T.R.1
  • 31
    • 0000910944 scopus 로고    scopus 로고
    • Bacteriocin production by Lactococcus lactis KCA2386 isolated from white kimachi
    • Ko, S.-H., and C. Ahn. 2000. Bacteriocin production by Lactococcus lactis KCA2386 isolated from white kimachi. Food Sci. Biotechnol. 9:263-269.
    • (2000) Food Sci. Biotechnol , vol.9 , pp. 263-269
    • Ko, S.-H.1    Ahn, C.2
  • 32
    • 0030015420 scopus 로고    scopus 로고
    • Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment
    • Li, S. C., N. K. Goto, K. A. Williams, and C. M. Deber. 1996. Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment. Proc. Natl. Acad. Sci. USA 93:6676-66781.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6676-66781
    • Li, S.C.1    Goto, N.K.2    Williams, K.A.3    Deber, C.M.4
  • 33
    • 0035957526 scopus 로고    scopus 로고
    • Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin
    • Lu, H., T. Marti, and P. J. Booth. 2001. Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin. J. Mol. Biol. 308:437-446.
    • (2001) J. Mol. Biol , vol.308 , pp. 437-446
    • Lu, H.1    Marti, T.2    Booth, P.J.3
  • 34
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., K. Bryson, and D. T. Jones. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 35
    • 0035961632 scopus 로고    scopus 로고
    • Detection and preliminary characterization of a bacteriocin (plantaricin 35d) produced by a Lactobacillus plantarum strain
    • Messi, P., M. Bondi, C. Sabia, R. Battini, and G. Manicardi. 2001. Detection and preliminary characterization of a bacteriocin (plantaricin 35d) produced by a Lactobacillus plantarum strain. Int. J. Food Microbiol. 64:193-198.
    • (2001) Int. J. Food Microbiol , vol.64 , pp. 193-198
    • Messi, P.1    Bondi, M.2    Sabia, C.3    Battini, R.4    Manicardi, G.5
  • 36
    • 0031745937 scopus 로고    scopus 로고
    • Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity
    • Miller, K. W., R Schamber, O. Osmanagaoglu, and B. Ray. 1998. Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity. Appl. Environ. Microbiol. 64:1997-2005.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 1997-2005
    • Miller, K.W.1    Schamber, R.2    Osmanagaoglu, O.3    Ray, B.4
  • 37
    • 1242307761 scopus 로고    scopus 로고
    • Enhancement of antibiotic activity by sub-lethal concentrations of enterocin CRL35
    • Minahk, C. J., F. Dupuy, and R. D. Morero. 2004. Enhancement of antibiotic activity by sub-lethal concentrations of enterocin CRL35. J. Antimicrob. Chemother. 53:240-246.
    • (2004) J. Antimicrob. Chemother , vol.53 , pp. 240-246
    • Minahk, C.J.1    Dupuy, F.2    Morero, R.D.3
  • 38
    • 4143107127 scopus 로고    scopus 로고
    • Mutational analysis of mesentericin Y105. an anti-Listeria bacteriocin. for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction
    • Morisset, D., J. M. Berjeaud, D. Marion, C. Lacombe, and J. Frére. 2004. Mutational analysis of mesentericin Y105. an anti-Listeria bacteriocin. for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction. Appl. Environ. Microbiol. 70:4672-4680.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 4672-4680
    • Morisset, D.1    Berjeaud, J.M.2    Marion, D.3    Lacombe, C.4    Frére, J.5
  • 39
    • 0033857685 scopus 로고    scopus 로고
    • Class II antimicrobial peptides from lactic acid bacteria
    • Nes, I. F., and H. Holo. 2000. Class II antimicrobial peptides from lactic acid bacteria. Biopolymers 55:50-61.
    • (2000) Biopolymers , vol.55 , pp. 50-61
    • Nes, I.F.1    Holo, H.2
  • 40
    • 0029109787 scopus 로고
    • Evidence for two bacteriocins produced by Carnobacterium divergens V41 and Carnobacterium piscicola V1 isolated from fish and active against Listeria monocytogenes
    • Pilet, M. F., X. Dousset, R. Barré, G. Novel, M. Desmazeaud, and J. C. Piard. 1995. Evidence for two bacteriocins produced by Carnobacterium divergens V41 and Carnobacterium piscicola V1 isolated from fish and active against Listeria monocytogenes. J. Food Prot. 3:256-262.
    • (1995) J. Food Prot , vol.3 , pp. 256-262
    • Pilet, M.F.1    Dousset, X.2    Barré, R.3    Novel, G.4    Desmazeaud, M.5    Piard, J.C.6
  • 41
    • 43949083747 scopus 로고    scopus 로고
    • NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecvlphosphocholine micelles
    • Porcelli, F., R. Verardi, L. Shi, K. A. Henzler-Widman, A. Ramamoorthy, and G. Veglia. 2008. NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecvlphosphocholine micelles. Biochemistry 47:5565-5572.
    • (2008) Biochemistry , vol.47 , pp. 5565-5572
    • Porcelli, F.1    Verardi, R.2    Shi, L.3    Henzler-Widman, K.A.4    Ramamoorthy, A.5    Veglia, G.6
  • 42
    • 0031030583 scopus 로고    scopus 로고
    • Effect of amino acid substitutions on the activity of carnobacteriocin B2. Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli
    • Quadri, L. E., L. Z. Yan, M. E. Stiles, and J. C. Vederas. 1997. Effect of amino acid substitutions on the activity of carnobacteriocin B2. Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli. J. Biol. Chem. 272:3384-3388.
    • (1997) J. Biol. Chem , vol.272 , pp. 3384-3388
    • Quadri, L.E.1    Yan, L.Z.2    Stiles, M.E.3    Vederas, J.C.4
  • 43
    • 23044477877 scopus 로고    scopus 로고
    • Evidence on correlation between number of disulfide bridge and toxicity of class 11a bacteriocins
    • Richard, C., R. Cañon, K. Naghmouchi, D. Bertrand, H. Prévost, and D. Drider. 2006. Evidence on correlation between number of disulfide bridge and toxicity of class 11a bacteriocins. Food Microbiol. 23:175-183.
    • (2006) Food Microbiol , vol.23 , pp. 175-183
    • Richard, C.1    Cañon, R.2    Naghmouchi, K.3    Bertrand, D.4    Prévost, H.5    Drider, D.6
  • 44
    • 3042651591 scopus 로고    scopus 로고
    • Heterologous expression and purification of active divercin V41, a class IIa bacteriocin encoded by a synthetic gene in Escherichia coli
    • Richard, C., D. Drider, K. Elmorjani, D. Marion, and H. Prévost. 2004. Heterologous expression and purification of active divercin V41, a class IIa bacteriocin encoded by a synthetic gene in Escherichia coli. J. Bacteriol. 186:4276-4284.
    • (2004) J. Bacteriol , vol.186 , pp. 4276-4284
    • Richard, C.1    Drider, D.2    Elmorjani, K.3    Marion, D.4    Prévost, H.5
  • 45
    • 0345869635 scopus 로고    scopus 로고
    • Generation and utilization of polyclonal antibodies to a synthetic C-terminal amino acid fragment of divercin V41, a class IIa bacteriocin
    • Richard, C., D. Drider, I. Fliss, S. Denery, and H. Prévost. 2004. Generation and utilization of polyclonal antibodies to a synthetic C-terminal amino acid fragment of divercin V41, a class IIa bacteriocin. Appl. Environ. Microbiol. 70:248-254.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 248-254
    • Richard, C.1    Drider, D.2    Fliss, I.3    Denery, S.4    Prévost, H.5
  • 47
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl, H. G., and G. Bierbaum. 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
  • 51
    • 0022591495 scopus 로고
    • The classification of amino acid conservation
    • Taylor, W. R. 1986. The classification of amino acid conservation. J. Theor. Biol. 119:205-218.
    • (1986) J. Theor. Biol , vol.119 , pp. 205-218
    • Taylor, W.R.1
  • 52
    • 5444266832 scopus 로고    scopus 로고
    • Effect of medium components on bacteriocin production by Lactobacillus pentasus ST151BR, a strain isolated from beer produced by the fermentation of maize, barley and soy flour
    • Todorov, S. D., and L. M. T. Dicks. 2004. Effect of medium components on bacteriocin production by Lactobacillus pentasus ST151BR, a strain isolated from beer produced by the fermentation of maize, barley and soy flour. World J. Microbiol. Biotechnol. 20:643-650.
    • (2004) World J. Microbiol. Biotechnol , vol.20 , pp. 643-650
    • Todorov, S.D.1    Dicks, L.M.T.2
  • 53
    • 33144455595 scopus 로고    scopus 로고
    • Determination of essential and variable residues in pediocin PA-1 by NNK scanning
    • Tominaga, T., and Y. Hatakeyama. 2006. Determination of essential and variable residues in pediocin PA-1 by NNK scanning. Appl. Environ. Microbiol. 72:1141-1147.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 1141-1147
    • Tominaga, T.1    Hatakeyama, Y.2
  • 54
    • 0141817944 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge
    • Uteng, M., H. H. Hauge, P. R. L. Markwick, G. Fimland, D. Mantzilas, J. Nissen-Meyer, and C. Muhle-Goll. 2003. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge. Biochemistry 42:11417-11426.
    • (2003) Biochemistry , vol.42 , pp. 11417-11426
    • Uteng, M.1    Hauge, H.H.2    Markwick, P.R.L.3    Fimland, G.4    Mantzilas, D.5    Nissen-Meyer, J.6    Muhle-Goll, C.7
  • 56
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria
    • Wang, Y., M. E. Henz, N. L. Gallagher, S. Chai, A. C. Gibbs, L. Z. Yan, M. E. Stiles, D. S. Wishart, and J. C. Vederas. 1999. Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria. Biochemistry 38:15438-15447.
    • (1999) Biochemistry , vol.38 , pp. 15438-15447
    • Wang, Y.1    Henz, M.E.2    Gallagher, N.L.3    Chai, S.4    Gibbs, A.C.5    Yan, L.Z.6    Stiles, M.E.7    Wishart, D.S.8    Vederas, J.C.9
  • 57
    • 0035923448 scopus 로고    scopus 로고
    • Conformational changes in pediocin AcH upon vesicle binding and approximation of the membrane-bound structure in detergent micelles
    • Watson, R. M., R. W. Woody, R. V. Lewis, D. S. Bohle, A. H. Andreotti, B. Ray, and K. W. Miller. 2001. Conformational changes in pediocin AcH upon vesicle binding and approximation of the membrane-bound structure in detergent micelles. Biochemistry 40:14037-14046.
    • (2001) Biochemistry , vol.40 , pp. 14037-14046
    • Watson, R.M.1    Woody, R.W.2    Lewis, R.V.3    Bohle, D.S.4    Andreotti, A.H.5    Ray, B.6    Miller, K.W.7
  • 58
    • 3242877618 scopus 로고    scopus 로고
    • Dichroweb, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and B. A. Wallace. 2004. Dichroweb, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32:W668-W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 59
    • 0018945455 scopus 로고
    • Recombination-deficient mutant of Streptococcus faecalis
    • Yagi, Y., and D. B. Clewell. 1980. Recombination-deficient mutant of Streptococcus faecalis. J. Bacteriol. 143:966-970.
    • (1980) J. Bacteriol , vol.143 , pp. 966-970
    • Yagi, Y.1    Clewell, D.B.2
  • 60
    • 36249028708 scopus 로고    scopus 로고
    • Production of recombinant bacteriocin divercin V41 by high cell density Escherichia coli batch and fed-batch cultures
    • Yildirim, S., D. Konrad, S. Calvez, D. Drider, H. Prévost, and C. Lacroix. 2007. Production of recombinant bacteriocin divercin V41 by high cell density Escherichia coli batch and fed-batch cultures. Appl. Microbiol. Biotechnol. 77:525-531.
    • (2007) Appl. Microbiol. Biotechnol , vol.77 , pp. 525-531
    • Yildirim, S.1    Konrad, D.2    Calvez, S.3    Drider, D.4    Prévost, H.5    Lacroix, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.