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Volumn 70, Issue 6, 2004, Pages 3292-3297

Novel expression system for large-scale production and purification of recombinant class IIa bacteriocins and its application to piscicolin 126

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BACTERIA; ESCHERICHIA COLI; GENES; PROTEINS; PURIFICATION;

EID: 2942592015     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.6.3292-3297.2004     Document Type: Article
Times cited : (41)

References (39)
  • 1
    • 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
    • Abee, T., T. R. Klaenhammer, and L. Letellier. 1994. 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. 60:1006-1013.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1006-1013
    • Abee, T.1    Klaenhammer, T.R.2    Letellier, L.3
  • 4
    • 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
  • 5
    • 0025960702 scopus 로고
    • Mode of action of pediocin AcH from Pediococcus acidilactici H on sensitive bacterial stains
    • Bhunia, A. K., M. C. Johnson, B. Ray, and N. Kalchayanand. 1991. Mode of action of pediocin AcH from Pediococcus acidilactici H on sensitive bacterial stains. J. Appl. Bacteriol. 70:25-33.
    • (1991) J. Appl. Bacteriol. , vol.70 , pp. 25-33
    • Bhunia, A.K.1    Johnson, M.C.2    Ray, B.3    Kalchayanand, N.4
  • 7
    • 0031034782 scopus 로고    scopus 로고
    • Purification of bacteriocins of lactic acid bacteria: Problems and pointers
    • Carolissen-Mackay, V., G. Arendse, and J. W. Hastings. 1997. Purification of bacteriocins of lactic acid bacteria: problems and pointers. Int. J. Food Microbiol. 34:1-16.
    • (1997) Int. J. Food Microbiol. , vol.34 , pp. 1-16
    • Carolissen-Mackay, V.1    Arendse, G.2    Hastings, J.W.3
  • 8
    • 0028868950 scopus 로고
    • Efflux of ions and ATP depletion induced by pediocin PA-1 are concomitant with cell death in Listeria monocytogenes Scott A
    • Chen, Y., and T. J. Montville. 1995. Efflux of ions and ATP depletion induced by pediocin PA-1 are concomitant with cell death in Listeria monocytogenes Scott A. J. Appl. Bacteriol. 79:684-690.
    • (1995) J. Appl. Bacteriol. , vol.79 , pp. 684-690
    • Chen, Y.1    Montville, T.J.2
  • 9
    • 0029931089 scopus 로고    scopus 로고
    • A food-grade process for isolation and partial purification of bacteriocins of lactic acid bacteria that uses diatomite calcium silicate
    • Coventry, M. J., J. B. Gordon, M. Alexander, M. W. Hickey, and J. Wan. 1996. A food-grade process for isolation and partial purification of bacteriocins of lactic acid bacteria that uses diatomite calcium silicate. Appl. Environ. Microbiol. 62:1764-1769.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1764-1769
    • Coventry, M.J.1    Gordon, J.B.2    Alexander, M.3    Hickey, M.W.4    Wan, J.5
  • 10
    • 0030034707 scopus 로고    scopus 로고
    • Production of brevicin 286 by Lactobacillus brevis VB286 and partial characterization
    • Coventry, M. J., J. Wan, J. B. Gordon, R. F. Mawson, and M. W. Hickey. 1996. Production of brevicin 286 by Lactobacillus brevis VB286 and partial characterization. J. Appl. Bacteriol. 80:91-98.
    • (1996) J. Appl. Bacteriol. , vol.80 , pp. 91-98
    • Coventry, M.J.1    Wan, J.2    Gordon, J.B.3    Mawson, R.F.4    Hickey, M.W.5
  • 11
    • 0033661296 scopus 로고    scopus 로고
    • The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins
    • Dalet, K., C. Briand, Y. Cenatiempo, and Y. Hechard. 2000. The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins. Curr. Microbiol. 41:441-443.
    • (2000) Curr. Microbiol. , vol.41 , pp. 441-443
    • Dalet, K.1    Briand, C.2    Cenatiempo, Y.3    Hechard, Y.4
  • 12
    • 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
    • Dalet, K., Y. Cenatiempo, P. Cossart, and Y. Hechard. 2001. A sigma(54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 147:3263-3269.
    • (2001) Microbiology , vol.147 , pp. 3263-3269
    • Dalet, K.1    Cenatiempo, Y.2    Cossart, P.3    Hechard, Y.4
  • 13
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman, A. I., W. A. Prinz, D. Belin, and J. Beckwith. 1993. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262:1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 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 specificity
    • 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 specificity. 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
    • 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., R. Jack, G. Jung, I. F. Nes, and J. Nissen-Meyer. 1998. 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. 64:5057-5060.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 5057-5060
    • Fimland, G.1    Jack, R.2    Jung, G.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 17
    • 0034120704 scopus 로고    scopus 로고
    • Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative beta-glucoside-specific PTS system
    • Gravesen, A., P. Warthoe, S. Knochel, and K. Thirstrup. 2000. Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative beta-glucoside-specific PTS system, Microbiology 146:1381-1389,
    • (2000) Microbiology , vol.146 , pp. 1381-1389
    • Gravesen, A.1    Warthoe, P.2    Knochel, S.3    Thirstrup, K.4
  • 18
    • 13144267947 scopus 로고
    • The cyanogen bromide reaction
    • Gross, E. 1967. The cyanogen bromide reaction. Methods Enzymol. 11:238-255.
    • (1967) Methods Enzymol. , vol.11 , pp. 238-255
    • Gross, E.1
  • 19
    • 0034127005 scopus 로고    scopus 로고
    • Method for rapid purification of class IIa bacteriocins and comparison of their activities
    • Guyonnet, D., C. Fremaux, Y. Cenatiempo, and J. M. Berjeaud. 2000. Method for rapid purification of class IIa bacteriocins and comparison of their activities. Appl. Environ. Microbiol. 66:1744-1748.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1744-1748
    • Guyonnet, D.1    Fremaux, C.2    Cenatiempo, Y.3    Berjeaud, J.M.4
  • 20
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings, J. W., M. Sailer, K. Johnson, K. L. Roy, J. C. Vederas, and M. E. Stiles. 1991. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173:7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1    Sailer, M.2    Johnson, K.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 22
    • 0033764357 scopus 로고    scopus 로고
    • Engineering increased stability in the antimicrobial peptide pediocin PA-1
    • Johnsen, L., G. Fimland, V. Eijsink, and J. Nissen-Meyer. 2000. Engineering increased stability in the antimicrobial peptide pediocin PA-1. Appl. Environ. Microbiol. 66:4798-4802.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4798-4802
    • Johnsen, L.1    Fimland, G.2    Eijsink, V.3    Nissen-Meyer, J.4
  • 23
    • 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
  • 24
    • 0030721749 scopus 로고    scopus 로고
    • Controlled gene expression systems for lactic acid bacteria: Transferable nisin-inducible expression cassettes for Lactococcus, Leuconostoc, and Lactobacillus spp
    • Kleerebezem, M., M. M. Beerthuyzen, E. E. Vaughan, W. M. de Vos, and O. P. Kuipers. 1997. Controlled gene expression systems for lactic acid bacteria: transferable nisin-inducible expression cassettes for Lactococcus, Leuconostoc, and Lactobacillus spp. 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
  • 25
    • 0025941179 scopus 로고
    • Interactions of an antimicrobial peptide, tachyplesin I, with lipid membranes
    • Matsuzaki, K., M. Fukui, N. Fujii, and K. Miyajima. 1991. Interactions of an antimicrobial peptide, tachyplesin I, with lipid membranes. Biochim. Biophys. Acta 1070:259-264.
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 259-264
    • Matsuzaki, K.1    Fukui, M.2    Fujii, N.3    Miyajima, K.4
  • 26
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki, K., K. Sugishita, M. Harada, N. Fujii, and K. Miyajima. 1997. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327:119-130.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 27
    • 0031985197 scopus 로고    scopus 로고
    • Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon
    • Erratum, 64:1587
    • Miller, K. W., R. Schamber, Y. Chen, and B. Ray. 1998. Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon. Appl Environ Microbiol. 64:14-20. (Erratum, 64:1587.)
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 14-20
    • Miller, K.W.1    Schamber, R.2    Chen, Y.3    Ray, B.4
  • 28
    • 0031745937 scopus 로고    scopus 로고
    • Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity
    • Miller, K. W., R. Sehamber, 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    Sehamber, R.2    Osmanagaoglu, O.3    Ray, B.4
  • 29
    • 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
  • 30
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto Lozano, J. C., J. Nissen-Meyer, K. Sletten, C. Pelaz, and I. F. Nes. 1992. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 138:1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Nieto Lozano, J.C.1    Nissen-Meyer, J.2    Sletten, K.3    Pelaz, C.4    Nes, I.F.5
  • 31
    • 0026514561 scopus 로고
    • High-level temperature-induced synthesis of an antibody VH-domain in Escherichia coli using the PelB secretion signal
    • Power, B. E., N. Ivancic, V. R. Harley, R. G. Webster, A. A. Kortt, R. A. Irving, and P. J. Hudson. 1992, High-level temperature-induced synthesis of an antibody VH-domain in Escherichia coli using the PelB secretion signal. Gene 113:95-99.
    • (1992) Gene , vol.113 , pp. 95-99
    • Power, B.E.1    Ivancic, N.2    Harley, V.R.3    Webster, R.G.4    Kortt, A.A.5    Irving, R.A.6    Hudson, P.J.7
  • 32
    • 0028363167 scopus 로고
    • Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B
    • Quadri, L. E., M. Sailer, K. L. Roy, J. C. Vederas, and M. E. Stiles. 1994. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B. J. Biol. Chem. 269:12204-12211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12204-12211
    • Quadri, L.E.1    Sailer, M.2    Roy, K.L.3    Vederas, J.C.4    Stiles, M.E.5
  • 33
    • 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
  • 34
    • 0033930978 scopus 로고    scopus 로고
    • Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Ramnath, M., M. Beukes, K. Tamura, and J. W. Hastings. 2000. Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Appl. Environ. Microbiol. 66:3098-3101.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3098-3101
    • Ramnath, M.1    Beukes, M.2    Tamura, K.3    Hastings, J.W.4
  • 35
    • 0036154401 scopus 로고    scopus 로고
    • Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium
    • Uteng, M., H. H. Hauge, I. Brondz, J. Nissen-Meyer, and G. Fimland. 2002. Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium. Appl. Environ. Microbiol. 68:952-956.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 952-956
    • Uteng, M.1    Hauge, H.H.2    Brondz, I.3    Nissen-Meyer, J.4    Fimland, G.5
  • 36
    • 0031014418 scopus 로고    scopus 로고
    • Rapid and efficient purification method for small, hydrophobic, cationic bacteriocins: Purification of lactococcin B and pediocin PA-1
    • Venema, K., M. L. Chikindas, J. F. M. L. Seegers, A. J. Haandrikman, K. J. Leenhouts, G. Venema, and J. Kok. 1997. Rapid and efficient purification method for small, hydrophobic, cationic bacteriocins: purification of lactococcin B and pediocin PA-1. Appl. Environ. Microbiol. 63:305-309.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 305-309
    • Venema, K.1    Chikindas, M.L.2    Seegers, J.F.M.L.3    Haandrikman, A.J.4    Leenhouts, K.J.5    Venema, G.6    Kok, J.7
  • 37
    • 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
  • 38
    • 0034736095 scopus 로고    scopus 로고
    • Analogues of bacteriocins: Antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2 and truncated derivatives
    • Yan, L. Z., A. C. Gibbs, M. E. Stiles, D. S. Wishart, and J. C. Vederas. 2000. Analogues of bacteriocins: antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2 and truncated derivatives. J. Med. Chem. 43:4579-4581.
    • (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
  • 39
    • 0032925428 scopus 로고    scopus 로고
    • Purification, amino acid sequence and mode of action of bifidocin B produced by Bifidobacterium bifidum NCFB 1454
    • Yildirim, Z., D. K. Winters, and M. G. Johnson. 1999. Purification, amino acid sequence and mode of action of bifidocin B produced by Bifidobacterium bifidum NCFB 1454. J. Appl. Microbiol. 86:45-54.
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 45-54
    • Yildirim, Z.1    Winters, D.K.2    Johnson, M.G.3


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