메뉴 건너뛰기




Volumn 70, Issue 12, 2007, Pages 2792-2798

Chimeras of mature pediocin PA-1 fused to the signal peptide of enterocin P permits the cloning, production, and expression of pediocin PA-1 in Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROCOCCUS FAECIUM; LACTOCOCCUS LACTIS; PEDIOCOCCUS ACIDILACTICI;

EID: 37349111013     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X-70.12.2792     Document Type: Article
Times cited : (18)

References (39)
  • 1
    • 32944455291 scopus 로고    scopus 로고
    • Production of pediocin PA-1 in the methylotrophic yeast Pichia pastoris reveals unexpected inhibition of its biological activity due to the presence of collagen-like material
    • Beaulieu, L., D. Groleau, C. B. Míguez, J. F. Jette, H. Aomari, and M. Subirade. 2005. Production of pediocin PA-1 in the methylotrophic yeast Pichia pastoris reveals unexpected inhibition of its biological activity due to the presence of collagen-like material. Prot. Expr. Purif. 43:111-125.
    • (2005) Prot. Expr. Purif , vol.43 , pp. 111-125
    • Beaulieu, L.1    Groleau, D.2    Míguez, C.B.3    Jette, J.F.4    Aomari, H.5    Subirade, M.6
  • 2
    • 0021209585 scopus 로고
    • Two plasmid-determined restriction and modification systems in Streptococcus lactis
    • Chopin, M. C., A. Chopin, A. Moillo-Bott, and P. Langella. 1984. Two plasmid-determined restriction and modification systems in Streptococcus lactis. Plasmid 11:260-263.
    • (1984) Plasmid , vol.11 , pp. 260-263
    • Chopin, M.C.1    Chopin, A.2    Moillo-Bott, A.3    Langella, P.4
  • 4
    • 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. E 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.E.5
  • 5
    • 0034462540 scopus 로고    scopus 로고
    • Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q
    • Cintas, L. M., P. Casaus, C. Herranz, L. S. Håvarstein, H. Holo, P E. Hernández, and I. F. Nes. 2000. Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q. J. Bacteriol. 182: 6806-6814.
    • (2000) J. Bacteriol , vol.182 , pp. 6806-6814
    • Cintas, L.M.1    Casaus, P.2    Herranz, C.3    Håvarstein, L.S.4    Holo, H.5    Hernández, P.E.6    Nes, I.F.7
  • 7
    • 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. Nature Rev. Microbiol. 3:777-788.
    • (2005) Nature Rev. Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 8
    • 0036418802 scopus 로고    scopus 로고
    • Production of class II bacteriocins by lactic acid bacteria: An example of biological warfare and communication
    • Eijsink, V. G. H., L. Axelsson, D. B. Diep, L. S. Håvarstein, H. Holo, and I. F. Nes. 2002. Production of class II bacteriocins by lactic acid bacteria: an example of biological warfare and communication. Antonie Leeuwenhoek 81:639-654.
    • (2002) Antonie Leeuwenhoek , vol.81 , pp. 639-654
    • Eijsink, V.G.H.1    Axelsson, L.2    Diep, D.B.3    Håvarstein, L.S.4    Holo, H.5    Nes, I.F.6
  • 10
    • 28044472548 scopus 로고    scopus 로고
    • Pediocin-like antimicrobial peptides (class II bacteriocins) and their immunity proteins: Biosynthesis, structure and mode of action
    • Fimland, G., L. Johnsen, B. Dalhus, and J. Nissen-Meyer. 2005. Pediocin-like antimicrobial peptides (class II bacteriocins) and their immunity proteins: biosynthesis, structure and mode of action. J. Pept. Sci. 11:688-696.
    • (2005) J. Pept. Sci , vol.11 , pp. 688-696
    • Fimland, G.1    Johnsen, L.2    Dalhus, B.3    Nissen-Meyer, J.4
  • 11
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic Streptococci after protoplast-induced curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic Streptococci after protoplast-induced curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 12
  • 14
    • 21444446658 scopus 로고    scopus 로고
    • Gutiérrez, J., R. Criado, M. Martín, C. Herranz, L. M. Cintas, and P. E. Hernández. 2005. Production of enterocin P, an antilisterial pediocin-like bacteriocin from Enterococcus faecium P13, in Pichia pastoris. Antimicrob. Agents Chemother. 49:3004-3008.
    • Gutiérrez, J., R. Criado, M. Martín, C. Herranz, L. M. Cintas, and P. E. Hernández. 2005. Production of enterocin P, an antilisterial pediocin-like bacteriocin from Enterococcus faecium P13, in Pichia pastoris. Antimicrob. Agents Chemother. 49:3004-3008.
  • 15
    • 33747087571 scopus 로고    scopus 로고
    • High-level heterologous production and functional expression of the sec-dependent enterocin P from Enterococcus faecium P13 in Lactococcus lactis
    • Gutiérrez, J., R. Larsen, L. M. Cintas, J. Kok, and P. E. Hernández. 2006. High-level heterologous production and functional expression of the sec-dependent enterocin P from Enterococcus faecium P13 in Lactococcus lactis. Appl. Microbiol. Biotechnol. 72:41-51.
    • (2006) Appl. Microbiol. Biotechnol , vol.72 , pp. 41-51
    • Gutiérrez, J.1    Larsen, R.2    Cintas, L.M.3    Kok, J.4    Hernández, P.E.5
  • 16
    • 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 I. 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, I.F.3
  • 17
    • 17444395256 scopus 로고    scopus 로고
    • Sec-mediated secretion of enterocin P by Lactococcus lactis
    • Herranz, C., and A. J. M. Driessen. 2005. Sec-mediated secretion of enterocin P by Lactococcus lactis. Appl. Environ. Microbiol. 71: 1959-1963.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 1959-1963
    • Herranz, C.1    Driessen, A.J.M.2
  • 18
    • 0024345189 scopus 로고
    • High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media
    • Holo, H., and I. F. Nes. 1989. High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media. Appl. Environ. Microbiol. 55:3119-3123.
    • (1989) Appl. Environ. Microbiol , vol.55 , pp. 3119-3123
    • Holo, H.1    Nes, I.F.2
  • 19
    • 4143082901 scopus 로고    scopus 로고
    • Nisin-controlled production of pediocin PA-1 and colicin V in nisin- and non-nisin-producing Lactococcus lactis strains
    • Horn, N., A. Fernández, H. M. Dodd, M. J. Gasson, and J. M. Rodríguez. 2004. Nisin-controlled production of pediocin PA-1 and colicin V in nisin- and non-nisin-producing Lactococcus lactis strains. Appl. Environ. Microbiol. 70:5030-5032.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 5030-5032
    • Horn, N.1    Fernández, A.2    Dodd, H.M.3    Gasson, M.J.4    Rodríguez, J.M.5
  • 22
    • 14844326665 scopus 로고    scopus 로고
    • A versatile system for the expression of nonmodified bacteriocins in Escherichia coli
    • Ingham, A. B., K. W. Sproat, M. L. V. Tizard, and R. J. Moore. 2005. A versatile system for the expression of nonmodified bacteriocins in Escherichia coli. J. Appl. Microbiol. 98:676-683.
    • (2005) J. Appl. Microbiol , vol.98 , pp. 676-683
    • Ingham, A.B.1    Sproat, K.W.2    Tizard, M.L.V.3    Moore, R.J.4
  • 23
    • 0042029595 scopus 로고    scopus 로고
    • Differences in susceptibility of L. monocytogenes strains to sakacin P, sakacin A, pediocin PA-1, and nisin
    • Katla, T., K. Naterstad, M. Vancanneyt, J. Swings, and L. Axelsson. 2003. Differences in susceptibility of L. monocytogenes strains to sakacin P, sakacin A, pediocin PA-1, and nisin. Appl. Environ. Microbiol. 69:4431-4437.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 4431-4437
    • Katla, T.1    Naterstad, K.2    Vancanneyt, M.3    Swings, J.4    Axelsson, L.5
  • 25
    • 0035464768 scopus 로고    scopus 로고
    • Signal peptide and propeptide optimization for heterologous protein secretion in Lactococcus lactis
    • Le Loir, Y., S. Nouialle, J. Commissaire, L. Bretign, A. Gruss, and P. Langella. 2001. Signal peptide and propeptide optimization for heterologous protein secretion in Lactococcus lactis. Appl. Environ. Microbiol. 67:4119-4127.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 4119-4127
    • Le Loir, Y.1    Nouialle, S.2    Commissaire, J.3    Bretign, L.4    Gruss, A.5    Langella, P.6
  • 26
    • 33644883328 scopus 로고    scopus 로고
    • Genes encoding bacteriocins and their expression, and potential virulence factors of enterococci isolated from wood pigeons (Columba palumbus)
    • Martín, M., J. Gutiérrez, R. Criado, C. Herranz, L. M. Cintas, and P. E. Hernández. 2006. Genes encoding bacteriocins and their expression, and potential virulence factors of enterococci isolated from wood pigeons (Columba palumbus). J. Food Prot. 69:520-531.
    • (2006) J. Food Prot , vol.69 , pp. 520-531
    • Martín, M.1    Gutiérrez, J.2    Criado, R.3    Herranz, C.4    Cintas, L.M.5    Hernández, P.E.6
  • 27
    • 0033856851 scopus 로고    scopus 로고
    • Heterologous co-production of enterocin A and pediocin PA-1 by Lactococcus lactis: Detection by specific peptide-directed antibodies
    • Martínez, J. M., J. Kok, J. W. Sanders, and P. E. Hernández. 2000. Heterologous co-production of enterocin A and pediocin PA-1 by Lactococcus lactis: detection by specific peptide-directed antibodies. Appl. Environ. Microbiol. 66:3543-3549.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 3543-3549
    • Martínez, J.M.1    Kok, J.2    Sanders, J.W.3    Hernández, P.E.4
  • 28
    • 0033668020 scopus 로고    scopus 로고
    • Use of genetic and immunological probes for pediocin PA-1 detection and quantification of bacteriocin production in Pediococcus acidilactici strains of meat origin
    • Martínez, J. M., M. I. Martínez, C. Herranz, A. M. Suárez, L. M. Cintas, M. F. Fernández, J. M. Rodríguez, and P. E. Hernández. 2000. Use of genetic and immunological probes for pediocin PA-1 detection and quantification of bacteriocin production in Pediococcus acidilactici strains of meat origin. Food Agric. Immunol. 12:299-310.
    • (2000) Food Agric. Immunol , vol.12 , pp. 299-310
    • Martínez, J.M.1    Martínez, M.I.2    Herranz, C.3    Suárez, A.M.4    Cintas, L.M.5    Fernández, M.F.6    Rodríguez, J.M.7    Hernández, P.E.8
  • 31
    • 0029802390 scopus 로고    scopus 로고
    • Expression of the antimicrobial peptide carnobacteriocin B2 by a signal-peptide dependent general secretory pathway
    • McCormick, J. K., R. W. Worobo, and M. E. Stiles. 1996. Expression of the antimicrobial peptide carnobacteriocin B2 by a signal-peptide dependent general secretory pathway. Appl. Environ. Microbiol. 62: 4095-4099.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 4095-4099
    • McCormick, J.K.1    Worobo, R.W.2    Stiles, M.E.3
  • 32
    • 25144487810 scopus 로고    scopus 로고
    • Secretion of recombinant pediocin PA-1 by Bifidobacterium longum, using the signal sequence for bifidobacterial α-amylase
    • Moon, G. S., Y. R. Pyun, M. S. Park, G. E. Ji, and W. J. Kim. 2005. Secretion of recombinant pediocin PA-1 by Bifidobacterium longum, using the signal sequence for bifidobacterial α-amylase. Appl. Environ. Microbiol. 71:5630-5632.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 5630-5632
    • Moon, G.S.1    Pyun, Y.R.2    Park, M.S.3    Ji, G.E.4    Kim, W.J.5
  • 33
    • 85036993709 scopus 로고    scopus 로고
    • Moreira, W. L. 1994. Aislamiento y caracterización parcial de una bacteriocina producida por Pediococcus sp. 347, de origen cárnico. Ph.D. thesis. Universidad Complutense de Madrid, Madrid.
    • Moreira, W. L. 1994. Aislamiento y caracterización parcial de una bacteriocina producida por Pediococcus sp. 347, de origen cárnico. Ph.D. thesis. Universidad Complutense de Madrid, Madrid.
  • 36
    • 0033564202 scopus 로고    scopus 로고
    • The development of bactericidal yeast strains expressing the Pediococcus acidilactici pediocin gene (pedA) in Saccharomyces cerevisae
    • Schoeman, H., M. A. Vivier, M. du Toit, L. M. T. Dicks, and I. S. Pretorius. 1999. The development of bactericidal yeast strains expressing the Pediococcus acidilactici pediocin gene (pedA) in Saccharomyces cerevisae. Yeast 15:647-656.
    • (1999) Yeast , vol.15 , pp. 647-656
    • Schoeman, H.1    Vivier, M.A.2    du Toit, M.3    Dicks, L.M.T.4    Pretorius, I.S.5
  • 37
    • 0036284765 scopus 로고    scopus 로고
    • Lactococcus lactis DPC5598, a plasmid-free derivative of a commercial starter, provides a valuable alternative host for culture improvement studies
    • Trotter, M., R. P. Ross, G. F. Fitzgerald, and A. Coffey. 2002. Lactococcus lactis DPC5598, a plasmid-free derivative of a commercial starter, provides a valuable alternative host for culture improvement studies. J. Appl. Microbiol. 93:134-143.
    • (2002) J. Appl. Microbiol , vol.93 , pp. 134-143
    • Trotter, M.1    Ross, R.P.2    Fitzgerald, G.F.3    Coffey, A.4
  • 38
    • 0024493090 scopus 로고
    • Construction of a lactococcal expression vector: Expression of hen egg white lysozyme in Lactococcus lactis subsp. lactis
    • Van de Guchte, M., J. M. B. M. van der Vossen, J. Kok, and G. Venema. 1989. Construction of a lactococcal expression vector: expression of hen egg white lysozyme in Lactococcus lactis subsp. lactis. Appl. Environ. Microbiol. 55:224-228.
    • (1989) Appl. Environ. Microbiol , vol.55 , pp. 224-228
    • Van de Guchte, M.1    van der Vossen, J.M.B.M.2    Kok, J.3    Venema, G.4
  • 39
    • 0029074843 scopus 로고
    • Functional analysis of the pediocin Operon of Pediococcus acidilactici PAC1.0: PedB is the immunity protein and PedD is the precursor processing enzyme
    • Venema, K., J. Kok, J. D. Marugg, M. Y. Toonen, A. M. Ledeboer, G. Venema, and M. L. Chikindas. 1995. Functional analysis of the pediocin Operon of Pediococcus acidilactici PAC1.0: PedB is the immunity protein and PedD is the precursor processing enzyme. Mol. Microbiol. 17:515-522.
    • (1995) Mol. Microbiol , vol.17 , pp. 515-522
    • Venema, K.1    Kok, J.2    Marugg, J.D.3    Toonen, M.Y.4    Ledeboer, A.M.5    Venema, G.6    Chikindas, M.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.