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Volumn 13, Issue 12, 2012, Pages 16668-16707

Class IIa bacteriocins: Diversity and new developments

Author keywords

Class IIa bacteriocin; Discovery; Diversity; Genetic organization; Lactic acid bacteria

Indexed keywords

ACIDOCIN A; AVICIN A; BACTERIOCIN; BACTERIOCIN 2A; BAVARICIN A; BIFIDOCIN B; CURVACIN A; CURVATICIN L442; DURACIN GL; ENTEROCIN A; ENTEROCIN HF; ENTEROCIN P; LEUCOCIN A; LEUCOCIN B; LEUCOCIN C; LISTERIOCIN 743A; MUNDTICIN; MUNDTICIN L; PEDIOCIN; PENOCIN A; PISCICOCIN CS526; PISCICOLIN 126; PLANTARICIN 423; PLANTARICIN C19; SAKACIN G; SAKACIN P; SAKACIN X; UBERICIN A; UNCLASSIFIED DRUG; WEISSELLIN A; ANTIINFECTIVE AGENT; FOOD PRESERVATIVE;

EID: 84871694756     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms131216668     Document Type: Review
Times cited : (93)

References (217)
  • 1
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic bacteria
    • Klaenhammer, T.R. Genetics of bacteriocins produced by lactic bacteria. FEMS Microbiol. Rev. 1993, 12, 39-86.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-86
    • Klaenhammer, T.R.1
  • 3
    • 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.; Oppegård, 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    Oppegård, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 4
    • 0032788906 scopus 로고    scopus 로고
    • Class IIa bacteriocins from lactic acid bacteria: Antibacterial activity and food preservation
    • Ennahar, S.; Sonomoto, K.; Ishizaki, A. Class IIa bacteriocins from lactic acid bacteria: Antibacterial activity and food preservation. J. Biosci. Bioeng. 1999, 87, 705-716.
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 705-716
    • Ennahar, S.1    Sonomoto, K.2    Ishizaki, A.3
  • 6
    • 77955927487 scopus 로고    scopus 로고
    • Food biopreservation: Promising strategies using bacteriocins, bacteriophages and endolysins
    • García, P.; Rodríguez, L.; Rodríguez, A.; Martínez, B. Food biopreservation: Promising strategies using bacteriocins, bacteriophages and endolysins. Trends Food Sci. Technol. 2010, 21, 373-382.
    • (2010) Trends Food Sci. Technol. , vol.21 , pp. 373-382
    • García, P.1    Rodríguez, L.2    Rodríguez, A.3    Martínez, B.4
  • 7
    • 80052212888 scopus 로고    scopus 로고
    • New developments and applications of bacteriocins and peptides in foods
    • Mills, S.; Stanton, C.; Hill, C.; Ross, R.P. New developments and applications of bacteriocins and peptides in foods. Annu. Rev. Food Sci. Technol. 2011, 2, 299-329.
    • (2011) Annu. Rev. Food Sci. Technol. , vol.2 , pp. 299-329
    • Mills, S.1    Stanton, C.2    Hill, C.3    Ross, R.P.4
  • 9
    • 79953737558 scopus 로고    scopus 로고
    • Production, purification, sequencing and activity spectra of mutacins D-123.1 and F-59.1
    • Nicolas, G.G.; LaPointe, G.; Lavoie, M.C. Production, purification, sequencing and activity spectra of mutacins D-123.1 and F-59.1. BMC Microbiol. 2011, 11, 69.
    • (2011) BMC Microbiol. , vol.11 , pp. 69
    • Nicolas, G.G.1    LaPointe, G.2    Lavoie, M.C.3
  • 10
    • 0031881842 scopus 로고    scopus 로고
    • Characterization and antimicrobial spectrum of bifidocin B, a bacteriocin produced by Bifidobacterium bifidum NCFB 1454
    • Yildirim, Z.; Johnson, M.G. Characterization and antimicrobial spectrum of bifidocin B, a bacteriocin produced by Bifidobacterium bifidum NCFB 1454. J. Food Prot. 1998, 61, 47-51.
    • (1998) J. Food Prot. , vol.61 , pp. 47-51
    • Yildirim, Z.1    Johnson, M.G.2
  • 11
    • 0032925428 scopus 로고    scopus 로고
    • Purification, amino acid sequence and mode of action of bifidocin B produced by Bifidobacterium bifidum NCFB 1454
    • Yildirim, Z.; Winters, D.K.; Johnson, M.G. Purification, amino acid sequence and mode of action of bifidocin B produced by Bifidobacterium bifidum NCFB 1454. J. Appl. Microbiol. 1999, 86, 45-54.
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 45-54
    • Yildirim, Z.1    Winters, D.K.2    Johnson, M.G.3
  • 12
    • 73549095170 scopus 로고    scopus 로고
    • Bifidin I-A new bacteriocin produced by Bifidobacterium infantis BCRC 14602: Purification and partial amino acid sequence
    • Cheikhyoussef, A.; Cheikhyoussef, N.; Chen, H.Q.; Zhao, J.X.; Tang, J.; Zhang, H. Bifidin I-A new bacteriocin produced by Bifidobacterium infantis BCRC 14602: Purification and partial amino acid sequence. Food Control. 2010, 21, 746-753.
    • (2010) Food Control. , vol.21 , pp. 746-753
    • Cheikhyoussef, A.1    Cheikhyoussef, N.2    Chen, H.Q.3    Zhao, J.X.4    Tang, J.5    Zhang, H.6
  • 13
    • 0034467777 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of coagulin, a new antilisterial bacteriocin in the pediocin family of bacteriocins, produced by Bacillus coagulans I4
    • Le Marrec, C.; Hyronimus, B.; Bressollier, P.; Verneuil, B.; Urdaci, M.C. Biochemical and genetic characterization of coagulin, a new antilisterial bacteriocin in the pediocin family of bacteriocins, produced by Bacillus coagulans I4. Appl. Environ. Microbiol. 2000, 66, 5213-5220.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 5213-5220
    • Le Marrec, C.1    Hyronimus, B.2    Bressollier, P.3    Verneuil, B.4    Urdaci, M.C.5
  • 14
    • 0035461360 scopus 로고    scopus 로고
    • Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743
    • Kalmokoff, M.L.; Banerjee, S.K.; Cyr, T.; Hefford, M.A.; Gleeson, T. Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743. Appl. Environ. Microbiol. 2001, 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
  • 15
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Håvarstein, L.S.; Diep, D.B.; Nes, I.F. A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export. Mol. Microbiol. 1995, 16, 229-240.
    • (1995) Mol. Microbiol. , vol.16 , pp. 229-240
    • Håvarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 16
    • 77956265577 scopus 로고    scopus 로고
    • A new structure-based classification of Gram-positive bacteriocins
    • Zouhir, A.; Hammami, R.; Fliss, I.; Hamida, J.B. A new structure-based classification of Gram-positive bacteriocins. Protein J. 2010, 29, 432-439.
    • (2010) Protein J. , vol.29 , pp. 432-439
    • Zouhir, A.1    Hammami, R.2    Fliss, I.3    Hamida, J.B.4
  • 17
    • 79960087668 scopus 로고    scopus 로고
    • Classification of Bacteriocins from Gram-Positive Bacteria
    • In, Drider, D., Rebuffat, S., Eds.; Springer Publishing Inc: New York, NY, USA
    • Rea, M.C.; Ross, R.P.; Cotter, P.D.; Hill, C. Classification of Bacteriocins from Gram-Positive Bacteria. In Prokaryotic Antimicrobial Peptides: From Genes to Applications; Drider, D., Rebuffat, S., Eds.; Springer Publishing Inc: New York, NY, USA, 2011; pp. 29-53.
    • (2011) Prokaryotic Antimicrobial Peptides: From Genes to Applications , pp. 29-53
    • Rea, M.C.1    Ross, R.P.2    Cotter, P.D.3    Hill, C.4
  • 18
    • 0036216314 scopus 로고    scopus 로고
    • Ribosomally synthesized antibacterial peptides in Gram positive bacteria
    • Diep, D.B.; Nes, I.F. Ribosomally synthesized antibacterial peptides in Gram positive bacteria. Curr. Drug Targets 2002, 3, 107-122.
    • (2002) Curr. Drug Targets , vol.3 , pp. 107-122
    • Diep, D.B.1    Nes, I.F.2
  • 19
    • 84858004398 scopus 로고    scopus 로고
    • Class IIa Bacteriocins: Current Knowledge and Perspectives
    • In, Drider, D., Rebuffat, S., Eds.; Springer Publishing, Inc.: New York, NY, USA
    • Belguesmia, Y.; Naghmouchi, K.; Chihib, N.-E.; Drider, D. Class IIa Bacteriocins: Current Knowledge and Perspectives. In Prokaryotic Antimicrobial Peptides: From Genes to Applications; Drider, D., Rebuffat, S., Eds.; Springer Publishing, Inc.: New York, NY, USA, 2011; pp. 171-195.
    • (2011) Prokaryotic Antimicrobial Peptides: From Genes to Applications , pp. 171-195
    • Belguesmia, Y.1    Naghmouchi, K.2    Chihib, N.-E.3    Drider, D.4
  • 20
    • 28044472548 scopus 로고    scopus 로고
    • Pediocinlike antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure and mode of action
    • Fimland, G.; Johnsen, L.; Dalhus, B.; Nissen-Meyer, J. Pediocinlike antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure and mode of action. J. Pept. Sci. 2005, 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
  • 21
    • 75249089137 scopus 로고    scopus 로고
    • Molecular and genetic characterization of a novel bacteriocin locus in Enterococcus avium isolates from infants
    • Birri, D.J.; Brede, D.A.; Forberg, T.; Holo, H.; Nes, I.F. Molecular and genetic characterization of a novel bacteriocin locus in Enterococcus avium isolates from infants. Appl. Environ. Microbiol. 2010, 76, 483-492.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 483-492
    • Birri, D.J.1    Brede, D.A.2    Forberg, T.3    Holo, H.4    Nes, I.F.5
  • 22
    • 0027247835 scopus 로고
    • Antimicrobial activity of lactic acid bacteria isolated from sour doughs: Purification and characterization of bavaricin A, a bacteriocin produced by Lactobacillus bavaricus MI401
    • Larsen, A.G.; Vogensen, F.K.; Josephsen, J. Antimicrobial activity of lactic acid bacteria isolated from sour doughs: Purification and characterization of bavaricin A, a bacteriocin produced by Lactobacillus bavaricus MI401. J. Appl. Microbiol. 1993, 75, 113-122.
    • (1993) J. Appl. Microbiol. , vol.75 , pp. 113-122
    • Larsen, A.G.1    Vogensen, F.K.2    Josephsen, J.3
  • 24
    • 3042675440 scopus 로고    scopus 로고
    • Enhancement of the enterocin CRL35 activity by a synthetic peptide derived from the NH2-terminal sequence
    • Saavedra, L.; Minahk, C.; de Ruiz Holgado, A.P.; Sesma, F. Enhancement of the enterocin CRL35 activity by a synthetic peptide derived from the NH2-terminal sequence. Antimicrob. Agents Chemother. 2004, 48, 2778-2781.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 2778-2781
    • Saavedra, L.1    Minahk, C.2    de Ruiz Holgado, A.P.3    Sesma, F.4
  • 25
    • 79955574621 scopus 로고    scopus 로고
    • Purification, amino acid sequence and characterization of the class IIa bacteriocin weissellin A, produced by Weissella paramesenteroides DX
    • Papagianni, M.; Papamichae, E.M. Purification, amino acid sequence and characterization of the class IIa bacteriocin weissellin A, produced by Weissella paramesenteroides DX. Bioresour. Technol. 2011, 102, 6730-6734.
    • (2011) Bioresour. Technol. , vol.102 , pp. 6730-6734
    • Papagianni, M.1    Papamichae, E.M.2
  • 27
    • 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
    • Kaiser, A.L.; Montville, T.J. Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles. J. Appl. Microbiol. 1996, 62, 4529-4535.
    • (1996) J. Appl. Microbiol. , vol.62 , pp. 4529-4535
    • Kaiser, A.L.1    Montville, T.J.2
  • 29
    • 0028921701 scopus 로고
    • Isolation and characterization of acidocin A and cloning of the bacteriocin gene from Lactobacillus acidophilus
    • Kanatani, K.; Oshimura, M.; Sano, K. Isolation and characterization of acidocin A and cloning of the bacteriocin gene from Lactobacillus acidophilus. Appl. Environ. Microbiol. 1995, 61, 1061-1067.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1061-1067
    • Kanatani, K.1    Oshimura, M.2    Sano, K.3
  • 32
    • 69449104828 scopus 로고    scopus 로고
    • Characterization of mundticin L, a class IIa anti-Listeria bacteriocin from Enterococcus mundtii CUGF08
    • Feng, G.; Guron, G.K.; Churey, J.J.; Worobo, R.W. Characterization of mundticin L, a class IIa anti-Listeria bacteriocin from Enterococcus mundtii CUGF08. Appl. Environ. Microbiol. 2009, 75, 5708-5713.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5708-5713
    • Feng, G.1    Guron, G.K.2    Churey, J.J.3    Worobo, R.W.4
  • 33
    • 0028015625 scopus 로고
    • Characterization of leucocin B-Ta11a, a bacteriocin from Leuconostoc carnosum Ta11a isolated from meat
    • Felix, J.V.; Papathanasopoulos, M.A.; Smith, A.A.; von Holy, A.; Hastings, J.W. Characterization of leucocin B-Ta11a, a bacteriocin from Leuconostoc carnosum Ta11a isolated from meat. Curr. Microbiol. 1994, 29, 207-212.
    • (1994) Curr. Microbiol. , vol.29 , pp. 207-212
    • Felix, J.V.1    Papathanasopoulos, M.A.2    Smith, A.A.3    von Holy, A.4    Hastings, J.W.5
  • 34
    • 41549134454 scopus 로고    scopus 로고
    • A "retrocidal" plasmid in Enterococcus faecalis, passage and protection
    • Flannagan, S.E.; Clewell, D.B.; Sedgley, C.M. A "retrocidal" plasmid in Enterococcus faecalis, passage and protection. Plasmid 2008, 59, 217-230.
    • (2008) Plasmid , vol.59 , pp. 217-230
    • Flannagan, S.E.1    Clewell, D.B.2    Sedgley, C.M.3
  • 35
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • Arnold, K.; Bordoli, L.; Kopp, J.; Schwede, T. The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 2006, 22, 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 36
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T.; Kopp, J.; Guex, N.; Peitsch, M.C. SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res. 2003, 31, 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 37
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N.; Peitsch, M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 1997, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 38
    • 0026802510 scopus 로고
    • Characterization of the bacteriocins curvacin A from Lactobacillus curvatus LTH1174 and sakacin P from L sake LTH673
    • Tichaczek, P.S.; Nissen-Meyer, J.; Nes, I.F.; Vogel, R.F.; Hammes, W.P. Characterization of the bacteriocins curvacin A from Lactobacillus curvatus LTH1174 and sakacin P from L. sake LTH673. Syst. Appl. Microbiol. 1992, 15, 460-468.
    • (1992) Syst. Appl. Microbiol. , vol.15 , pp. 460-468
    • Tichaczek, P.S.1    Nissen-Meyer, J.2    Nes, I.F.3    Vogel, R.F.4    Hammes, W.P.5
  • 39
    • 34648830880 scopus 로고    scopus 로고
    • Sequencing and expression analysis of sakacin genes in Lactobacillus curvatus strains
    • Cocolin, L.; Rantsiou, K. Sequencing and expression analysis of sakacin genes in Lactobacillus curvatus strains. Appl. Environ. Microbiol. 2007, 76, 1403-1411.
    • (2007) Appl. Environ. Microbiol. , vol.76 , pp. 1403-1411
    • Cocolin, L.1    Rantsiou, K.2
  • 40
    • 0028344604 scopus 로고
    • Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH 673
    • Tichaczek, P.S.; Vogel, R.F.; Hammes, W.P. Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH 673. Microbiology 1994, 140, 361-367.
    • (1994) Microbiology , vol.140 , pp. 361-367
    • Tichaczek, P.S.1    Vogel, R.F.2    Hammes, W.P.3
  • 41
    • 33745938113 scopus 로고    scopus 로고
    • Sequencing and expression analysis of the sakacin P bacteriocin produced by a Lactobacillus sakei strain isolated from naturally fermented sausages
    • Urso, R.; Rantsiou, K.; Cantoni, C.; Comi, G.; Cocolin, L. Sequencing and expression analysis of the sakacin P bacteriocin produced by a Lactobacillus sakei strain isolated from naturally fermented sausages. Appl. Environ. Microbiology 2006, 71, 480-485.
    • (2006) Appl. Environ. Microbiology , vol.71 , pp. 480-485
    • Urso, R.1    Rantsiou, K.2    Cantoni, C.3    Comi, G.4    Cocolin, L.5
  • 42
    • 0000815399 scopus 로고
    • Plasmid-associated bacteriocin production and sucrose fermentation in Pediococcus acidilactici
    • Gonzalez, C.F.; Kunka, B.S. Plasmid-associated bacteriocin production and sucrose fermentation in Pediococcus acidilactici. Appl. Environ. Microbiol. 1987, 53, 2534-2538.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2534-2538
    • Gonzalez, C.F.1    Kunka, B.S.2
  • 43
    • 0023637662 scopus 로고
    • Direct detection of an antimicrobial peptide of Pediococcus acidilactici in SDS-PAGE
    • Bhunia, A.K.; Johnson, M.C.; Ray, B. Direct detection of an antimicrobial peptide of Pediococcus acidilactici in SDS-PAGE. J. Ind. Microbiol. 1987, 2, 319-322.
    • (1987) J. Ind. Microbiol. , vol.2 , pp. 319-322
    • Bhunia, A.K.1    Johnson, M.C.2    Ray, B.3
  • 44
    • 0026783465 scopus 로고
    • Nucleotide and amino acid sequence of pap-gene (pediocin AcH production) in Pediococcus acidilactici H
    • Motlagh, A.M.; Bhunia, A.K.; Szostek, F.; Hansen, T.R.; Johnson, M.C.; Ray, B. Nucleotide and amino acid sequence of pap-gene (pediocin AcH production) in Pediococcus acidilactici H. Lett. Appl. Microbiol. 1992, 15, 45-48.
    • (1992) Lett. Appl. Microbiol. , vol.15 , pp. 45-48
    • Motlagh, A.M.1    Bhunia, A.K.2    Szostek, F.3    Hansen, T.R.4    Johnson, M.C.5    Ray, B.6
  • 45
    • 0024553991 scopus 로고
    • Bacteriocin plasmids of Pediococcus acidilactici
    • Ray, S.K.; Johnson, M.C.; Ray, B. Bacteriocin plasmids of Pediococcus acidilactici. J. Ind. Microbiol. 1989, 4, 163-171.
    • (1989) J. Ind. Microbiol. , vol.4 , pp. 163-171
    • Ray, S.K.1    Johnson, M.C.2    Ray, B.3
  • 46
    • 0026603727 scopus 로고
    • Plasmid transfers by conjugation and electroporation in Pediococcus acidilactici
    • Kim, W.J.; Ray, B.; Johnson, M.C. Plasmid transfers by conjugation and electroporation in Pediococcus acidilactici. J. Appl. Bacteriol. 1992, 72, 201-207.
    • (1992) J. Appl. Bacteriol. , vol.72 , pp. 201-207
    • Kim, W.J.1    Ray, B.2    Johnson, M.C.3
  • 47
    • 0036210206 scopus 로고    scopus 로고
    • Bacteriocin produced by Pediococcus sp in kimchi and its characteristics
    • Kwon, D.Y.; Koo, M.; Ryoo, C.R.; Kang, C.H.; Min, K.H.; Kim, W.J. Bacteriocin produced by Pediococcus sp. in kimchi and its characteristics. J. Microbiol. Biot. 2002, 12, 96-105.
    • (2002) J. Microbiol. Biot. , vol.12 , pp. 96-105
    • Kwon, D.Y.1    Koo, M.2    Ryoo, C.R.3    Kang, C.H.4    Min, K.H.5    Kim, W.J.6
  • 48
    • 33947593420 scopus 로고    scopus 로고
    • Characterization of two bacteriocins produced by Pediococcus acidilactici isolated from "Alheira", a fermented sausage traditionally produced in Portugal
    • Albano, H.; Todorov, S.D.; van Reenen, C.A.; Hogg, T.; Dicks, L.M.T.; Teixeira, P. Characterization of two bacteriocins produced by Pediococcus acidilactici isolated from "Alheira", a fermented sausage traditionally produced in Portugal. Int. J. Food Microbiol. 2007, 116, 239-247.
    • (2007) Int. J. Food Microbiol. , vol.116 , pp. 239-247
    • Albano, H.1    Todorov, S.D.2    van Reenen, C.A.3    Hogg, T.4    Dicks, L.M.T.5    Teixeira, P.6
  • 49
    • 37249054494 scopus 로고    scopus 로고
    • Purification and identification of the pediocin produced by Pediococcus acidilactici MM33, a new human intestinal strain
    • Millette, M.; Dupont, C.; Shareck, F.; Ruiz, M.T.; Archambault, D.; Lacroix, M. Purification and identification of the pediocin produced by Pediococcus acidilactici MM33, a new human intestinal strain. J. Appl. Microbiol. 2008, 104, 269-275.
    • (2008) J. Appl. Microbiol. , vol.104 , pp. 269-275
    • Millette, M.1    Dupont, C.2    Shareck, F.3    Ruiz, M.T.4    Archambault, D.5    Lacroix, M.6
  • 50
    • 0030805155 scopus 로고    scopus 로고
    • Interactions of nisin and pediocin PA-1 with closely related lactic acid bacteria that manifest over 100-fold differences in bacteriocin sensitivity
    • Bennik, M.H.J.; Verheul, A.; Abee, T.; Naaktgeboren-Stoffels, G.; Gorris, L.G.M.; Smid, E.J. Interactions of nisin and pediocin PA-1 with closely related lactic acid bacteria that manifest over 100-fold differences in bacteriocin sensitivity. Appl. Environ. Microbiol. 1997, 63, 3628-3636.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3628-3636
    • Bennik, M.H.J.1    Verheul, A.2    Abee, T.3    Naaktgeboren-Stoffels, G.4    Gorris, L.G.M.5    Smid, E.J.6
  • 51
    • 69149088926 scopus 로고    scopus 로고
    • Pediocin A modulates intestinal microflora metabolism in swine in vitro intestinal fermentations
    • Casadei, G.; Grilli, E.; Piva, A. Pediocin A modulates intestinal microflora metabolism in swine in vitro intestinal fermentations. J. Anim. Sci. 2009, 87, 2020-2028.
    • (2009) J. Anim. Sci. , vol.87 , pp. 2020-2028
    • Casadei, G.1    Grilli, E.2    Piva, A.3
  • 53
    • 33645458822 scopus 로고    scopus 로고
    • Lactobacillus plantarum inhibits growth of Listeria monocytogenes in an in vitro continuous flow gut model, but promotes invasion of L monocytogenes in the gut of gnotobiotic rats
    • Bernbom, N.; Licht, T.R.; Saadbye, P.; Vogensen, F.K.; Norrung, B. Lactobacillus plantarum inhibits growth of Listeria monocytogenes in an in vitro continuous flow gut model, but promotes invasion of L. monocytogenes in the gut of gnotobiotic rats. Int. J. Food Microbiol. 2006, 108, 10-14.
    • (2006) Int. J. Food Microbiol. , vol.108 , pp. 10-14
    • Bernbom, N.1    Licht, T.R.2    Saadbye, P.3    Vogensen, F.K.4    Norrung, B.5
  • 54
    • 0003000418 scopus 로고
    • A bacteriocin produced by Pediococcus species associated with a 5.5 megadalton plasmid
    • Hoover, D.G.; Walsh, P.M.; Kolaetis, K.M.; Daly, M.M. A bacteriocin produced by Pediococcus species associated with a 5.5 megadalton plasmid. J. Food Prot. 1988, 59, 29-31.
    • (1988) J. Food Prot. , vol.59 , pp. 29-31
    • Hoover, D.G.1    Walsh, P.M.2    Kolaetis, K.M.3    Daly, M.M.4
  • 55
    • 0026673262 scopus 로고
    • Characterization of a bacteriocin from Pediococcus acidilactici PC and comparison of bacteriocin-producing strains using molecular typing procedures
    • Jager, K.; Harlander, S. Characterization of a bacteriocin from Pediococcus acidilactici PC and comparison of bacteriocin-producing strains using molecular typing procedures. Appl. Environ. Microbiol. 1992, 37, 631-637.
    • (1992) Appl. Environ. Microbiol. , vol.37 , pp. 631-637
    • Jager, K.1    Harlander, S.2
  • 56
    • 0026640460 scopus 로고
    • Mapping of pSMB74, a plasmid encoding bacteriocin AcH production (Pap+) trait in Pediococcus acidilactici H
    • Ray, B.; Motlagh, A.M.; Johnson, M.C.; Bozoglu, F. Mapping of pSMB74, a plasmid encoding bacteriocin AcH production (Pap+) trait in Pediococcus acidilactici H. Lett. Appl. Microbiol. 1992, 15, 35-37.
    • (1992) Lett. Appl. Microbiol. , vol.15 , pp. 35-37
    • Ray, B.1    Motlagh, A.M.2    Johnson, M.C.3    Bozoglu, F.4
  • 57
    • 0027398487 scopus 로고
    • Purification, partial characterization and plasmid linkage of pediocin SJ-1, a bacteriocin produced by Pediococcus acidilactici
    • Schved, F.; Lalazar, A.; Henis, Y.; Juven, B.J. Purification, partial characterization and plasmid linkage of pediocin SJ-1, a bacteriocin produced by Pediococcus acidilactici. J. Appl. Bacteriol. 1993, 74, 67-77.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 67-77
    • Schved, F.1    Lalazar, A.2    Henis, Y.3    Juven, B.J.4
  • 58
    • 0028235139 scopus 로고
    • Determination of bacteriocin-encoding plasmids of Pediococcus acidilactici strains by southern hybridization
    • Bhunia, A.K.; Bhowmik, T.K.; Johnson, M.G. Determination of bacteriocin-encoding plasmids of Pediococcus acidilactici strains by southern hybridization. Lett. Appl. Microbiol. 1994, 18, 168-170.
    • (1994) Lett. Appl. Microbiol. , vol.18 , pp. 168-170
    • Bhunia, A.K.1    Bhowmik, T.K.2    Johnson, M.G.3
  • 59
    • 18844469504 scopus 로고    scopus 로고
    • Detection of pediocin PA-1 producing pediococci by rapid molecular producing by rapid molecular biology techniques
    • Rodríguez, J.M.; Cintas, L.M.; Casaus, P.; Martínez, M.I.; Suárez, A.; Hernández, P.E. Detection of pediocin PA-1 producing pediococci by rapid molecular producing by rapid molecular biology techniques. Food Microbiol. 1997, 14, 363-371.
    • (1997) Food Microbiol. , vol.14 , pp. 363-371
    • Rodríguez, J.M.1    Cintas, L.M.2    Casaus, P.3    Martínez, M.I.4    Suárez, A.5    Hernández, P.E.6
  • 60
    • 84985058401 scopus 로고
    • Conjugal transfer of a plasmid encoding bacteriocin production and immunity in Pediococcus acidilactici H
    • Ray, S.K.; Kim, W.J.; Johnson, M.C.; Ray, B. Conjugal transfer of a plasmid encoding bacteriocin production and immunity in Pediococcus acidilactici H. J. Appl. Bacteriol. 1989, 66, 393-399.
    • (1989) J. Appl. Bacteriol. , vol.66 , pp. 393-399
    • Ray, S.K.1    Kim, W.J.2    Johnson, M.C.3    Ray, B.4
  • 61
    • 0036222084 scopus 로고    scopus 로고
    • Pediocin PA-1, a wide-spectrum bacteriocin from lactic acid bacteria
    • Rodríguez, J.M.; Martínez, M.I.; Kok, J. Pediocin PA-1, a wide-spectrum bacteriocin from lactic acid bacteria. Crit. Rev. Food Sci. Nutr. 2002, 42, 91-121.
    • (2002) Crit. Rev. Food Sci. Nutr. , vol.42 , pp. 91-121
    • Rodríguez, J.M.1    Martínez, M.I.2    Kok, J.3
  • 62
    • 12444300238 scopus 로고    scopus 로고
    • Gene organization and sequences of pediocin AcH/PA-1, production operons in Pediococcus and Lactococcus plasmids
    • Miller, K.W.; Ray, P.; Steinmetz, T.; Hanekamp, T.; Ray, B. Gene organization and sequences of pediocin AcH/PA-1, production operons in Pediococcus and Lactococcus plasmids. Lett. Appl. Microbiol. 2005, 40, 52-62.
    • (2005) Lett. Appl. Microbiol. , vol.40 , pp. 52-62
    • Miller, K.W.1    Ray, P.2    Steinmetz, T.3    Hanekamp, T.4    Ray, B.5
  • 63
    • 0031905297 scopus 로고    scopus 로고
    • Rolling-circle plasmids from B subtilis: Complete nucleotide sequences and analyses of genes of pTA1015, pTA1040, pTA1050 and pTA1060, and comparisons with related plasmids from Gram-positive bacteria
    • Meijer, W.J.J.; Wisman, G.B.A.; Terpstra, P.; Thorsted, P.B.; Thomas, C.M.; Holsappel, S.; Venema, G.; Bron, S. Rolling-circle plasmids from B. subtilis: Complete nucleotide sequences and analyses of genes of pTA1015, pTA1040, pTA1050 and pTA1060, and comparisons with related plasmids from Gram-positive bacteria. FEMS Microbiol. Rev. 1998, 21, 337-368.
    • (1998) FEMS Microbiol. Rev. , vol.21 , pp. 337-368
    • Meijer, W.J.J.1    Wisman, G.B.A.2    Terpstra, P.3    Thorsted, P.B.4    Thomas, C.M.5    Holsappel, S.6    Venema, G.7    Bron, S.8
  • 64
    • 77954936569 scopus 로고    scopus 로고
    • Molecular genetics, genomics and biochemistry of mutacins
    • Nicolas, G.G.; Lavoie, M.C.; Lapointe, G. Molecular genetics, genomics and biochemistry of mutacins. Genes Genomes Genomics 2007, 1, 193-208.
    • (2007) Genes Genomes Genomics , vol.1 , pp. 193-208
    • Nicolas, G.G.1    Lavoie, M.C.2    Lapointe, G.3
  • 65
    • 18444414327 scopus 로고    scopus 로고
    • Production of bacteriocin-like compounds by human faecal Bifidobacterium strains
    • Collado, M. C.; Hernández, M.; Sanz, Y. Production of bacteriocin-like compounds by human faecal Bifidobacterium strains. J. Food Prot. 2005, 68, 1034-1040.
    • (2005) J. Food Prot. , vol.68 , pp. 1034-1040
    • Collado, M.C.1    Hernández, M.2    Sanz, Y.3
  • 66
    • 61849180908 scopus 로고    scopus 로고
    • Pediocin PA-1 and a pediocin producing Lactobacillus plantarum strain do not change the HMA rat microbiota
    • Bernbom, N.; Jelle, B.; Brogren, C.H.; Vogensen, F.K.; Norrung, B.; Licht, T.R. Pediocin PA-1 and a pediocin producing Lactobacillus plantarum strain do not change the HMA rat microbiota. Int. J. Food Microbiol. 2009, 130, 251-257.
    • (2009) Int. J. Food Microbiol. , vol.130 , pp. 251-257
    • Bernbom, N.1    Jelle, B.2    Brogren, C.H.3    Vogensen, F.K.4    Norrung, B.5    Licht, T.R.6
  • 67
    • 0036377147 scopus 로고    scopus 로고
    • The complete aminoacid sequence of the pediocin-like antimicrobial peptide leucocin C
    • Fimland, G.; Sletten, K.; Nissen-Meyer, J. The complete aminoacid sequence of the pediocin-like antimicrobial peptide leucocin C. Biochem. Biophys. Res. Commun. 2002, 295, 826-827.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 826-827
    • Fimland, G.1    Sletten, K.2    Nissen-Meyer, J.3
  • 70
    • 34247098486 scopus 로고    scopus 로고
    • Amino acid and nucleotide sequence, adjacent genes, and heterologous expression of hiracin JM79, a sec-dependent bacteriocin produced by Enterococcus hirae DCH5, isolated from Mallard ducks (Anas platyrhynchos)
    • Sánchez, J.; Die, D. B.; Herranz, C.; Nes, I.F.; Cintas, L.M.; Hernandez, P.E. Amino acid and nucleotide sequence, adjacent genes, and heterologous expression of hiracin JM79, a sec-dependent bacteriocin produced by Enterococcus hirae DCH5, isolated from Mallard ducks (Anas platyrhynchos). FEMS Microbiol. Lett. 2007, 270, 227-236.
    • (2007) FEMS Microbiol. Lett. , vol.270 , pp. 227-236
    • Sánchez, J.1    Die, D.B.2    Herranz, C.3    Nes, I.F.4    Cintas, L.M.5    Hernandez, P.E.6
  • 71
    • 0036353079 scopus 로고    scopus 로고
    • Isolation of enterocin SE-K4-encoding plasmid and a high enterocin SE-K4 producing strain of Enterococcus faecalis K-4
    • Doi, K.; Eguchi, T.; Choi, S.-H.; Iwatake, A.; Ohmomo, S.; Ogata, S. Isolation of enterocin SE-K4-encoding plasmid and a high enterocin SE-K4 producing strain of Enterococcus faecalis K-4. J. Biosci. Bioeng. 2002, 93, 434-436.
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 434-436
    • Doi, K.1    Eguchi, T.2    Choi, S.-H.3    Iwatake, A.4    Ohmomo, S.5    Ogata, S.6
  • 72
    • 0030000298 scopus 로고    scopus 로고
    • Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI17
    • Tomita, H.; Fujimoto, S.; Tanimoto, K.; Ike, Y. Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone-responsive conjugative plasmid pYI17. J. Bacteriol. 1996, 178, 3585-3593.
    • (1996) J. Bacteriol. , vol.178 , pp. 3585-3593
    • Tomita, H.1    Fujimoto, S.2    Tanimoto, K.3    Ike, Y.4
  • 73
    • 0031876870 scopus 로고    scopus 로고
    • Isolation, purification and partial characterization of plantaricin 423, a bacteriocin produced by Lactobacillus plantarum
    • Van Reenen, C.A.; Dicks, L.M.T.; Chikindas, M.L. Isolation, purification and partial characterization of plantaricin 423, a bacteriocin produced by Lactobacillus plantarum. J. Appl. Microbiol. 1998, 84, 1131-1137.
    • (1998) J. Appl. Microbiol. , vol.84 , pp. 1131-1137
    • van Reenen, C.A.1    Dicks, L.M.T.2    Chikindas, M.L.3
  • 74
    • 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
    • Gallager, N.L.F.; Sailer, V.; Niemczura, W.P.; Nakashima, T.T.; Stiles, M.E.; Vederas, J.C. 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 1997, 36, 15062-15072.
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Gallager, N.L.F.1    Sailer, V.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 75
    • 84155184291 scopus 로고    scopus 로고
    • Substitution of a conserved disulfide in the type IIa bacteriocin, leucocin A, with L-leucine and L-serine residues: Effects on activity and three-dimensional structure
    • Sit, C.S.; Lohans, C.T.; van Belkum, M.J.; Campbell, C.D.; Miskolzie, M.; Vederas, J.C. Substitution of a conserved disulfide in the type IIa bacteriocin, leucocin A, with L-leucine and L-serine residues: Effects on activity and three-dimensional structure. ChemBioChem 2012, 13, 35-38.
    • (2012) ChemBioChem , vol.13 , pp. 35-38
    • Sit, C.S.1    Lohans, C.T.2    van Belkum, M.J.3    Campbell, C.D.4    Miskolzie, M.5    Vederas, J.C.6
  • 76
    • 0035960722 scopus 로고    scopus 로고
    • Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product
    • Ferchichi, M.; Frère, J.; Mabrouk, K.; Manai, M. Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product. FEMS Microbiol. Lett. 2001, 205, 49-55.
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 49-55
    • Ferchichi, M.1    Frère, J.2    Mabrouk, K.3    Manai, M.4
  • 77
    • 0028363167 scopus 로고
    • Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B
    • Quadri, L.E.; Sailer, M.; Roy, K.L.; Vederas, J.C.; Stiles, M.E. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B. J. Biol. Chem. 1994, 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
  • 78
    • 4143071761 scopus 로고    scopus 로고
    • Sodium chloride reduces production of Curvacin A, a bacteriocin produced by Lactobacillus curvatus strain LTH 1174, originating from fermented sausage
    • Verluyten, J.; Messens, W.; de Vuyst, L. Sodium chloride reduces production of Curvacin A, a bacteriocin produced by Lactobacillus curvatus strain LTH 1174, originating from fermented sausage. Appl. Environ. Microbiol. 2004, 70, 2271-2278.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2271-2278
    • Verluyten, J.1    Messens, W.2    de Vuyst, L.3
  • 79
    • 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.; Casaus, P.; Havarstein, L.S.; Hernandez, P.E.; Nes, I.F. Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum. Appl. Environ. Microbiol. 1997, 63, 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
  • 80
    • 0042160257 scopus 로고    scopus 로고
    • Characteristics and identification of enterocins produced by Enterococcus faecium JCM 5804T
    • Park, S.H.; Itoh, K.; Fujisawa, T. Characteristics and identification of enterocins produced by Enterococcus faecium JCM 5804T. J. Appl. Microbiol. 2003, 95, 294-300.
    • (2003) J. Appl. Microbiol. , vol.95 , pp. 294-300
    • Park, S.H.1    Itoh, K.2    Fujisawa, T.3
  • 81
    • 17644368144 scopus 로고    scopus 로고
    • Characterization of a bacteriocin produced by Enterococcus faecium GM-1 isolated from an infant
    • Kang, J.H.; Lee, M.S. Characterization of a bacteriocin produced by Enterococcus faecium GM-1 isolated from an infant. J. Appl. Microbiol. 2005, 98, 1169-1176.
    • (2005) J. Appl. Microbiol. , vol.98 , pp. 1169-1176
    • Kang, J.H.1    Lee, M.S.2
  • 82
    • 33845962373 scopus 로고    scopus 로고
    • Single nucleotide polymorphism analysis of the enterocin P structural gene of Enterococcus faecium strains isolated from nonfermented animal foods
    • Samuel, A.; Calo, P.; Franco, C.M.; Prado, M.; Cepeda, A.; Barros-Velazquez, J. Single nucleotide polymorphism analysis of the enterocin P structural gene of Enterococcus faecium strains isolated from nonfermented animal foods. Mol. Nutr. Food Res. 2006, 20, 1229-1238.
    • (2006) Mol. Nutr. Food Res. , vol.20 , pp. 1229-1238
    • Samuel, A.1    Calo, P.2    Franco, C.M.3    Prado, M.4    Cepeda, A.5    Barros-Velazquez, J.6
  • 83
    • 70349154139 scopus 로고    scopus 로고
    • Molecular and probiotic characterization of bacteriocin-producing Enterococcus faecium strains isolated from nonfermented animal foods
    • Hosseini, S.V.; Arlindo, S.; Böhme, K.; Fernández-No, C.; Calo-Mata, P.; Barros-Velázquez, J. Molecular and probiotic characterization of bacteriocin-producing Enterococcus faecium strains isolated from nonfermented animal foods. J. Appl. Microbiol. 2009, 107, 1392-1403.
    • (2009) J. Appl. Microbiol. , vol.107 , pp. 1392-1403
    • Hosseini, S.V.1    Arlindo, S.2    Böhme, K.3    Fernández-No, C.4    Calo-Mata, P.5    Barros-Velázquez, J.6
  • 84
    • 75349101606 scopus 로고    scopus 로고
    • Production, characterization, and antimicrobial activity of a bacteriocin from newly isolated Enterococcus faecium IJ-31
    • Javed, I.; Ahmed, S.; Manam, S.; Riaz, M.; Ahmad, B.; Ali, M.I.; Hameed, A.; Chaudry, G.J. Production, characterization, and antimicrobial activity of a bacteriocin from newly isolated Enterococcus faecium IJ-31. J. Food Prot. 2010, 73, 44-52.
    • (2010) J. Food Prot. , vol.73 , pp. 44-52
    • Javed, I.1    Ahmed, S.2    Manam, S.3    Riaz, M.4    Ahmad, B.5    Ali, M.I.6    Hameed, A.7    Chaudry, G.J.8
  • 85
    • 27944442272 scopus 로고    scopus 로고
    • Quorum sensing: Cell-to-cell communication in bacteria
    • Waters, C.M.; Bassler, B.L. Quorum sensing: Cell-to-cell communication in bacteria. Annu. Rev. Cell Dev. Biol. 2005, 21, 319-346.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 319-346
    • Waters, C.M.1    Bassler, B.L.2
  • 86
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem, M.; Quadri, L.E.N.; Kuipers, O.P.; de Vos, W.M. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol. Microbiol. 1997, 24, 895-904.
    • (1997) Mol. Microbiol. , vol.24 , pp. 895-904
    • Kleerebezem, M.1    Quadri, L.E.N.2    Kuipers, O.P.3    de Vos, W.M.4
  • 87
    • 70349772034 scopus 로고    scopus 로고
    • Quorum sensing and social networking in the microbial world
    • Atkinson, S.; Williams, P. Quorum sensing and social networking in the microbial world. J. R. Soc. Interface 2009, 6, 959-978.
    • (2009) J.R. Soc. Interface , vol.6 , pp. 959-978
    • Atkinson, S.1    Williams, P.2
  • 88
    • 0003085654 scopus 로고    scopus 로고
    • Regulation of Group II Peptide Bacteriocin Synthesis by Quorum-Sensing Mechanisms
    • In, Dunny, G.M., Winans, S.C., Eds.; American Society for Microbiology: Washington, DC, USA
    • Nes, I.F.; Eijsink, V.G.H. Regulation of Group II Peptide Bacteriocin Synthesis by Quorum-Sensing Mechanisms. In Cell-Cell Signalling in Bacteria; Dunny, G.M., Winans, S.C., Eds.; American Society for Microbiology: Washington, DC, USA, 1999; pp. 175-192.
    • (1999) Cell-Cell Signalling in Bacteria , pp. 175-192
    • Nes, I.F.1    Eijsink, V.G.H.2
  • 91
    • 0030012762 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins
    • Aymerich, T.; Holo, H.; Havarstein, L.S.; Hugas, M.; Garriga, M.; Nes, I.F. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microbiol. 1996, 62, 1676-1682.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1676-1682
    • Aymerich, T.1    Holo, H.2    Havarstein, L.S.3    Hugas, M.4    Garriga, M.5    Nes, I.F.6
  • 93
    • 0029919969 scopus 로고    scopus 로고
    • Analysis of the sakacin P gene cluster from Lactobacillus sake Lb674 and its expression in sakacin-negative Lb sake strains
    • Hühne, K.; Axelsson, L.; Holck, A.; Kröckel, L. Analysis of the sakacin P gene cluster from Lactobacillus sake Lb674 and its expression in sakacin-negative Lb. sake strains. Microbiology 1996, 142, 1437-1448.
    • (1996) Microbiology , vol.142 , pp. 1437-1448
    • Hühne, K.1    Axelsson, L.2    Holck, A.3    Kröckel, L.4
  • 94
    • 0030930569 scopus 로고    scopus 로고
    • Characterization of a locus from Carnobacterium piscicola LV17B involved in bacteriocin production and immunity: Evidence for global inducer-mediated transcriptional regulation
    • Quadri, L.E.N.; Kleerebezem, M.; Kuipers, O.P.; de Vos, W.M.; Roy, K.L.; Vederas, J.C.; Stiles, M.E. Characterization of a locus from Carnobacterium piscicola LV17B involved in bacteriocin production and immunity: Evidence for global inducer-mediated transcriptional regulation. J. Bacteriol. 1997, 179, 6163-6171.
    • (1997) J. Bacteriol. , vol.179 , pp. 6163-6171
    • Quadri, L.E.N.1    Kleerebezem, M.2    Kuipers, O.P.3    de Vos, W.M.4    Roy, K.L.5    Vederas, J.C.6    Stiles, M.E.7
  • 95
    • 17444395256 scopus 로고    scopus 로고
    • Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis
    • Herranz, C.; Driessen, A.J.M. Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis. Appl. Environ. Microbiol. 2005, 71, 1959-1963.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1959-1963
    • Herranz, C.1    Driessen, A.J.M.2
  • 96
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch, L.M. Signal sequences. Biochemistry 1989, 28, 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 97
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A.P. The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev. 1993, 57, 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 98
    • 0028128453 scopus 로고
    • Signal peptides: Exquisitely designed transport promoters
    • Izard, J.W.; Kendall, D.A. Signal peptides: Exquisitely designed transport promoters. Microbiol. Biotechnol. 1994, 13, 765-773.
    • (1994) Microbiol. Biotechnol. , vol.13 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 99
    • 0028845019 scopus 로고
    • Molecular characterization of genes involved in the production of the bacteriocin leucocin A from Leuconostoc gelidum
    • Van Belkum, M.J.; Stiles, M.E. Molecular characterization of genes involved in the production of the bacteriocin leucocin A from Leuconostoc gelidum. Appl. Environ. Microbiol. 1995, 61, 3573-3579.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3573-3579
    • van Belkum, M.J.1    Stiles, M.E.2
  • 101
    • 1542308527 scopus 로고    scopus 로고
    • Functional characterization of a composite bacteriocin locus from malt isolate Lactobacillus sakei 5
    • Vaughan, A.; Eijsink, V.G.; van Sinderen, D. Functional characterization of a composite bacteriocin locus from malt isolate Lactobacillus sakei 5. Appl. Environ. Microbiol. 2003, 69, 7194-7203.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 7194-7203
    • Vaughan, A.1    Eijsink, V.G.2    van Sinderen, D.3
  • 103
    • 0029094242 scopus 로고
    • Mesentericin Y105 gene clusters in Leuconostoc rnesenteroides Y 105
    • Fremaux, C.; Héchard, Y.; Cenatiempo, Y. Mesentericin Y105 gene clusters in Leuconostoc rnesenteroides Y 105. Microbiology 1995, 14, 1637-1645.
    • (1995) Microbiology , vol.14 , pp. 1637-1645
    • Fremaux, C.1    Héchard, Y.2    Cenatiempo, Y.3
  • 106
    • 56549098060 scopus 로고    scopus 로고
    • Anti-listerial activity of bacteriocin-producing Lactobacillus curvatus CWBI-B28 and Lactobacillus sakei CWBI-B1365 on raw beef and poultry meat
    • Dortu, C.; Huch, M.; Holzapfel, W.H.; Franz, C.M.A.P.; Thonart, P. Anti-listerial activity of bacteriocin-producing Lactobacillus curvatus CWBI-B28 and Lactobacillus sakei CWBI-B1365 on raw beef and poultry meat. Lett. Appl. Microbiol. 2008, 47, 581-586.
    • (2008) Lett. Appl. Microbiol. , vol.47 , pp. 581-586
    • Dortu, C.1    Huch, M.2    Holzapfel, W.H.3    Franz, C.M.A.P.4    Thonart, P.5
  • 108
    • 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.; Henz, M.E.; Gallagher, N.L.; Chai, S.; 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.
    • (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
  • 109
    • 0141817944 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge
    • Uteng, M.; Hauge, H.H.; Markwick, P.R.; Fimland, G.; Mantzilas, D.; Nissen-Meyer, J.; Muhle-Goll, C. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge. Biochemistry 2003, 42, 11417-11426.
    • (2003) Biochemistry , vol.42 , pp. 11417-11426
    • Uteng, M.1    Hauge, H.H.2    Markwick, P.R.3    Fimland, G.4    Mantzilas, D.5    Nissen-Meyer, J.6    Muhle-Goll, C.7
  • 110
    • 28944447119 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A
    • Haugen, H.S.; Fimland, G.; Nissen-Meyer, J.; Kristiansen, P.E. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A. Biochemistry 2005, 44, 16149-16157.
    • (2005) Biochemistry , vol.44 , pp. 16149-16157
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3    Kristiansen, P.E.4
  • 111
    • 3142737226 scopus 로고    scopus 로고
    • Dynamic relationships among type IIa bacteriocins: Temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic α-helix as a receptor binding region
    • 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 α-helix as a receptor binding region. Biochemistry 2004, 43, 9009-9020.
    • (2004) Biochemistry , vol.43 , pp. 9009-9020
    • Kaur, K.1    Andrew, L.C.2    Wishart, D.S.3    Vederas, J.C.4
  • 112
    • 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.; Blingsmo, O.R.; Sletten, K.; Jung, G.; Nes, I.F.; Nissen-Meyer, J. 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. 1996, 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
  • 113
    • 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.; Johnsen, L.; Axelsson, L.; Brurberg, M.B.; Nes, I.F.; Eijsink, V.G.H.; Nissen-Meyer, J. 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. 2000, 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
  • 114
    • 54349099254 scopus 로고    scopus 로고
    • Hydrophobic interactions as substitutes for a conserved disulfide linkage in the type IIa bacteriocins, leucocin A and pediocin PA-1
    • Derksen, D.J.; Boudreau, M.A.; Vederas, J.C. Hydrophobic interactions as substitutes for a conserved disulfide linkage in the type IIa bacteriocins, leucocin A and pediocin PA-1. ChemBioChem 2008, 9, 1898-1901.
    • (2008) ChemBioChem , vol.9 , pp. 1898-1901
    • Derksen, D.J.1    Boudreau, M.A.2    Vederas, J.C.3
  • 115
    • 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
  • 116
    • 33144455595 scopus 로고    scopus 로고
    • Determination of essential and variable residues in pediocin PA-1 by NNK scanning
    • Tominaga, T.; Hatakeyama, Y. Determination of essential and variable residues in pediocin PA-1 by NNK scanning. Appl. Environ. Microbiol. 2006, 72, 1141-1147.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1141-1147
    • Tominaga, T.1    Hatakeyama, Y.2
  • 117
    • 33750708896 scopus 로고    scopus 로고
    • Antimicrobial leucocin analogues with a disulfide bridge replaced by a carbocycle or by noncovalent interactions of allyl glycine residues
    • Derksen, D.J.; Stymiest, J.L.; Vederas, J.C. Antimicrobial leucocin analogues with a disulfide bridge replaced by a carbocycle or by noncovalent interactions of allyl glycine residues. J. Am. Chem. Soc. 2006, 128, 14252-14253.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14252-14253
    • Derksen, D.J.1    Stymiest, J.L.2    Vederas, J.C.3
  • 118
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson, E.G.; Thornton, J.M. A revised set of potentials for beta-turn formation in proteins. Protein Sci. 1994, 3, 2207-2216.
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 119
    • 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.; Gibbs, A.C.; Stiles, M.E.; Wishart, D.S.; Vederas, J.C. Analogues of bacteriocins: antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives. J. Med. Chem. 2000, 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
  • 120
    • 0031030583 scopus 로고    scopus 로고
    • Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli
    • Quadri, L.E.N.; Yan, L.Z.; Stiles, M.E.; Vederas, J.C. Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli. J. Biol. Chem. 1997, 272, 3384-3388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3384-3388
    • Quadri, L.E.N.1    Yan, L.Z.2    Stiles, M.E.3    Vederas, J.C.4
  • 121
    • 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.
    • (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
  • 123
    • 23044477877 scopus 로고    scopus 로고
    • Evidence on correlation between number ofdisulfide bridge and toxicity of class IIa bacteriocins
    • Richard, C.; Cañon, R.; Naghmouchi, K.; Bertrand, D.; Prévosta, H.; Drider, D. Evidence on correlation between number ofdisulfide bridge and toxicity of class IIa bacteriocins. Food Microbiol. 2006, 23, 175-183.
    • (2006) Food Microbiol. , vol.23 , pp. 175-183
    • Richard, C.1    Cañon, R.2    Naghmouchi, K.3    Bertrand, D.4    Prévosta, H.5    Drider, D.6
  • 124
    • 0030613798 scopus 로고    scopus 로고
    • The rpoN (σ54) gene from Listeria monocytogenes is involved in resistance to mesentericin Y105, an antibacterial peptide from Leuconostoc mesenteroides
    • Robichon, D.; Gouin, E.; Débarbouillé, M.; Cossart, P.; Cenatiempo, Y.; Héchard, Y. The rpoN (σ54) gene from Listeria monocytogenes is involved in resistance to mesentericin Y105, an antibacterial peptide from Leuconostoc mesenteroides. J. Bacteriol. 1997, 179, 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
  • 125
    • 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 sulfatepolyacrylamide gel electrophoresis
    • Ramnath, M.; Beukes, M.; Tamura, K.; Hastings, J.W. 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 sulfatepolyacrylamide gel electrophoresis. Appl. Environ. Microbiol. 2000, 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
  • 126
    • 0033661296 scopus 로고    scopus 로고
    • The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins
    • Dalet, K.; Briand, C.; Cenatiempo, Y.; Héchard, Y. The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins. Curr. Microbiol. 2000, 41, 441-443.
    • (2000) Curr. Microbiol. , vol.41 , pp. 441-443
    • Dalet, K.1    Briand, C.2    Cenatiempo, Y.3    Héchard, Y.4
  • 127
    • 0034969179 scopus 로고    scopus 로고
    • Analysis of σ54-dependent genes in Enterococcus faecalis: A mannose PTS permease (EIIMan) is involved in sensitivity to a bacteriocin, mesentericin Y105
    • Héchard, Y.; Pelletier, C.; Cenatiempo, Y.; Frère, J. Analysis of σ54-dependent genes in Enterococcus faecalis: A mannose PTS permease (EIIMan) is involved in sensitivity to a bacteriocin, mesentericin Y105. Microbiology 2001, 147, 1575-1580.
    • (2001) Microbiology , vol.147 , pp. 1575-1580
    • Héchard, Y.1    Pelletier, C.2    Cenatiempo, Y.3    Frère, J.4
  • 128
    • 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.; Héchard, Y. Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis. Microbiology 2004, 150, 2663-2668.
    • (2004) Microbiology , vol.150 , pp. 2663-2668
    • Ramnath, M.1    Arous, S.2    Gravesen, A.3    Hastings, J.W.4    Héchard, Y.5
  • 129
    • 33847796246 scopus 로고    scopus 로고
    • Common mechanisms of target cell recognition and immunity for class II bacteriocins
    • Diep, D.B.; Skaugen, M.; Salehian, Z.; Holo, H.; Nes, I.F. Common mechanisms of target cell recognition and immunity for class II bacteriocins. Proc. Natl. Acad. Sci. USA 2007, 104, 2384-2389.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2384-2389
    • Diep, D.B.1    Skaugen, M.2    Salehian, Z.3    Holo, H.4    Nes, I.F.5
  • 130
    • 78049439560 scopus 로고    scopus 로고
    • An extracellular loop of the mannose phosphotransferase system component IIC is responsible for specific targeting by class IIa bacteriocins
    • Kjos, M.; Salehian, Z.; Nes, I.F.; Diep, D.B. An extracellular loop of the mannose phosphotransferase system component IIC is responsible for specific targeting by class IIa bacteriocins. J. Bacteriol. 2010, 192, 5906-5913.
    • (2010) J. Bacteriol. , vol.192 , pp. 5906-5913
    • Kjos, M.1    Salehian, Z.2    Nes, I.F.3    Diep, D.B.4
  • 132
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P.W.; Lengeler, J.W.; Jacobson, G.R. Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 1993, 57, 543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 133
    • 0028934812 scopus 로고
    • Functional reconstitution of the purified mannose phosphotransferase system of Escherichia coli into phospholipid vesicles
    • Mao, Q.; Schunk, T.; Flukiger, K.; Erni, B. Functional reconstitution of the purified mannose phosphotransferase system of Escherichia coli into phospholipid vesicles. J. Biol. Chem. 1995, 270, 5258-5265.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5258-5265
    • Mao, Q.1    Schunk, T.2    Flukiger, K.3    Erni, B.4
  • 134
    • 84866290009 scopus 로고    scopus 로고
    • Natural antimicrobial peptides from bacteria: Characteristics and potential applications to fight against antibiotic resistance
    • Hassan, M.; Kjos, M.; Nes, I.F.; Diep, D.B.; Lotfipour, F. Natural antimicrobial peptides from bacteria: Characteristics and potential applications to fight against antibiotic resistance. J. Appl. Microbiol. 2012, 113, 723-736.
    • (2012) J. Appl. Microbiol. , vol.113 , pp. 723-736
    • Hassan, M.1    Kjos, M.2    Nes, I.F.3    Diep, D.B.4    Lotfipour, F.5
  • 135
    • 79958192769 scopus 로고    scopus 로고
    • Mechanisms of resistance to bacteriocins targeting the mannose phosphotransferase system
    • Kjos, M.; Nes I.F.; Diep, D.B. Mechanisms of resistance to bacteriocins targeting the mannose phosphotransferase system. Appl. Environ. Microbiol. 2011, 77, 3335-3342.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 3335-3342
    • Kjos, M.1    Nes, I.F.2    Diep, D.B.3
  • 136
    • 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
  • 137
    • 33745268861 scopus 로고    scopus 로고
    • Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745
    • Diep, D.B.; Godager, L.; Brede, D.; Nes, I.F. Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745. Microbiology 2006, 152, 1649-1659.
    • (2006) Microbiology , vol.152 , pp. 1649-1659
    • Diep, D.B.1    Godager, L.2    Brede, D.3    Nes, I.F.4
  • 138
    • 0042029595 scopus 로고    scopus 로고
    • Differences in susceptibility of Listeria monocytogenes strains to sakacin P, sakacin A, pediocin PA-1, and nisin
    • Katla, T.; Naterstad, K.; Vancanneyt, M.; Swings, J.; Axelsson, L. Differences in susceptibility of Listeria monocytogenes strains to sakacin P, sakacin A, pediocin PA-1, and nisin. Appl. Environ. Microbiol. 2003, 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
  • 139
    • 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
    • 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.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 140
    • 79953227398 scopus 로고    scopus 로고
    • Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1
    • Haugen, H.S.; Fimland, G.; Nissen-Meyer, J. Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1. Appl. Environ. Microbiol. 2011, 77, 1966-1972.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1966-1972
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3
  • 141
    • 33749608085 scopus 로고    scopus 로고
    • The mannose transporter complex: An open door for the macromolecular invasion of bacteria
    • Erni, B. The mannose transporter complex: An open door for the macromolecular invasion of bacteria. J. Bacteriol. 2006, 188, 7036-7038.
    • (2006) J. Bacteriol. , vol.188 , pp. 7036-7038
    • Erni, B.1
  • 143
    • 70449408699 scopus 로고    scopus 로고
    • Complex phenotypic and genotypic responses of Listeria monocytogenes strains exposed to the class IIa bacteriocin sakacin P
    • Tessema, G.T.; Moretro, T.; Kohler, A.; Axelsson, L.; Naterstad, K. Complex phenotypic and genotypic responses of Listeria monocytogenes strains exposed to the class IIa bacteriocin sakacin P. Appl. Environ. Microbiol. 2009, 75, 6973-6980.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6973-6980
    • Tessema, G.T.1    Moretro, T.2    Kohler, A.3    Axelsson, L.4    Naterstad, K.5
  • 144
    • 0035216679 scopus 로고    scopus 로고
    • A sigma (σ54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105
    • Dalet, K.; Cenatiempo, Y.; Cossart, P.; Hechard, Y. A sigma (σ54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 2001, 147, 3263-3269.
    • (2001) Microbiology , vol.147 , pp. 3263-3269
    • Dalet, K.1    Cenatiempo, Y.2    Cossart, P.3    Hechard, Y.4
  • 145
    • 0033771017 scopus 로고    scopus 로고
    • Use of two-dimensional electrophoresis to study differential protein expression in divercin V41-resistant and wild-type strains of Listeria monocytogenes
    • Duffes, F.; Jenoe, P.; Boyaval, P. Use of two-dimensional electrophoresis to study differential protein expression in divercin V41-resistant and wild-type strains of Listeria monocytogenes. Appl. Environ. Microbiol. 2000, 66, 4318-4324.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4318-4324
    • Duffes, F.1    Jenoe, P.2    Boyaval, P.3
  • 146
    • 15444378200 scopus 로고    scopus 로고
    • Novel activator of mannose-specific phosphotransferase system permease expression in Listeria innocua, identified by screening for pediocin AcH resistance
    • Xue, J.; Hunter, I.; Steinmetz, T.; Peters, A.; Ray, B.; Miller, K.W. Novel activator of mannose-specific phosphotransferase system permease expression in Listeria innocua, identified by screening for pediocin AcH resistance. Appl. Environ. Microbiol. 2005, 71, 1283-1290.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1283-1290
    • Xue, J.1    Hunter, I.2    Steinmetz, T.3    Peters, A.4    Ray, B.5    Miller, K.W.6
  • 147
    • 4444273749 scopus 로고    scopus 로고
    • Involvement of the mpo operon in resistance to class IIa bacteriocins in Listeria monocytogenes
    • Arous, S.; Dalet, K.; Hechard, Y. Involvement of the mpo operon in resistance to class IIa bacteriocins in Listeria monocytogenes. FEMS Microbiol. Lett. 2004, 238, 37-41.
    • (2004) FEMS Microbiol. Lett. , vol.238 , pp. 37-41
    • Arous, S.1    Dalet, K.2    Hechard, Y.3
  • 148
    • 79957640799 scopus 로고    scopus 로고
    • Nisin and class IIa bacteriocin resistance among Listeria and other foodborne pathogens and spoilage bacteria
    • Kaur, G.; Malik, R.K.; Mishra, S.K.; Singh, T.P.; Bhardwaj, A.; Singroha, G.; Vij, S.; Kumar, N. Nisin and class IIa bacteriocin resistance among Listeria and other foodborne pathogens and spoilage bacteria. Microb. Drug Resist. 2011, 17, 197-205.
    • (2011) Microb. Drug Resist. , vol.17 , pp. 197-205
    • Kaur, G.1    Malik, R.K.2    Mishra, S.K.3    Singh, T.P.4    Bhardwaj, A.5    Singroha, G.6    Vij, S.7    Kumar, N.8
  • 150
    • 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.; Axelsson, L.; Diep, D.B.; Håvarstein, L.S.; Holo, H.; Nes, I.F. Production of class II bacteriocins by lactic acid bacteria: An example of biological warfare and communication. Antonie Van Leeuwenhoek 2002, 81, 639-654.
    • (2002) Antonie Van 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
  • 151
    • 38949123362 scopus 로고    scopus 로고
    • High-throughput isolation of bacteriocin-producing lactic acid bacteria, with potential application in the brewing industry
    • Rouse, S.; Sun, F.; Vaughan, A.; van Sinderen, D. High-throughput isolation of bacteriocin-producing lactic acid bacteria, with potential application in the brewing industry. J. Inst. Brew. 2007, 113, 256-262.
    • (2007) J. Inst. Brew. , vol.113 , pp. 256-262
    • Rouse, S.1    Sun, F.2    Vaughan, A.3    van Sinderen, D.4
  • 152
    • 79551632430 scopus 로고    scopus 로고
    • Development of a PCR-based assay for rapid detection of class IIa bacteriocin genes
    • Wie{ogonek}ckowicz, M.; Schmidt, M.; Sip, A.; Grajek, W. Development of a PCR-based assay for rapid detection of class IIa bacteriocin genes. Lett. Appl. Microbiol. 2011, 52, 281-289.
    • (2011) Lett. Appl. Microbiol. , vol.52 , pp. 281-289
    • Wieckowicz, M.1    Schmidt, M.2    Sip, A.3    Grajek, W.4
  • 153
    • 0035018342 scopus 로고    scopus 로고
    • Characterization of bacteriocin N15 produced by Enterococcus faecium N15 and cloning of the related genes
    • Losteinkit, C.; Uchiyama, K.; Ochi, S.; Takaoka, T.; Nagahisa, K.; Shioya, S. Characterization of bacteriocin N15 produced by Enterococcus faecium N15 and cloning of the related genes. J. Biosci. Bioeng. 2001, 91, 390-395.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 390-395
    • Losteinkit, C.1    Uchiyama, K.2    Ochi, S.3    Takaoka, T.4    Nagahisa, K.5    Shioya, S.6
  • 155
    • 71549122267 scopus 로고    scopus 로고
    • Antimicrobial activity, safety aspects, and some technological properties of bacteriocinogenic Enterococcus faecium from artisanal Tunisian fermented meat
    • Belgacem, Z.B.; Abriouel, H.; Omar, N.B.; Lucas, R.; Martínez-Canamero, M.; Gálvez, A.; Manai, M. Antimicrobial activity, safety aspects, and some technological properties of bacteriocinogenic Enterococcus faecium from artisanal Tunisian fermented meat. Food Control 2010, 21, 462-470.
    • (2010) Food Control , vol.21 , pp. 462-470
    • Belgacem, Z.B.1    Abriouel, H.2    Omar, N.B.3    Lucas, R.4    Martínez-Canamero, M.5    Gálvez, A.6    Manai, M.7
  • 156
    • 71549123681 scopus 로고    scopus 로고
    • A novel method for rapid detection of class IIa bacteriocin-producing lactic acid bacteria
    • Yi, H.; Zhang, L.; Tuo, Y.; Han, X.; Du, M. A novel method for rapid detection of class IIa bacteriocin-producing lactic acid bacteria. Food Control 2010, 21, 426-430.
    • (2010) Food Control , vol.21 , pp. 426-430
    • Yi, H.1    Zhang, L.2    Tuo, Y.3    Han, X.4    Du, M.5
  • 157
    • 54049133603 scopus 로고    scopus 로고
    • Genetic screening of lactic acid bacteria of oenological origin for bacteriocin-encoding genes
    • Knoll, C.; Divol, B.; Toit, M. Genetic screening of lactic acid bacteria of oenological origin for bacteriocin-encoding genes. Food Microbiol. 2008, 25, 983-991.
    • (2008) Food Microbiol. , vol.25 , pp. 983-991
    • Knoll, C.1    Divol, B.2    Toit, M.3
  • 158
    • 29244432526 scopus 로고    scopus 로고
    • Genome update: Lactic acid bacteria genome sequencing is booming
    • Liu, M.J.; van Enckevort, F.H.J.; Siezen, R.J. Genome update: Lactic acid bacteria genome sequencing is booming. Microbiology 2005, 151, 3811-3814.
    • (2005) Microbiology , vol.151 , pp. 3811-3814
    • Liu, M.J.1    van Enckevort, F.H.J.2    Siezen, R.J.3
  • 159
  • 160
    • 1842664393 scopus 로고    scopus 로고
    • Exploration of antimicrobial potential in LAB by genomics
    • Nes, I.F.; Johnsborg, O. Exploration of antimicrobial potential in LAB by genomics. Curr. Opin. Biotechnol. 2004, 15, 100-104.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 100-104
    • Nes, I.F.1    Johnsborg, O.2
  • 161
    • 2942578482 scopus 로고    scopus 로고
    • Peptide signal molecules and bacteriocins in Gram-negative bacteria: A genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters
    • Dirix, G.; Monsieurs, P.; Dombrecht, B.; Daniels, R.; Marchalb, K.; Vanderleydena, J.; Michielsa, J. Peptide signal molecules and bacteriocins in Gram-negative bacteria: A genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters. Peptides 2004, 25, 1425-1440.
    • (2004) Peptides , vol.25 , pp. 1425-1440
    • Dirix, G.1    Monsieurs, P.2    Dombrecht, B.3    Daniels, R.4    Marchalb, K.5    Vanderleydena, J.6    Michielsa, J.7
  • 162
    • 2942525390 scopus 로고    scopus 로고
    • Screening genomes of Gram-positive bacteria for double-glycine-motif containing peptides
    • Dirix, G.; Monsieurs, P.; Marchal, K.; Vanderleyden, J.; Michiels, J. Screening genomes of Gram-positive bacteria for double-glycine-motif containing peptides. Microbiology 2004, 150, 1121-1126.
    • (2004) Microbiology , vol.150 , pp. 1121-1126
    • Dirix, G.1    Monsieurs, P.2    Marchal, K.3    Vanderleyden, J.4    Michiels, J.5
  • 163
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Wang, Z.; Wang, G. APD: The antimicrobial peptide database. Nucleic Acids Res. 2004, 32, D590-D592.
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.2
  • 165
    • 34249858459 scopus 로고    scopus 로고
    • AMPer: A database and an automated discovery tool for antimicrobial peptides
    • Fjell, C.D.; Hancock, R.E.; Cherkasov, A. AMPer: A database and an automated discovery tool for antimicrobial peptides. Bioinformatics 2007, 23, 1148-1155.
    • (2007) Bioinformatics , vol.23 , pp. 1148-1155
    • Fjell, C.D.1    Hancock, R.E.2    Cherkasov, A.3
  • 166
    • 84871683126 scopus 로고    scopus 로고
    • Available online, (accessed on 20 November 2012)
    • Bactibase: Database dedicated to bacteriocins. Available online: http://bactibase.pfba-lab-tun.org (accessed on 20 November 2012).
    • Bactibase: Database dedicated to bacteriocins
  • 167
    • 84871698698 scopus 로고    scopus 로고
    • Available online, (accessed on 20 November 2012)
    • Bagel2: The bacteriocin mining tool. Available online: http://bagel2.molgenrug.nl (accessed on 20 November 2012).
    • Bagel2: The bacteriocin mining tool
  • 168
    • 77249117208 scopus 로고    scopus 로고
    • BACTIBASE second release: A database and tool platform for bacteriocin characterization
    • Hammami, R.; Zouhir, A.; Lay, C.L.; Hamida, J.B.; Fliss, I. BACTIBASE second release: A database and tool platform for bacteriocin characterization. BMC Microbiol. 2010, 10, 22.
    • (2010) BMC Microbiol. , vol.10 , pp. 22
    • Hammami, R.1    Zouhir, A.2    Lay, C.L.3    Hamida, J.B.4    Fliss, I.5
  • 170
    • 79954616130 scopus 로고    scopus 로고
    • Prediction of antimicrobial peptides based on sequence alignment and feature selection methods
    • Wang, P.; Hu, L.; Liu, G.Y.; Jiang, N.; Chen, X.Y.; Xu, J.Y.; Zheng, W.; Li, L.; Tan, M.; Chen, Z.; et al. Prediction of antimicrobial peptides based on sequence alignment and feature selection methods. PLoS One 2011, 6, e18476.
    • (2011) PLoS One , vol.6
    • Wang, P.1    Hu, L.2    Liu, G.Y.3    Jiang, N.4    Chen, X.Y.5    Xu, J.Y.6    Zheng, W.7    Li, L.8    Tan, M.9    Chen, Z.10
  • 171
    • 84871155207 scopus 로고    scopus 로고
    • Prediction of antimicrobial peptides based on the adaptive neuro-Fuzzy inference system application
    • Fernandes, F.C.; Rigden, D.J.; Franco, O.L. Prediction of antimicrobial peptides based on the adaptive neuro-Fuzzy inference system application. Pept. Sci. 2012, 98, 280-287.
    • (2012) Pept. Sci. , vol.98 , pp. 280-287
    • Fernandes, F.C.1    Rigden, D.J.2    Franco, O.L.3
  • 172
    • 77954313195 scopus 로고    scopus 로고
    • Current trends in antimicrobial agent research: Chemo-and bioinformatics approaches
    • Hammami, R.; Fliss, I. Current trends in antimicrobial agent research: Chemo-and bioinformatics approaches. Drug Discov. Today 2010, 15, 540-546.
    • (2010) Drug Discov. Today , vol.15 , pp. 540-546
    • Hammami, R.1    Fliss, I.2
  • 174
    • 38849155828 scopus 로고    scopus 로고
    • QSAR modeling and computer-aided design of antimicrobial peptides
    • Jenssen, H.; Fjell, C.D.; Cherkasov, A.; Hancock, R.E. QSAR modeling and computer-aided design of antimicrobial peptides. J. Pept. Sci. 2008, 14, 110-114.
    • (2008) J. Pept. Sci. , vol.14 , pp. 110-114
    • Jenssen, H.1    Fjell, C.D.2    Cherkasov, A.3    Hancock, R.E.4
  • 175
    • 4344638189 scopus 로고    scopus 로고
    • De novo design of potent antimicrobial peptides
    • Frecer, V.; Ho, B.; Ding, J.L. De novo design of potent antimicrobial peptides. Antimicrob. Agents Chemother. 2004, 48, 3349-3357.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3349-3357
    • Frecer, V.1    Ho, B.2    Ding, J.L.3
  • 176
    • 12344320524 scopus 로고    scopus 로고
    • Application of 'inductive' QSAR descriptors for quantification of antibacterial activity of cationic polypeptides
    • Cherkasov, A.; Jankovic, B. Application of 'inductive' QSAR descriptors for quantification of antibacterial activity of cationic polypeptides. Molecules 2004, 9, 1034-1052.
    • (2004) Molecules , vol.9 , pp. 1034-1052
    • Cherkasov, A.1    Jankovic, B.2
  • 178
    • 83355168944 scopus 로고    scopus 로고
    • Prediction of antibacterial activity from physicochemical properties of antimicrobial peptides
    • Melo, M.N.; Ferre, R.; Feliu, L.; Bardají, E.; Planas, M.; Castanho, M.A.R.B. Prediction of antibacterial activity from physicochemical properties of antimicrobial peptides. PLoS One 2011, 6, e28549.
    • (2011) PLoS One , vol.6
    • Melo, M.N.1    Ferre, R.2    Feliu, L.3    Bardají, E.4    Planas, M.5    Castanho, M.A.R.B.6
  • 179
    • 33748950268 scopus 로고    scopus 로고
    • Molecular mechanism of antimicrobial peptides: The origin of cooperativity
    • Huang, H.W. Molecular mechanism of antimicrobial peptides: The origin of cooperativity. Biochim. Biophys. Acta 2006, 1758, 1292-1302.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1292-1302
    • Huang, H.W.1
  • 181
    • 34047249400 scopus 로고    scopus 로고
    • Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation
    • Melo, M.N.; Castanho, M.A. Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation. Biochim. Biophys. Acta 2007, 1768, 1277-1290.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1277-1290
    • Melo, M.N.1    Castanho, M.A.2
  • 182
    • 34548650215 scopus 로고    scopus 로고
    • Membrane insertion and bilayer perturbation by antimicrobial peptide CM15
    • Pistolesi, S.; Pogni, R.; Feix, J.B. Membrane insertion and bilayer perturbation by antimicrobial peptide CM15. Biophys. J. 2007, 93, 1651-1660.
    • (2007) Biophys. J. , vol.93 , pp. 1651-1660
    • Pistolesi, S.1    Pogni, R.2    Feix, J.B.3
  • 183
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, M.N.; Ferre, R.; Castanho, M.A. Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 2009, 7, 245-250.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 185
    • 79958768732 scopus 로고    scopus 로고
    • Development of wide-spectrum hybrid bacteriocins for food biopreservation
    • Acuña, L.; Morero, R.D.; Bellomio, A. Development of wide-spectrum hybrid bacteriocins for food biopreservation. Food Bioprocess Technol. 2011, 4, 1029-1049.
    • (2011) Food Bioprocess Technol. , vol.4 , pp. 1029-1049
    • Acuña, L.1    Morero, R.D.2    Bellomio, A.3
  • 186
    • 0032884253 scopus 로고    scopus 로고
    • Bacteriocin-like inhibitory activities among various species of Listeria
    • Kalmokoff, M.L.; Daley, E.; Austin, J.W.; Farber, J.M. Bacteriocin-like inhibitory activities among various species of Listeria. Int. J. Food Microbiol. 1999, 50, 191-201.
    • (1999) Int. J. Food Microbiol. , vol.50 , pp. 191-201
    • Kalmokoff, M.L.1    Daley, E.2    Austin, J.W.3    Farber, J.M.4
  • 187
    • 0032516737 scopus 로고    scopus 로고
    • A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: Full characterization and interaction with target organisms
    • Bennik, M.H.J.; Vanloo, B.; Brasseur, R.; Gorris, L.G.M.; Smid, E.J. A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: full characterization and interaction with target organisms. Biochim. Biophys. Acta 1998, 1373, 47-58.
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 47-58
    • Bennik, M.H.J.1    Vanloo, B.2    Brasseur, R.3    Gorris, L.G.M.4    Smid, E.J.5
  • 190
    • 12244269723 scopus 로고    scopus 로고
    • Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from Surimi-associated Carnobacterium piscicola CS526
    • Yamazaki, K.; Suzuki, M.; Kawai, Y.; Inoue, N.; Montville, T.J. Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from Surimi-associated Carnobacterium piscicola CS526. Appl. Environ. Microbiol. 2005, 71, 554-557.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 554-557
    • Yamazaki, K.1    Suzuki, M.2    Kawai, Y.3    Inoue, N.4    Montville, T.J.5
  • 191
    • 33749078143 scopus 로고    scopus 로고
    • Production of piscicolin 126 by Carnobacterium maltaromaticum UAL26 is controlled by temperature and induction peptide concentration
    • Gursky, L.J.; Martin, N.I.; Derksen, D.J.; van Belkum, M.J.; Kaur, K.; Vederas, J.C.; Stiles, M.E.; McMullen, L.M. Production of piscicolin 126 by Carnobacterium maltaromaticum UAL26 is controlled by temperature and induction peptide concentration. Arch. Microbiol. 2006, 186, 317-325.
    • (2006) Arch. Microbiol. , vol.186 , pp. 317-325
    • Gursky, L.J.1    Martin, N.I.2    Derksen, D.J.3    van Belkum, M.J.4    Kaur, K.5    Vederas, J.C.6    Stiles, M.E.7    McMullen, L.M.8
  • 193
    • 0029909789 scopus 로고    scopus 로고
    • Purification and amino acid sequences of piscicocins V1a and V1b, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity
    • Bhugaloo-Vial, P.; Dousset, X.; Metivier, A.; Sorokine, O.; Anglade, P.; Boyaval, P.; Marion, D. Purification and amino acid sequences of piscicocins V1a and V1b, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity. Appl. Environ. Microbiol. 1996, 62, 4410-4416.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4410-4416
    • Bhugaloo-Vial, P.1    Dousset, X.2    Metivier, A.3    Sorokine, O.4    Anglade, P.5    Boyaval, P.6    Marion, D.7
  • 194
    • 0031880230 scopus 로고    scopus 로고
    • Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4
    • Hyronimus, B.; Le Marrec, C.; Urdaci, M.C. Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4. J. Appl. Microbiol. 1998, 85, 42-50.
    • (1998) J. Appl. Microbiol. , vol.85 , pp. 42-50
    • Hyronimus, B.1    Le Marrec, C.2    Urdaci, M.C.3
  • 195
    • 0028339135 scopus 로고
    • Complete nucleotide sequence of pSMB 74, a plasmid encoding the production of pediocin AcH in Pediococcus acidilactici
    • Motlagh, A.; Bukhtiyarova, M.; Ray, B. Complete nucleotide sequence of pSMB 74, a plasmid encoding the production of pediocin AcH in Pediococcus acidilactici. Lett. Appl. Microbiol. 1994, 18, 305-312.
    • (1994) Lett. Appl. Microbiol. , vol.18 , pp. 305-312
    • Motlagh, A.1    Bukhtiyarova, M.2    Ray, B.3
  • 196
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto, L.J.C.; Meyer, J.N.; Sletten, K.; Peláz, C.; Nes, I.F. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 1992, 138, 1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Nieto, L.J.C.1    Meyer, J.N.2    Sletten, K.3    Peláz, C.4    Nes, I.F.5
  • 198
    • 34347400417 scopus 로고    scopus 로고
    • High resolution crystal structure of PedB: A structural basis for the classification of pediocin-like immunity proteins
    • Kim, I.K.; Kim, M.K.; Kim, J.Y.; Yim, H.S.; Cha, S.S.; Kang, S.O. High resolution crystal structure of PedB: A structural basis for the classification of pediocin-like immunity proteins. BMC Struct. Biol. 2007, 7, 35.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 35
    • Kim, I.K.1    Kim, M.K.2    Kim, J.Y.3    Yim, H.S.4    Cha, S.S.5    Kang, S.O.6
  • 199
    • 63849304558 scopus 로고    scopus 로고
    • Insights into structure-activity relationships in the c-terminal region of divercin V41, a class IIa bacteriocin with high-level antilisterial activity
    • Rihakova, J.; Petit, V.W.; Demnerova, K.; Prévost, H.; Rebuffat, S.; Drider, D. Insights into structure-activity relationships in the c-terminal region of divercin V41, a class IIa bacteriocin with high-level antilisterial activity. Appl. Environ. Microbiol. 2009, 75, 1811-1819.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 1811-1819
    • Rihakova, J.1    Petit, V.W.2    Demnerova, K.3    Prévost, H.4    Rebuffat, S.5    Drider, D.6
  • 200
    • 8344223629 scopus 로고    scopus 로고
    • Purification, characterization and amino acid sequencing of divergicin M35: A novel class IIa bacteriocin produced by Carnobacterium divergens M35
    • Tahiri, I.; Desbiens, M.; Benech, R.; Kheadr, E.; Lacroix, C.; Thibault, S.; Ouellet, D.; Fliss, I. Purification, characterization and amino acid sequencing of divergicin M35: a novel class IIa bacteriocin produced by Carnobacterium divergens M35. Int. J. Food Microbiol. 2004, 97, 123-136.
    • (2004) Int. J. Food Microbiol. , vol.97 , pp. 123-136
    • Tahiri, I.1    Desbiens, M.2    Benech, R.3    Kheadr, E.4    Lacroix, C.5    Thibault, S.6    Ouellet, D.7    Fliss, I.8
  • 201
    • 0035829346 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for production of enterocins A and B by Enterococcus faecium WHE 81
    • Ennahar, S.; Asou, Y.; Zendo, T.; Sonomoto, K.; Ishizaki, A. Biochemical and genetic evidence for production of enterocins A and B by Enterococcus faecium WHE 81. Int. J. Food Microbiol. 2001, 70, 291-301.
    • (2001) Int. J. Food Microbiol. , vol.70 , pp. 291-301
    • Ennahar, S.1    Asou, Y.2    Zendo, T.3    Sonomoto, K.4    Ishizaki, A.5
  • 202
    • 0032963888 scopus 로고    scopus 로고
    • Characterization and heterologous expression of the genes encoding enterocin a production, immunity, and regulation in Enterococcus faecium DPC1146
    • O'Keeffe, T.; Hill, C.; Ross, R.P. Characterization and heterologous expression of the genes encoding enterocin a production, immunity, and regulation in Enterococcus faecium DPC1146. Appl. Environ. Microbiol. 1999, 65, 1506-1515.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1506-1515
    • O'Keeffe, T.1    Hill, C.2    Ross, R.P.3
  • 203
    • 0034808402 scopus 로고    scopus 로고
    • Isolation and characterization of enterocin BC25 and occurrence of the entA gene among ruminal gram-positive cocci
    • Morovský, M.; Pristas, P.; Javorský, P.; Nes, I.F.; Holo, H. Isolation and characterization of enterocin BC25 and occurrence of the entA gene among ruminal gram-positive cocci. Microbiol. Res. 2001, 156, 133-138.
    • (2001) Microbiol. Res. , vol.156 , pp. 133-138
    • Morovský, M.1    Pristas, P.2    Javorský, P.3    Nes, I.F.4    Holo, H.5
  • 204
    • 33750973385 scopus 로고    scopus 로고
    • Genetic analysis of bacteriocin 43 of vancomycin-resistant Enterococcus faecium
    • Todokoro, D.; Tomita, H.; Inoue, T.; Ike, Y. Genetic analysis of bacteriocin 43 of vancomycin-resistant Enterococcus faecium. Appl. Environ. Microbiol. 2006, 72, 6955-6964.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 6955-6964
    • Todokoro, D.1    Tomita, H.2    Inoue, T.3    Ike, Y.4
  • 206
    • 33746069036 scopus 로고    scopus 로고
    • Bacteriocin T8, a novel class IIa sec-dependent bacteriocin produced by Enterococcus faecium T8, isolated from vaginal secretions of children infected with human immunodeficiency virus
    • De Kwaadsteniet, M.; Fraser, T.; van Reenen, C.A.; Dicks, L.M. Bacteriocin T8, a novel class IIa sec-dependent bacteriocin produced by Enterococcus faecium T8, isolated from vaginal secretions of children infected with human immunodeficiency virus. Appl. Environ. Microbiol. 2006, 72, 4761-4766.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4761-4766
    • de Kwaadsteniet, M.1    Fraser, T.2    van Reenen, C.A.3    Dicks, L.M.4
  • 208
    • 0030834391 scopus 로고    scopus 로고
    • Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese
    • Herbin, S.; Mathieu, F.; Brule, F.; Branlant, C.; Lefebvre, G.; Lebrihi, A. Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese. Curr. Microbiol. 1997, 35, 319-326.
    • (1997) Curr. Microbiol. , vol.35 , pp. 319-326
    • Herbin, S.1    Mathieu, F.2    Brule, F.3    Branlant, C.4    Lefebvre, G.5    Lebrihi, A.6
  • 209
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings, J.W.; Sailer, M.; Johnson, K.; Roy, K.L.; Vederas, J.C.; Stiles, M.E. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 1991, 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
  • 210
    • 0037464988 scopus 로고    scopus 로고
    • Characterization and heterologous expression of a class IIa bacteriocin, plantaricin 423 from Lactobacillus plantarum 423, in
    • Van Reenen, C.A.; Chikindas, M.L.; van Zyl, W.H.; Dicks, L.M. Characterization and heterologous expression of a class IIa bacteriocin, plantaricin 423 from Lactobacillus plantarum 423, in Saccharomyces cerevisiae. Int. J. Food Microbiol. 2003, 81, 29-40.
    • (2003) Saccharomyces cerevisiae. Int. J. Food Microbiol. , vol.81 , pp. 29-40
    • van Reenen, C.A.1    Chikindas, M.L.2    van Zyl, W.H.3    Dicks, L.M.4
  • 211
    • 33845520468 scopus 로고    scopus 로고
    • Expression of the immunity protein of plantaricin 423, produced by Lactobacillus plantarum 423, and analysis of the plasmid encoding the bacteriocin
    • Van Reenen, C.A.; van Zyl, W.H.; Dicks, L.M. Expression of the immunity protein of plantaricin 423, produced by Lactobacillus plantarum 423, and analysis of the plasmid encoding the bacteriocin. Appl. Environ. Microbiol. 2006, 72, 7644-7651.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 7644-7651
    • van Reenen, C.A.1    van Zyl, W.H.2    Dicks, L.M.3
  • 212
    • 33645098532 scopus 로고    scopus 로고
    • Adhesion of Lactobacillus plantarum 423 and Lactobacillus salivarius 241 to the intestinal tract of piglets, as recorded with fluorescent in situ hybridization (FISH), and production of plantaricin 423 by cells colonized to the ileum
    • Maré, L.; Wolfaardt, G.M.; Dicks, L.M.T. Adhesion of Lactobacillus plantarum 423 and Lactobacillus salivarius 241 to the intestinal tract of piglets, as recorded with fluorescent in situ hybridization (FISH), and production of plantaricin 423 by cells colonized to the ileum. J. Appl. Microbiol. 2006, 100, 838-845.
    • (2006) J. Appl. Microbiol. , vol.100 , pp. 838-845
    • Maré, L.1    Wolfaardt, G.M.2    Dicks, L.M.T.3
  • 213
    • 0027366019 scopus 로고
    • Detection of bacteriocins produced by Lactobacillus plantarum isolated from different foods
    • Atrih, A.; Rekhif, N.; Michel, M.; Lefebvre, G. Detection of bacteriocins produced by Lactobacillus plantarum isolated from different foods. Microbiology 1993, 75, 117-123.
    • (1993) Microbiology , vol.75 , pp. 117-123
    • Atrih, A.1    Rekhif, N.2    Michel, M.3    Lefebvre, G.4
  • 214
    • 0035882219 scopus 로고    scopus 로고
    • Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19
    • Atrih, A.; Rekhif, N.; Moir, A.J.; Lebrihi, A.; Lefebvre, G. Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19. Int. J. Food Microbiol. 2001, 68, 93-104.
    • (2001) Int. J. Food Microbiol. , vol.68 , pp. 93-104
    • Atrih, A.1    Rekhif, N.2    Moir, A.J.3    Lebrihi, A.4    Lefebvre, G.5
  • 215
    • 0027077825 scopus 로고
    • Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706
    • Holck, A.; Axelsson, L.; Birkeland, S.E.; Aukrust, T.; Blom, H. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706. J. Gen. Microbiol. 1992, 138, 2715-2720.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2715-2720
    • Holck, A.1    Axelsson, L.2    Birkeland, S.E.3    Aukrust, T.4    Blom, H.5
  • 216
    • 0027182036 scopus 로고
    • Cloning and nucleotide sequence of a gene from Lactobacillus sake Lb706 necessary for sakacin A production and immunity
    • Axelsson, L.; Holck, A.; Birkeland, S.E.; Aukrust, T.; Blom, H. Cloning and nucleotide sequence of a gene from Lactobacillus sake Lb706 necessary for sakacin A production and immunity. Appl. Environ. Microbiol. 1993, 59, 2868-2875.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2868-2875
    • Axelsson, L.1    Holck, A.2    Birkeland, S.E.3    Aukrust, T.4    Blom, H.5
  • 217
    • 0028963921 scopus 로고
    • The genes involved in production of and immunity to sakacin A, a bacteriocin from Lactobacillus sake Lb706
    • Axelsson, L.; Holck, A. The genes involved in production of and immunity to sakacin A, a bacteriocin from Lactobacillus sake Lb706. J. Bacteriol. 1995, 177, 2125-2137.
    • (1995) J. Bacteriol. , vol.177 , pp. 2125-2137
    • Axelsson, L.1    Holck, A.2


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