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Volumn 157, Issue 12, 2011, Pages 3256-3267

Target recognition, resistance, immunity and genome mining of class II bacteriocins from Gram-positive bacteria

Author keywords

[No Author keywords available]

Indexed keywords

AVICIN A; BACTERIOCIN; ENTEROCIN X; GARVICIN ML; LACTOCOCCIN A; LACTOCOCCIN B; PENOCIN A; UNCLASSIFIED DRUG;

EID: 82555181655     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.052571-0     Document Type: Review
Times cited : (107)

References (87)
  • 1
  • 2
    • 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. (2010). Molecular and genetic characterization of a novel bacteriocin locus in Enterococcus avium isolates from infants. Appl Environ Microbiol 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
  • 3
    • 78651070477 scopus 로고    scopus 로고
    • Use of the usp45 lactococcal secretion signal sequence to drive the secretion and functional expression of enterococcal bacteriocins in Lactococcus lactis
    • Borrero, J., Jiménez, J. J., Gútiez, L., Herranz, C., Cintas, L. M. & Hernández, P. E. (2011a). Use of the usp45 lactococcal secretion signal sequence to drive the secretion and functional expression of enterococcal bacteriocins in Lactococcus lactis. Appl Microbiol Biotechnol 89, 131-143.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 131-143
    • Borrero, J.1    Jiménez, J.J.2    Gútiez, L.3    Herranz, C.4    Cintas, L.M.5    Hernández, P.E.6
  • 4
    • 79251607581 scopus 로고    scopus 로고
    • Characterization of garvicin ML, a novel circular bacteriocin produced by Lactococcus garvieae DCC43, isolated from mallard ducks (Anas platyrhynchos)
    • Borrero, J., Brede, D. A., Skaugen, M., Diep, D. B., Herranz, C., Nes, I. F., Cintas, L. M. & Hernández, P. E. (2011b). Characterization of garvicin ML, a novel circular bacteriocin produced by Lactococcus garvieae DCC43, isolated from mallard ducks (Anas platyrhynchos). Appl Environ Microbiol 77, 369-373.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 369-373
    • Borrero, J.1    Brede, D.A.2    Skaugen, M.3    Diep, D.B.4    Herranz, C.5    Nes, I.F.6    Cintas, L.M.7    Hernández, P.E.8
  • 6
    • 77957346244 scopus 로고    scopus 로고
    • The ABC transporter AnrAB contributes to the innate resistance of Listeria monocytogenes to nisin, bacitracin, and various beta-lactam antibiotics
    • Collins, B., Curtis, N., Cotter, P. D., Hill, C. & Ross, R. P. (2010). The ABC transporter AnrAB contributes to the innate resistance of Listeria monocytogenes to nisin, bacitracin, and various beta-lactam antibiotics. Antimicrob Agents Chemother 54, 4416-4423.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 4416-4423
    • Collins, B.1    Curtis, N.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 7
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P. D., Hill, C. & Ross, R. P. (2005). Bacteriocins: developing innate immunity for food. Nat Rev Microbiol 3, 777-788.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 8
    • 33750071105 scopus 로고    scopus 로고
    • Complete sequence of the enterocin Q-encoding plasmid pCIZ2 from the multiple bacteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity
    • Criado, R., Diep, D. B., Aakra, A., Gutiérrez, J., Nes, I. F., Hernández, P. E. & Cintas, L. M. (2006). Complete sequence of the enterocin Q-encoding plasmid pCIZ2 from the multiple bacteriocin producer Enterococcus faecium L50 and genetic characterization of enterocin Q production and immunity. Appl Environ Microbiol 72, 6653-6666.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6653-6666
    • Criado, R.1    Diep, D.B.2    Aakra, A.3    Gutiérrez, J.4    Nes, I.F.5    Hernández, P.E.6    Cintas, L.M.7
  • 9
    • 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. (2000). The rpoN gene of Enterococcus faecalis directs sensitivity to subclass IIa bacteriocins. Curr Microbiol 41, 441-443.
    • (2000) Curr Microbiol , vol.41 , pp. 441-443
    • Dalet, K.1    Briand, C.2    Cenatiempo, Y.3    Héchard, Y.4
  • 10
    • 0035216679 scopus 로고    scopus 로고
    • A s54-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105
    • & European Listeria Genome Consortium
    • Dalet, K., Cenatiempo, Y., Cossart, P., Héchard, Y. & European Listeria Genome Consortium (2001). A s54-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105. Microbiology 147, 3263-3269.
    • (2001) Microbiology , vol.147 , pp. 3263-3269
    • Dalet, K.1    Cenatiempo, Y.2    Cossart, P.3    Héchard, Y.4
  • 11
    • 77954305252 scopus 로고    scopus 로고
    • BAGEL2: Mining for bacteriocins in genomic data
    • de Jong, A., van Heel, A. J., Kok, J. & Kuipers, O. P. (2010). BAGEL2: mining for bacteriocins in genomic data. Nucleic Acids Res 38 (Web Server issue), W647-W651
    • (2010) Nucleic Acids Res , vol.38 , Issue.Web Server issue
    • de Jong, A.1    van Heel, A.J.2    Kok, J.3    Kuipers, O.P.4
  • 12
    • 34548472002 scopus 로고    scopus 로고
    • Bacteriocins from lactic acid bacteria: Production, purification, and food applications
    • De Vuyst, L. & Leroy, F. (2007). Bacteriocins from lactic acid bacteria: production, purification, and food applications. J Mol Microbiol Biotechnol 13, 194-199.
    • (2007) J Mol Microbiol Biotechnol , vol.13 , pp. 194-199
    • de Vuyst, L.1    Leroy, F.2
  • 15
    • 0029565798 scopus 로고
    • A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11
    • Diep, D. B., Havarstein, L. S. & Nes, I. F. (1995). A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol Microbiol 18, 631-639.
    • (1995) Mol Microbiol , vol.18 , pp. 631-639
    • Diep, D.B.1    Havarstein, L.S.2    Nes, I.F.3
  • 16
    • 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. (2006). Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745. Microbiology 152, 1649-1659.
    • (2006) Microbiology , vol.152 , pp. 1649-1659
    • Diep, D.B.1    Godager, L.2    Brede, D.3    Nes, I.F.4
  • 17
    • 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. (2007). Common mechanisms of target cell recognition and immunity for class II bacteriocins. Proc Natl Acad Sci U S A 104, 2384-2389.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2384-2389
    • Diep, D.B.1    Skaugen, M.2    Salehian, Z.3    Holo, H.4    Nes, I.F.5
  • 18
    • 2942525390 scopus 로고    scopus 로고
    • Screening genomes of Gram-positive bacteria for doubleglycine-motif-containing peptides
    • Dirix, G., Monsieurs, P., Marchal, K., Vanderleyden, J. & Michiels, J. (2004). Screening genomes of Gram-positive bacteria for doubleglycine-motif-containing peptides. Microbiology 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
  • 21
    • 45149121558 scopus 로고    scopus 로고
    • The generation of nisin variants with enhanced activity against specific gram-positive pathogens
    • Field, D., Connor, P. M., Cotter, P. D., Hill, C. & Ross, R. P. (2008). The generation of nisin variants with enhanced activity against specific gram-positive pathogens. Mol Microbiol 69, 218-230.
    • (2008) Mol Microbiol , vol.69 , pp. 218-230
    • Field, D.1    Connor, P.M.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 22
    • 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. (1998). The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C terminus. Appl Environ Microbiol 64, 5057-5060.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 5057-5060
    • Fimland, G.1    Jack, R.2    Jung, G.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 23
    • 0041848440 scopus 로고    scopus 로고
    • Comparative studies of immunity proteins of pediocin-like bacteriocins
    • Fimland, G., Eijsink, V. G. & Nissen-Meyer, J. (2002a). Comparative studies of immunity proteins of pediocin-like bacteriocins. Microbiology 148, 3661-3670.
    • (2002) Microbiology , vol.148 , pp. 3661-3670
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 24
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland, G., Eijsink, V. G. & Nissen-Meyer, J. (2002b). Mutational analysis of the role of tryptophan residues in an antimicrobial peptide. Biochemistry 41, 9508-9515.
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 25
    • 33745467496 scopus 로고    scopus 로고
    • Mutational analysis and membrane-interactions of the b-sheet-like N-terminal domain of the pediocin-like antimicrobial peptide sakacin P
    • Fimland, G., Pirneskoski, J., Kaewsrichan, J., Jutila, A., Kristiansen, P. E., Kinnunen, P. K. & Nissen-Meyer, J. (2006). Mutational analysis and membrane-interactions of the b-sheet-like N-terminal domain of the pediocin-like antimicrobial peptide sakacin P. Biochim Biophys Acta 1764, 1132-1140.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1132-1140
    • Fimland, G.1    Pirneskoski, J.2    Kaewsrichan, J.3    Jutila, A.4    Kristiansen, P.E.5    Kinnunen, P.K.6    Nissen-Meyer, J.7
  • 26
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Fregeau Gallagher, N. L., Sailer, M., Niemczura, W. P., Nakashima, T. T., Stiles, M. E. & Vederas, J. C. (1997). Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria. Biochemistry 36, 15062-15072.
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Gallagher, N.L.F.1    Sailer, M.2    Niemczura, W.P.3    Nakashima, T.T.4    Stiles, M.E.5    Vederas, J.C.6
  • 27
    • 0141557576 scopus 로고    scopus 로고
    • Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins
    • Gajic, O., Buist, G., Kojic, M., Topisirovic, L., Kuipers, O. P. & Kok, J. (2003). Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal multidrug resistance proteins. J Biol Chem 278, 34291-34298.
    • (2003) J Biol Chem , vol.278 , pp. 34291-34298
    • Gajic, O.1    Buist, G.2    Kojic, M.3    Topisirovic, L.4    Kuipers, O.P.5    Kok, J.6
  • 29
    • 34250692043 scopus 로고    scopus 로고
    • Recent advances in bacteriocin application as antimicrobials
    • Gillor, O. & Ghazaryan, L. (2007). Recent advances in bacteriocin application as antimicrobials. Recent Pat Antiinfect Drug Discov 2, 115-122.
    • (2007) Recent Pat Antiinfect Drug Discov , vol.2 , pp. 115-122
    • Gillor, O.1    Ghazaryan, L.2
  • 30
    • 0036156627 scopus 로고    scopus 로고
    • Frequency of bacteriocin resistance development and associated fitness costs in Listeria monocytogenes
    • Gravesen, A., Jydegaard Axelsen, A. M., Mendes da Silva, J., Hansen, T. B. & Knøchel, S. (2002a). Frequency of bacteriocin resistance development and associated fitness costs in Listeria monocytogenes. Appl Environ Microbiol 68, 756-764.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 756-764
    • Gravesen, A.1    Axelsen, A.M.J.2    da Silva, J.M.3    Hansen, T.B.4    Knøchel, S.5
  • 32
    • 1642355184 scopus 로고    scopus 로고
    • Pbp2229-mediated nisin resistance mechanism in Listeria monocytogenes confers cross-protection to class IIa bacteriocins and affects virulence gene expression
    • Gravesen, A., Kallipolitis, B., Holmstrøm, K., Høiby, P. E., Ramnath, M. & Knøchel, S. (2004). Pbp2229-mediated nisin resistance mechanism in Listeria monocytogenes confers cross-protection to class IIa bacteriocins and affects virulence gene expression. Appl Environ Microbiol 70, 1669-1679.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 1669-1679
    • Gravesen, A.1    Kallipolitis, B.2    Holmstrøm, K.3    Høiby, P.E.4    Ramnath, M.5    Knøchel, S.6
  • 33
    • 20844444771 scopus 로고    scopus 로고
    • Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: Genetic requirements
    • Guiral, S., Mitchell, T. J., Martin, B. & Claverys, J. P. (2005). Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirements. Proc Natl Acad Sci U S A 102, 8710-8715.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8710-8715
    • Guiral, S.1    Mitchell, T.J.2    Martin, B.3    Claverys, J.P.4
  • 35
    • 28944447119 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocinlike antimicrobial peptide curvacin A
    • Haugen, H. S., Fimland, G., Nissen-Meyer, J. & Kristiansen, P. E. (2005). Three-dimensional structure in lipid micelles of the pediocinlike antimicrobial peptide curvacin A. Biochemistry 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
  • 36
    • 55049088136 scopus 로고    scopus 로고
    • Mutational analysis of the class IIa bacteriocin curvacin A and its orientation in target cell membranes
    • Haugen, H. S., Kristiansen, P. E., Fimland, G. & Nissen-Meyer, J. (2008). Mutational analysis of the class IIa bacteriocin curvacin A and its orientation in target cell membranes. Appl Environ Microbiol 74, 6766-6773.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6766-6773
    • Haugen, H.S.1    Kristiansen, P.E.2    Fimland, G.3    Nissen-Meyer, J.4
  • 37
    • 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. (2011). Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1. Appl Environ Microbiol 77, 1966-1972.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 1966-1972
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3
  • 38
    • 0034969179 scopus 로고    scopus 로고
    • Analysis of s54-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. & Frére, J. (2001). Analysis of s54-dependent genes in Enterococcus faecalis: a mannose PTS permease (EIIMan) is involved in sensitivity to a bacteriocin, mesentericin Y105. Microbiology 147, 1575-1580.
    • (2001) Microbiology , vol.147 , pp. 1575-1580
    • Héchard, Y.1    Pelletier, C.2    Cenatiempo, Y.3    Frére, J.4
  • 39
    • 0025861639 scopus 로고
    • A new bacteriocin from Lactococcus lactis subsp. cremoris: Isolation and characterization of the protein and its gene
    • Holo, H., Nilssen, O. & Nes, I. F. (1991). Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. J Bacteriol 173, 3879-3887.
    • (1991) J Bacteriol , vol.173 , pp. 3879-3887
    • Holo, H.1    Nilssen, O.2    Nes, I.F.3    Lactococcin, A.4
  • 40
    • 77954298757 scopus 로고    scopus 로고
    • Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides
    • Hu, C. B., Malaphan, W., Zendo, T., Nakayama, J. & Sonomoto, K. (2010). Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides. Appl Environ Microbiol 76, 4542-4545.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 4542-4545
    • Hu, C.B.1    Malaphan, W.2    Zendo, T.3    Nakayama, J.4    Sonomoto, K.5
  • 42
    • 0028990155 scopus 로고
    • Bacteriocins of gram-positive bacteria
    • Jack, R. W., Tagg, J. R. & Ray, B. (1995). Bacteriocins of gram-positive bacteria. Microbiol Rev 59, 171-200.
    • (1995) Microbiol Rev , vol.59 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 43
    • 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. (2005). 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 280, 9243-9250.
    • (2005) J Biol Chem , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 44
    • 0029768962 scopus 로고    scopus 로고
    • Characterisation of plantaricin KW30, a bacteriocin produced by Lactobacillus plantarum
    • Kelly, W. J., Asmundson, R. V. & Huang, C. M. (1996). Characterisation of plantaricin KW30, a bacteriocin produced by Lactobacillus plantarum. J Appl Bacteriol 81, 657-662.
    • (1996) J Appl Bacteriol , vol.81 , pp. 657-662
    • Kelly, W.J.1    Asmundson, R.V.2    Huang, C.M.3
  • 45
    • 0037335990 scopus 로고    scopus 로고
    • Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574
    • Kemperman, R., Kuipers, A., Karsens, H., Nauta, A., Kuipers, O. & Kok, J. (2003). Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574. Appl Environ Microbiol 69, 1589-1597.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 1589-1597
    • Kemperman, R.1    Kuipers, A.2    Karsens, H.3    Nauta, A.4    Kuipers, O.5    Kok, J.6
  • 46
    • 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. (2009). Class II one-peptide bacteriocins target a phylogenetically defined subgroup of mannose phosphotransferase systems on sensitive cells. Microbiology 155, 2949-2961.
    • (2009) Microbiology , vol.155 , pp. 2949-2961
    • Kjos, M.1    Nes, I.F.2    Diep, D.B.3
  • 47
    • 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. (2010). An extracellular loop of the mannose phosphotransferase system component IIC is responsible for specific targeting by class IIa bacteriocins. J Bacteriol 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
  • 48
    • 79958192769 scopus 로고    scopus 로고
    • Mechanisms of resistance to bacteriocins targeting the mannose phosphotransferase system
    • Kjos, M., Nes, I. F. & Diep, D. B. (2011). Mechanisms of resistance to bacteriocins targeting the mannose phosphotransferase system. Appl Environ Microbiol 77, 3335-3342.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 3335-3342
    • Kjos, M.1    Nes, I.F.2    Diep, D.B.3
  • 50
    • 35648954612 scopus 로고    scopus 로고
    • Diversity of bacteriocins and activity spectrum in Streptococcus pneumoniae
    • Lux, T., Nuhn, M., Hakenbeck, R. & Reichmann, P. (2007). Diversity of bacteriocins and activity spectrum in Streptococcus pneumoniae. J Bacteriol 189, 7741-7751.
    • (2007) J Bacteriol , vol.189 , pp. 7741-7751
    • Lux, T.1    Nuhn, M.2    Hakenbeck, R.3    Reichmann, P.4
  • 51
    • 78650902755 scopus 로고    scopus 로고
    • Identification of a genetic locus responsible for antimicrobial peptide resistance in Clostridium difficile
    • McBride, S. M. & Sonenshein, A. L. (2011). Identification of a genetic locus responsible for antimicrobial peptide resistance in Clostridium difficile. Infect Immun 79, 167-176.
    • (2011) Infect Immun , vol.79 , pp. 167-176
    • McBride, S.M.1    Sonenshein, A.L.2
  • 52
    • 0031985197 scopus 로고    scopus 로고
    • Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon
    • Miller, K. W., Schamber, R., Chen, Y. & Ray, B. (1998). Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon. Appl Environ Microbiol 64, 14-20.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 14-20
    • Miller, K.W.1    Schamber, R.2    Chen, Y.3    Ray, B.4
  • 53
    • 22144472374 scopus 로고    scopus 로고
    • Sakacin P non-producing Lactobacillus sakei strains contain homologues of the sakacin P gene cluster
    • Møretrø, T., Naterstad, K., Wang, E., Aasen, I. M., Chaillou, S., Zagorec, M. & Axelsson, L. (2005). Sakacin P non-producing Lactobacillus sakei strains contain homologues of the sakacin P gene cluster. Res Microbiol 156, 949-960.
    • (2005) Res Microbiol , vol.156 , pp. 949-960
    • Møretrø, T.1    Naterstad, K.2    Wang, E.3    Aasen, I.M.4    Chaillou, S.5    Zagorec, M.6    Axelsson, L.7
  • 54
    • 34347243525 scopus 로고    scopus 로고
    • Class I/ Class IIa bacteriocin cross-resistance phenomenon in Listeria monocytogenes
    • Naghmouchi, K., Kheadr, E., Lacroix, C. & Fliss, I. (2007). Class I/ Class IIa bacteriocin cross-resistance phenomenon in Listeria monocytogenes. Food Microbiol 24, 718-727.
    • (2007) Food Microbiol , vol.24 , pp. 718-727
    • Naghmouchi, K.1    Kheadr, E.2    Lacroix, C.3    Fliss, I.4
  • 56
    • 45749122840 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides (bacteriocins) in lactic acid bacteria: A review
    • Nes, I. F., Yoon, S.-S. & Diep, D. B. (2007). Ribosomally synthesized antimicrobial peptides (bacteriocins) in lactic acid bacteria: a review. Food Sci Biotechnol 16, 675-690.
    • (2007) Food Sci Biotechnol , vol.16 , pp. 675-690
    • Nes, I.F.1    Yoon, S.-S.2    Diep, D.B.3
  • 57
    • 65149100197 scopus 로고    scopus 로고
    • Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by gram-positive bacteria
    • Nissen-Meyer, J., Rogne, P., Oppegard, C., Haugen, H. S. & Kristiansen, P. E. (2009). Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by gram-positive bacteria. Curr Pharm Biotechnol 10, 19-37.
    • (2009) Curr Pharm Biotechnol , vol.10 , pp. 19-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegard, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 59
    • 34248158850 scopus 로고    scopus 로고
    • Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis
    • Oppegard, C., Fimland, G., Thorbaek, L. & Nissen-Meyer, J. (2007). Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis. Appl Environ Microbiol 73, 2931-2938.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2931-2938
    • Oppegard, C.1    Fimland, G.2    Thorbaek, L.3    Nissen-Meyer, J.4
  • 60
    • 42949148663 scopus 로고    scopus 로고
    • Mutational analysis of putative helix-helix interacting GxxxGmotifs and tryptophan residues in the two-peptide bacteriocin lactococcin G
    • Oppegard, C., Schmidt, J., Kristiansen, P. E. & Nissen-Meyer, J. (2008). Mutational analysis of putative helix-helix interacting GxxxGmotifs and tryptophan residues in the two-peptide bacteriocin lactococcin G. Biochemistry 47, 5242-5249.
    • (2008) Biochemistry , vol.47 , pp. 5242-5249
    • Oppegard, C.1    Schmidt, J.2    Kristiansen, P.E.3    Nissen-Meyer, J.4
  • 61
    • 76649116857 scopus 로고    scopus 로고
    • The lactococcin G immunity protein recognizes specific regions in both peptides constituting the two-peptide bacteriocin lactococcin G
    • Oppegard, C., Emanuelsen, L., Thorbek, L., Fimland, G. & Nissen-Meyer, J. (2010). The lactococcin G immunity protein recognizes specific regions in both peptides constituting the two-peptide bacteriocin lactococcin G. Appl Environ Microbiol 76, 1267-1273.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 1267-1273
    • Oppegard, C.1    Emanuelsen, L.2    Thorbek, L.3    Fimland, G.4    Nissen-Meyer, J.5
  • 62
    • 77955831314 scopus 로고    scopus 로고
    • Class IIa bacteriocin resistance in Enterococcus faecalis V583: The mannose PTS operon mediates global transcriptional responses
    • Opsata, M., Nes, I. F. & Holo, H. (2010). Class IIa bacteriocin resistance in Enterococcus faecalis V583: the mannose PTS operon mediates global transcriptional responses. BMC Microbiol 10, 224
    • (2010) BMC Microbiol , vol.10 , pp. 224
    • Opsata, M.1    Nes, I.F.2    Holo, H.3
  • 63
    • 0035339494 scopus 로고    scopus 로고
    • Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
    • Pei, J. & Grishin, N. V. (2001). Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem Sci 26, 275-277.
    • (2001) Trends Biochem Sci , vol.26 , pp. 275-277
    • Pei, J.1    Grishin, N.V.2
  • 64
    • 79958720098 scopus 로고    scopus 로고
    • Expansion of type II CAAX proteases reveals evolutionary origin of c-secretase subunit APH-1
    • Pei, J., Mitchell, D. A., Dixon, J. E. & Grishin, N. V. (2011). Expansion of type II CAAX proteases reveals evolutionary origin of c-secretase subunit APH-1. J Mol Biol 410, 18-26.
    • (2011) J Mol Biol , vol.410 , pp. 18-26
    • Pei, J.1    Mitchell, D.A.2    Dixon, J.E.3    Grishin, N.V.4
  • 66
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., Lengeler, J. W. & Jacobson, G. R. (1993). Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 57, 543-594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 67
    • 0031030583 scopus 로고    scopus 로고
    • Effect of amino acid substitutions on the activity of carnobacteriocin B2. Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli
    • Quadri, L. E., Yan, L. Z., Stiles, M. E. & Vederas, J. C. (1997). Effect of amino acid substitutions on the activity of carnobacteriocin B2. Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli. J Biol Chem 272, 3384-3388.
    • (1997) J Biol Chem , vol.272 , pp. 3384-3388
    • Quadri, L.E.1    Yan, L.Z.2    Stiles, M.E.3    Vederas, J.C.4
  • 68
    • 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. (2000). Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Appl EnvironMicrobiol 66, 3098-3101.
    • (2000) Appl EnvironMicrobiol , vol.66 , pp. 3098-3101
    • Ramnath, M.1    Beukes, M.2    Tamura, K.3    Hastings, J.W.4
  • 69
    • 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. (2004). Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis. Microbiology 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
  • 70
    • 79952773376 scopus 로고    scopus 로고
    • Effect of broad-and narrow-spectrum antimicrobials on Clostridium difficile and microbial diversity in a model of the distal colon
    • Rea, M. C., Dobson, A., O'Sullivan, O., Crispie, F., Fouhy, F., Cotter, P. D., Shanahan, F., Kiely, B., Hill, C. & Ross, R. P. (2011). Effect of broad-and narrow-spectrum antimicrobials on Clostridium difficile and microbial diversity in a model of the distal colon. Proc Natl Acad Sci U S A 108 (Suppl. 1), 4639-4644.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.SUPPL. 1 , pp. 4639-4644
    • Rea, M.C.1    Dobson, A.2    O'Sullivan, O.3    Crispie, F.4    Fouhy, F.5    Cotter, P.D.6    Shanahan, F.7    Kiely, B.8    Hill, C.9    Ross, R.P.10
  • 71
    • 0030613798 scopus 로고    scopus 로고
    • The rpoN (s54) 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. (1997). The rpoN (s54) gene from Listeria monocytogenes is involved in resistance to mesentericin Y105, an antibacterial peptide from Leuconostoc mesenteroides. J Bacteriol 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
  • 72
    • 14644446027 scopus 로고    scopus 로고
    • Evolution of the bacterial phosphotransferase system: From carriers and enzymes to group translocators
    • Saier, M. H., Hvorup, R. N. & Barabote, R. D. (2005). Evolution of the bacterial phosphotransferase system: from carriers and enzymes to group translocators. Biochem Soc Trans 33, 220-224.
    • (2005) Biochem Soc Trans , vol.33 , pp. 220-224
    • Saier, M.H.1    Hvorup, R.N.2    Barabote, R.D.3
  • 73
    • 65549126460 scopus 로고    scopus 로고
    • Plasmid pAMS1-encoded, bacteriocin-related "siblicide" in Enterococcus faecalis
    • Sedgley, C. M., Clewell, D. B. & Flannagan, S. E. (2009). Plasmid pAMS1-encoded, bacteriocin-related "siblicide" in Enterococcus faecalis. J Bacteriol 191, 3183-3188.
    • (2009) J Bacteriol , vol.191 , pp. 3183-3188
    • Sedgley, C.M.1    Clewell, D.B.2    Flannagan, S.E.3
  • 74
    • 79953770908 scopus 로고    scopus 로고
    • Structure-activity relationships of an antimicrobial peptide plantaricin s from two-peptide class IIb bacteriocins
    • Soliman, W., Wang, L., Bhattacharjee, S. & Kaur, K. (2011). Structure-activity relationships of an antimicrobial peptide plantaricin s from two-peptide class IIb bacteriocins. J Med Chem 54, 2399-2408.
    • (2011) J Med Chem , vol.54 , pp. 2399-2408
    • Soliman, W.1    Wang, L.2    Bhattacharjee, S.3    Kaur, K.4
  • 75
    • 4644356516 scopus 로고    scopus 로고
    • NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2
    • Sprules, T., Kawulka, K. E. & Vederas, J. C. (2004). NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2. Biochemistry 43, 11740-11749.
    • (2004) Biochemistry , vol.43 , pp. 11740-11749
    • Sprules, T.1    Kawulka, K.E.2    Vederas, J.C.3
  • 77
    • 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., Møretrø, T., Kohler, A., Axelsson, L. & Naterstad, K. (2009). Complex phenotypic and genotypic responses of Listeria monocytogenes strains exposed to the class IIa bacteriocin sakacin P. Appl Environ Microbiol 75, 6973-6980.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 6973-6980
    • Tessema, G.T.1    Møretrø, T.2    Kohler, A.3    Axelsson, L.4    Naterstad, K.5
  • 78
    • 33144455595 scopus 로고    scopus 로고
    • Determination of essential and variable residues in pediocin PA-1 by NNK scanning
    • Tominaga, T. & Hatakeyama, Y. (2006). Determination of essential and variable residues in pediocin PA-1 by NNK scanning. Appl Environ Microbiol 72, 1141-1147.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1141-1147
    • Tominaga, T.1    Hatakeyama, Y.2
  • 79
    • 34548293678 scopus 로고    scopus 로고
    • Development of innovative pediocin PA-1 by DNA shuffling among class IIa bacteriocins
    • Tominaga, T. & Hatakeyama, Y. (2007). Development of innovative pediocin PA-1 by DNA shuffling among class IIa bacteriocins. Appl Environ Microbiol 73, 5292-5299.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5292-5299
    • Tominaga, T.1    Hatakeyama, Y.2
  • 80
    • 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. (2003). 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 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
  • 81
    • 0036840326 scopus 로고    scopus 로고
    • Membranes of class IIa bacteriocin-resistant Listeria monocytogenes cells contain increased levels of desaturated and short-acylchain phosphatidylglycerols
    • Vadyvaloo, V., Hastings, J. W., van der Merwe, M. J. & Rautenbach, M. (2002). Membranes of class IIa bacteriocin-resistant Listeria monocytogenes cells contain increased levels of desaturated and short-acylchain phosphatidylglycerols. Appl Environ Microbiol 68, 5223-5230.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5223-5230
    • Vadyvaloo, V.1    Hastings, J.W.2    van der Merwe, M.J.3    Rautenbach, M.4
  • 82
    • 1242318716 scopus 로고    scopus 로고
    • Physiological implications of class IIa bacteriocin resistance in Listeria monocytogenes strains
    • Vadyvaloo, V., Snoep, J. L., Hastings, J. W. & Rautenbach, M. (2004a). Physiological implications of class IIa bacteriocin resistance in Listeria monocytogenes strains. Microbiology 150, 335-340.
    • (2004) Microbiology , vol.150 , pp. 335-340
    • Vadyvaloo, V.1    Snoep, J.L.2    Hastings, J.W.3    Rautenbach, M.4
  • 85
    • 70350491392 scopus 로고    scopus 로고
    • Regulation of mannose phosphotransferase system permease and virulence gene expression in Listeria monocytogenes by the EIIMan t transporter
    • Vu-Khac, H. & Miller, K. W. (2009). Regulation of mannose phosphotransferase system permease and virulence gene expression in Listeria monocytogenes by the EIIMan t transporter. Appl Environ Microbiol 75, 6671-6678.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 6671-6678
    • Vu-Khac, H.1    Miller, K.W.2
  • 86
    • 34548515942 scopus 로고    scopus 로고
    • Regulation of the mpt operon in Listeria innocua by the ManR protein
    • Xue, J. & Miller, K. W. (2007). Regulation of the mpt operon in Listeria innocua by the ManR protein. Appl Environ Microbiol 73, 5648-5652.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5648-5652
    • Xue, J.1    Miller, K.W.2
  • 87
    • 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. (2000). Analogues of bacteriocins: antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives. J Med Chem 43, 4579-4581.
    • (2000) J Med Chem , vol.43 , pp. 4579-4581
    • Yan, L.Z.1    Gibbs, A.C.2    Stiles, M.E.3    Wishart, D.S.4    Vederas, J.C.5


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