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Volumn 64, Issue 6, 1998, Pages 2269-2272

Antagonistic activity of Lactobacillus plantarum C11: Two new two- peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIOCIN; PLANTARICIN; PLANTARICIN A; UNCLASSIFIED DRUG;

EID: 0031775980     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.6.2269-2272.1998     Document Type: Article
Times cited : (238)

References (33)
  • 1
    • 0029014984 scopus 로고
    • Pore-forming bacteriocins of gram-positive bacteria and self-protection mechanisms of producer organisms
    • Abee, T. 1995. Pore-forming bacteriocins of gram-positive bacteria and self-protection mechanisms of producer organisms. FEMS Microbiol. Lett. 129: 1-10.
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 1-10
    • Abee, T.1
  • 2
    • 0028220778 scopus 로고
    • Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon
    • Allison, G. E., C. Fremaux, and T. R. Klaenhammer. 1994. Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176:2235-2241.
    • (1994) J. Bacteriol. , vol.176 , pp. 2235-2241
    • Allison, G.E.1    Fremaux, C.2    Klaenhammer, T.R.3
  • 3
    • 0030779483 scopus 로고    scopus 로고
    • Pheromone-induced production of antimicrobial peptides in Lactobacillus
    • Brurberg, M. B., I. F. Nes, and V. G. H. Eijsink. 1997. Pheromone-induced production of antimicrobial peptides in Lactobacillus. Mol. Microbiol. 26: 347-360.
    • (1997) Mol. Microbiol. , vol.26 , pp. 347-360
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.H.3
  • 4
    • 0030789029 scopus 로고    scopus 로고
    • Enterocin B, a new bacteriocin from Enterococcus faecium T136 which can act synergistically with enterocin A
    • Casaus, P., T. Nilsen, L. M. Cintas, I. F. Nes, P. E. Hernández, and H. Holo. 1997. Enterocin B, a new bacteriocin from Enterococcus faecium T136 which can act synergistically with enterocin A. Microbiology 143:2287-2294.
    • (1997) Microbiology , vol.143 , pp. 2287-2294
    • Casaus, P.1    Nilsen, T.2    Cintas, L.M.3    Nes, I.F.4    Hernández, P.E.5    Holo, H.6
  • 6
    • 0029565798 scopus 로고
    • A bacteriocin-like peptide induces bacteriocin synthesis in L. plantarum C11
    • Diep, D. B., L. S. Håvarstein, and I. F. Nes. 1995. A bacteriocin-like peptide induces bacteriocin synthesis in L. plantarum C11. Mol. Microbiol. 18:631-639.
    • (1995) Mol. Microbiol. , vol.18 , pp. 631-639
    • Diep, D.B.1    Håvarstein, L.S.2    Nes, I.F.3
  • 7
    • 0029772572 scopus 로고    scopus 로고
    • Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11
    • Diep, D. B., L. S. Håvarstein, and I. F. Nes. 1996. Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J. Bacteriol. 178:4472-4483.
    • (1996) J. Bacteriol. , vol.178 , pp. 4472-4483
    • Diep, D.B.1    Håvarstein, L.S.2    Nes, I.F.3
  • 8
    • 0028052910 scopus 로고
    • The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcriptional unit as an agr-like regulatory system
    • Diep, D. B., L. S. Håvarstein, J. Nissen-Meyer, and I. F. Nes. 1994. The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcriptional unit as an agr-like regulatory system. Appl. Environ. Microbiol. 60:160-166.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 160-166
    • Diep, D.B.1    Håvarstein, L.S.2    Nissen-Meyer, J.3    Nes, I.F.4
  • 9
    • 0029989630 scopus 로고    scopus 로고
    • Induction of bacteriocin production in Lactobacillus sake by a secreted peptide
    • Eijsink, V. G. H., M. B. Brurberg, P. H. Middelhoven, and I. F. Nes. 1996. Induction of bacteriocin production in Lactobacillus sake by a secreted peptide. J. Bacteriol. 178:2232-2237.
    • (1996) J. Bacteriol. , vol.178 , pp. 2232-2237
    • Eijsink, V.G.H.1    Brurberg, M.B.2    Middelhoven, P.H.3    Nes, I.F.4
  • 10
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland, G., O. Blingsmo, K. Sletten, G. Jung, I. F. Nes, and J. Nissen-Meyer. 1996. New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: the C-terminal region is important for determining specificity. Appl. Environ. Microbiol. 62:3313-3318.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, O.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 11
    • 0032005933 scopus 로고    scopus 로고
    • Amphiphilic α-helices are important structural motifs in the α and β peptides that constitute the bacteriocin lactococcin G
    • Hauge, H. H., J. Nissen-Meyer, I. F. Nes, and V. G. H. Eijsink. 1998. Amphiphilic α-helices are important structural motifs in the α and β peptides that constitute the bacteriocin lactococcin G. Eur. J. Biochem. 251: 565-572.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 565-572
    • Hauge, H.H.1    Nissen-Meyer, J.2    Nes, I.F.3    Eijsink, V.G.H.4
  • 12
    • 84920308171 scopus 로고    scopus 로고
    • Håvarstein, L. S. Unpublished data
    • 11a. Håvarstein, L. S. Unpublished data.
  • 13
    • 0029013783 scopus 로고
    • A family of ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Håvarstein, L. S., D. B. Diep, and I. F. Nes. 1995. A family of ABC transporters carry out proteolytic processing of their substrates concomitant with export. Mol. Microbiol. 16:229-240.
    • (1995) Mol. Microbiol. , vol.16 , pp. 229-240
    • Håvarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 14
    • 0025861639 scopus 로고
    • Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: Isolation and characterization of the protein and its gene
    • Holo, H., Ø. Nilssen, and I. F. Nes. 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, Ø.2    Nes, I.F.3
  • 15
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer, T. R. 1993. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12:39-86.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-86
    • Klaenhammer, T.R.1
  • 16
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem, M., L. E. N. Quadri, O. P. Kuipers, and W. M. De Vos. 1997. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol. Microbiol. 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
  • 18
    • 0030921926 scopus 로고    scopus 로고
    • Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor
    • Marciset, O., M. C. Jeronimus-Stratingh, B. Mollet, and B. Poolman. 1997. Thermophilin 13, a nontypical antilisterial poration complex bacteriocin, that functions without a receptor. J. Biol. Chem. 272:14277-14284.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14277-14284
    • Marciset, O.1    Jeronimus-Stratingh, M.C.2    Mollet, B.3    Poolman, B.4
  • 21
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto Lozano, J. C., J. Nissen-Meyer, K. Sletten, C. Peláz, and I. F. Nes. 1992. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 138:1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Nieto Lozano, J.C.1    Nissen-Meyer, J.2    Sletten, K.3    Peláz, C.4    Nes, I.F.5
  • 22
    • 84920308170 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides produced by lactic acid bacteria: Their function, structure, biogenesis, and their mechanism of action
    • in press
    • Nissen-Meyer, J., H. H. Hange, G. Fimland, V. G. H. Eijsink, and I. F. Nes. Ribosomally synthesized antimicrobial peptides produced by lactic acid bacteria: their function, structure, biogenesis, and their mechanism of action. Recent Res. Dev. Microbiol., in press.
    • Recent Res. Dev. Microbiol.
    • Nissen-Meyer, J.1    Hange, H.H.2    Fimland, G.3    Eijsink, V.G.H.4    Nes, I.F.5
  • 23
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer, J., H. Holo, S. L. Håvarstein, K. Sletten, and I. F. Nes. 1992. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J. Bacteriol. 174:5686-5692.
    • (1992) J. Bacteriol. , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Håvarstein, S.L.3    Sletten, K.4    Nes, I.F.5
  • 24
    • 0027358736 scopus 로고
    • Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides
    • Nissen-Meyer, J., A. Granly Larsen, K. Sletten, M. Daeschel, and I. F. Nes. 1993. Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides. J. Gen. Microbiol. 139:1973-1978.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1973-1978
    • Nissen-Meyer, J.1    Granly Larsen, A.2    Sletten, K.3    Daeschel, M.4    Nes, I.F.5
  • 25
    • 0031030583 scopus 로고    scopus 로고
    • Effect of amino acid substitutions on the activity of carnobacteriocin B2
    • Quadri, L. E. N., L. Z. Yan, M. E. Stiles, and J. C. Vederas. 1997. Effect of amino acid substitutions on the activity of carnobacteriocin B2. J. Biol. Chem. 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
  • 26
    • 0028363167 scopus 로고
    • Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B
    • Quadri, L. E. N., M. Sailer, K. L. Roy, J. C. Vederas, and M. E. Stiles. 1994. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B. J. Biol. Chem. 269:12204-12211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12204-12211
    • Quadri, L.E.N.1    Sailer, M.2    Roy, K.L.3    Vederas, J.C.4    Stiles, M.E.5
  • 27
    • 0030010883 scopus 로고    scopus 로고
    • Genes responsible for nisin synthesis, regulation and immunity form a regulon of two operons and are induced by nisin in Lactococcus lactis N8
    • Ra, S. R., M. Qiao, T. Immonen, I. Pujana, and P. E. J. Saris. 1996. Genes responsible for nisin synthesis, regulation and immunity form a regulon of two operons and are induced by nisin in Lactococcus lactis N8. Microbiology 142:1281-1288.
    • (1996) Microbiology , vol.142 , pp. 1281-1288
    • Ra, S.R.1    Qiao, M.2    Immonen, T.3    Pujana, I.4    Saris, P.E.J.5
  • 28
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • Sahl, H.-G., R. W. Jack, and G. Bierbaum. 1995. Biosynthesis and biological activities of lantibiotics with unique post-translational modifications. Eur. J. Biochem. 230:827-853.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 827-853
    • Sahl, H.-G.1    Jack, R.W.2    Bierbaum, G.3
  • 29
    • 0030979140 scopus 로고    scopus 로고
    • Transcriptional analysis and regulation of carnobacteriocin production in Carnobacterium piscicola LV17
    • Saucier, L., A. S. Paradkar, L. S. Frost, S. E. Jensen, and M. E. Stiles. 1997. Transcriptional analysis and regulation of carnobacteriocin production in Carnobacterium piscicola LV17. Gene 188:271-277.
    • (1997) Gene , vol.188 , pp. 271-277
    • Saucier, L.1    Paradkar, A.S.2    Frost, L.S.3    Jensen, S.E.4    Stiles, M.E.5
  • 31
    • 0026802510 scopus 로고
    • Characterization of the bacteriocins curvacin a from Lactobacillus curvatus LTH1174 and sakacin P from L. sake LTH673
    • Tichaczek, P. S., J. Nissen-Meyer, I. F. Nes, R. F. Vogel, and W. P. Hammes. 1992. Characterization of the bacteriocins curvacin A from Lactobacillus curvatus LTH1174 and sakacin P from L. sake LTH673. Syst. Appl. Microbiol. 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
  • 33
    • 0029100551 scopus 로고
    • Lactococcal bacteriocins: Mode of action and immunity
    • Venema, K., G. Venema, and J. Kok. 1995. Lactococcal bacteriocins: mode of action and immunity. Trends Microbiol. 3:299-304.
    • (1995) Trends Microbiol. , vol.3 , pp. 299-304
    • Venema, K.1    Venema, G.2    Kok, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.