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Volumn 63, Issue 2, 1997, Pages 524-531

Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationshipto a predicted tertiary structure

Author keywords

[No Author keywords available]

Indexed keywords

LIPOSOME;

EID: 0030999249     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.2.524-531.1997     Document Type: Article
Times cited : (91)

References (56)
  • 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
  • 4
    • 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., H. Holo, L. S. Havarstein, M. Hugas, M. Garriga, and I. F. Nes. 1996. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microbiol. 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
  • 5
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M. J., S. Choe, and D. Eisenberg. 1994. Domain swapping: entangling alliances between proteins. Proc. Natl. Acad. Sci. USA 91:3127-3131.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 6
    • 0003123005 scopus 로고
    • Mechanism of channel formation by lantibiotics in black lipid membranes
    • G. Jung and H.-G. Salh (ed.), Escom Publishers, Leiden, The Netherlands
    • Bens, R., G. Jung, and H.-G. Shal. 1991. Mechanism of channel formation by lantibiotics in black lipid membranes. p. 359-372. In G. Jung and H.-G. Salh (ed.), Nisin and novel lantibiotics. Escom Publishers, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 359-372
    • Bens, R.1    Jung, G.2    Shal, H.-G.3
  • 8
    • 0027197506 scopus 로고
    • Common mechanistic action of bacteriocins from lactic acid bacteria
    • Bruno, M. E. C., and T. J. Montville. 1993. Common mechanistic action of bacteriocins from lactic acid bacteria. Appl. Environ. Microbiol. 59:3003-3010.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3003-3010
    • Bruno, M.E.C.1    Montville, T.J.2
  • 9
    • 0028868950 scopus 로고
    • Efflux of ions and ATP depletion induced by pediocin PA-1 are concomitant with cell death in Listeria monocytogenes Scott A
    • Chen, Y., and T. J. Montville. 1995. Efflux of ions and ATP depletion induced by pediocin PA-1 are concomitant with cell death in Listeria monocytogenes Scott A. J. Appl. Bacteriol. 79:684-690.
    • (1995) J. Appl. Bacteriol. , vol.79 , pp. 684-690
    • Chen, Y.1    Montville, T.J.2
  • 13
    • 0001040367 scopus 로고
    • An algorithm for protein secondary structure prediction based on class prediction
    • Deleage, G., and B. Roux. 1987. An algorithm for protein secondary structure prediction based on class prediction. Protein Eng. 1:289-294.
    • (1987) Protein Eng. , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 14
    • 0030047564 scopus 로고    scopus 로고
    • Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity, a monolayer study
    • Demel, R. A., T. Peelen, R. J. Siezen, B. de Kruijff, and O. P. Kuipers. 1996. Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipids correlate with antimicrobial activity, a monolayer study. Eur. J. Biochem. 235:267-274.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 267-274
    • Demel, R.A.1    Peelen, T.2    Siezen, R.J.3    De Kruijff, B.4    Kuipers, O.P.5
  • 15
    • 0027325787 scopus 로고
    • Insertion of lipids and proteins into bacterial membranes by fusion with liposomes
    • Driessen, A. J. M., and W. N. Konings. 1993. Insertion of lipids and proteins into bacterial membranes by fusion with liposomes. Methods Enzymol. 221: 394-408.
    • (1993) Methods Enzymol. , vol.221 , pp. 394-408
    • Driessen, A.J.M.1    Konings, W.N.2
  • 17
    • 0027453022 scopus 로고
    • In vitro pore-forming activity of the lantibiotic nisin: Role of the proton motive force and lipid composition
    • García-Garcerá, M. J., M. G. L. Elfernic, A. J. M. Driessen, and W. N. Konings. 1993. In vitro pore-forming activity of the lantibiotic nisin: role of the proton motive force and lipid composition. Eur. J. Biochem. 212:417-422.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 417-422
    • García-Garcerá, M.J.1    Elfernic, M.G.L.2    Driessen, A.J.M.3    Konings, W.N.4
  • 18
    • 0343116037 scopus 로고
    • Antheprot: A software to display and analyze 3D NMR structures
    • Geourjon, C., and G. Deleage. 1995. Antheprot: a software to display and analyze 3D NMR structures. Trace Microprob. Tech. 13:337-338.
    • (1995) Trace Microprob. Tech. , vol.13 , pp. 337-338
    • Geourjon, C.1    Deleage, G.2
  • 19
    • 0023555768 scopus 로고
    • Further developments of protein secondary structure prediction using information theory: New parameters and consideration of residue pairs
    • Gibrat, J. F., J. Garnier, and B. Robson. 1987. Further developments of protein secondary structure prediction using information theory: new parameters and consideration of residue pairs. J. Mol. Biol. 198:425-443.
    • (1987) J. Mol. Biol. , vol.198 , pp. 425-443
    • Gibrat, J.F.1    Garnier, J.2    Robson, B.3
  • 21
    • 0026788013 scopus 로고
    • Mechanism of magainin 2a induced permeabilization of phospholipid vesicles
    • Grant, E., Jr., T. J. Beeler, K. M. P. Taylor, K. Gable, and M. A. Roseman. 1992. Mechanism of magainin 2a induced permeabilization of phospholipid vesicles. Biochemistry 31:9912-9918.
    • (1992) Biochemistry , vol.31 , pp. 9912-9918
    • Grant Jr., E.1    Beeler, T.J.2    Taylor, K.M.P.3    Gable, K.4    Roseman, M.A.5
  • 22
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings, J. W., M. Sailer, K. Johnson, K. L. Roy, J. C. Vederas, and M. E. Stiles. 1991. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173:7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1    Sailer, M.2    Johnson, K.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 23
    • 0026724915 scopus 로고
    • Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0
    • Henderson, J. T., A. L. Chopko, and P. D. van Wassenaar. 1992. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch. Biochem. Biophys. 295:5-12.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 5-12
    • Henderson, J.T.1    Chopko, A.L.2    Van Wassenaar, P.D.3
  • 25
    • 0028990155 scopus 로고
    • Bacteriocins of Gram-positive bacteria
    • Jack, R. W., J. R. Tagg, and B. Ray. 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
  • 26
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones, D. T., W. R. Taylor, and J. M. Thornton. 1992. A new approach to protein fold recognition. Nature 358:86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 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., and T. J. Montville. 1996. Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles. Appl. Environ. Microbiol. 62:4529-4535.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4529-4535
    • Kaiser, A.L.1    Montville, T.J.2
  • 28
    • 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
  • 29
    • 0025334980 scopus 로고
    • Improvement in protein secondary structure prediction by an enhanced neural network
    • Kneller, D. G., F. E. Cohen, and R. Langridge. 1990. Improvement in protein secondary structure prediction by an enhanced neural network. J. Mol. Biol. 214:171-182.
    • (1990) J. Mol. Biol. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 30
    • 0001877372 scopus 로고
    • Principles and applications of hurdle technology
    • G. W. Grould (ed.), Blackie Academic and Professional, Glasgow, Scotland
    • Leistner, L. 1994. Principles and applications of hurdle technology, p. 1-21. In G. W. Grould (ed.), New methods of food preservation. Blackie Academic and Professional, Glasgow, Scotland.
    • (1994) New Methods of Food Preservation , pp. 1-21
    • Leistner, L.1
  • 31
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence similarity
    • Levin, J. M., B. Robson, and J. Garnier. 1986. An algorithm for secondary structure determination in proteins based on sequence similarity. FEBS Lett. 205:303-308.
    • (1986) FEBS Lett. , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Garnier, J.3
  • 32
    • 0021104775 scopus 로고
    • Molecular dynamics of native protein. I. Computer simulation of trajectories
    • Levitt, M. 1983. Molecular dynamics of native protein. I. Computer simulation of trajectories. J. Mol. Biol. 168:595-620.
    • (1983) J. Mol. Biol. , vol.168 , pp. 595-620
    • Levitt, M.1
  • 33
    • 0011593651 scopus 로고
    • NMR studies of the solution structure of nisin A and related peptides
    • G. Jung and H.-G. Sahl (ed.), Escom Publishers, Leiden, The Netherlands
    • Lian, L. Y., W. C. Chan, S. D. Morley, G. C. K. Roberts, B. W. Bycroft, and D. Jacson. 1991. NMR studies of the solution structure of nisin A and related peptides, p. 43-58. In G. Jung and H.-G. Sahl (ed.), Nisin and novel lantibiotics. Escom Publishers, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 43-58
    • Lian, L.Y.1    Chan, W.C.2    Morley, S.D.3    Roberts, G.C.K.4    Bycroft, B.W.5    Jacson, D.6
  • 36
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • Matsuzaki, K., K. Sugishita, N. Fujii, and K. Miyajima. 1995. Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. Biochemistry 34:3423-3429.
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 38
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1995. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry 34:6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 39
    • 0000649090 scopus 로고    scopus 로고
    • Biologically-based preservation systems and probiotic bacteria
    • M. P. Doyle, L. R. Beuchat, and T. J. Montville (ed.), American Society for Microbiology Press, Washington, D.C.
    • Montville, T. J., and K. Winkowski. 1997. Biologically-based preservation systems and probiotic bacteria, p. 557-577. In M. P. Doyle, L. R. Beuchat, and T. J. Montville (ed.), Food microbiology: fundamentals and frontiers. American Society for Microbiology Press, Washington, D.C.
    • (1997) Food Microbiology: Fundamentals and Frontiers , pp. 557-577
    • Montville, T.J.1    Winkowski, K.2
  • 40
    • 0026783465 scopus 로고
    • Nucleotide and amino acid sequence of pap-gene (pediocin AcH production) in Pediococcus acidilactici H
    • Motlagh, A. M., A. K. Bhunia, F. Szostek, T. R. Hansen, M. C. Johnson, and B. Ray. 1992. Nucleotide and amino acid sequence of pap-gene (pediocin AcH production) in Pediococcus acidilactici H. Lett. Appl. Microbiol. 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
  • 41
    • 0002960529 scopus 로고
    • Characterization of liposomes
    • R. R. C. New (ed.), IRL Press, Oxford, England
    • New, R. R. C. 1992. Characterization of liposomes, p. 105-162. In R. R. C. New (ed.), Liposomes: a practical approach. IRL Press, Oxford, England.
    • (1992) Liposomes: A Practical Approach , pp. 105-162
    • New, R.R.C.1
  • 42
    • 0025761657 scopus 로고
    • Cytoplasmic pore forming proteins and peptides: Is there a common structural motif?
    • Ojcious, D. M., and J. O. E. Young. 1991. Cytoplasmic pore forming proteins and peptides: is there a common structural motif? Trends Biochem. Sci. 16:225-229.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 225-229
    • Ojcious, D.M.1    Young, J.O.E.2
  • 44
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. K., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.K.1    Lipman, D.J.2
  • 45
    • 0023812186 scopus 로고
    • Inhibition of Listeria monocytogenes by using bacteriocin PA-1 produced by Pediococcus acidilactici PAC1.0
    • Pucci, M. J., E. R. Vedamuthu, B. S. Kunka, and P. A. Vandenberg. 1988. Inhibition of Listeria monocytogenes by using bacteriocin PA-1 produced by Pediococcus acidilactici PAC1.0. Appl. Environ. Microbiol. 54:2349-2353.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 2349-2353
    • Pucci, M.J.1    Vedamuthu, E.R.2    Kunka, B.S.3    Vandenberg, P.A.4
  • 46
    • 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. Venderas, 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    Venderas, J.C.4    Stiles, M.E.5
  • 47
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins Struct. Funct. Gene. 19:55-72.
    • (1994) Proteins Struct. Funct. Gene. , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 48
    • 0028177807 scopus 로고
    • Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices structure
    • Ryu S. E., A. Truneh, R. W. Sweet, and W. A. Hendrickson. 1994. Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices structure. Structure 2:59-74.
    • (1994) Structure , vol.2 , pp. 59-74
    • Ryu, S.E.1    Truneh, A.2    Sweet, R.W.3    Hendrickson, W.A.4
  • 49
    • 0027339076 scopus 로고
    • 15N- and 13C-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin A from Leuconostoc gelidum and nisin A from Lactococcus lactis
    • Sailer, M., G. L. Helms, T. Henkel, W. P. Niemczura, M. E. Stiles, and J. C. Vederas. 1992. 15N-and 13C-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin A from Leuconostoc gelidum and nisin A from Lactococcus lactis. Biochemistry 32:310-318.
    • (1992) Biochemistry , vol.32 , pp. 310-318
    • Sailer, M.1    Helms, G.L.2    Henkel, T.3    Niemczura, W.P.4    Stiles, M.E.5    Vederas, J.C.6
  • 50
    • 0026704815 scopus 로고
    • Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of unknown protein conformations
    • Sippl, M. J., and S. Weitckus. 1992. Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of unknown protein conformations. Proteins 13:258-271.
    • (1992) Proteins , vol.13 , pp. 258-271
    • Sippl, M.J.1    Weitckus, S.2
  • 51
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T. F., and M. S. Waterman. 1981. Identification of common molecular subsequences. J. Mol. Biol. 147:195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 52
    • 0026332723 scopus 로고
    • The bacteriocin lactococcin A specifically increases the permeability of lactococcal cytoplasmic membranes in a voltage-independent protein-mediated manner
    • van Belkum, M. J., J. Kok, G. Venema, H. Holo, I. F. Nes, W. N. Konings, and T. Abee. 1991. The bacteriocin lactococcin A specifically increases the permeability of lactococcal cytoplasmic membranes in a voltage-independent protein-mediated manner. J. Bacteriol. 173:7934-7941.
    • (1991) J. Bacteriol. , vol.173 , pp. 7934-7941
    • Van Belkum, M.J.1    Kok, J.2    Venema, G.3    Holo, H.4    Nes, I.F.5    Konings, W.N.6    Abee, T.7
  • 54
    • 0002821064 scopus 로고
    • The spatial structure of nisin in aqueous solution
    • G. Jung and H.-G. Sahl (ed.), Escom Publishers, Leiden, The Netherlands
    • van de Ven, F. J. M., H. W. van den Hooven, R. N. H. Konings, and C. W. Hilbers. 1991. The spatial structure of nisin in aqueous solution, p. 35-42. In G. Jung and H.-G. Sahl (ed.), Nisin and novel lantibiotics. Escom Publishers, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 35-42
    • Van De Ven, F.J.M.1    Van Den Hooven, H.W.2    Konings, R.N.H.3    Hilbers, C.W.4
  • 55
    • 0343987972 scopus 로고
    • Lactococcins: Mode of action, immunity and secretion
    • Venema, K., G. Venema, and J. Kok. 1995. Lactococcins: mode of action, immunity and secretion. Int. Dairy J. 5:815-832.
    • (1995) Int. Dairy J. , vol.5 , pp. 815-832
    • Venema, K.1    Venema, G.2    Kok, J.3
  • 56
    • 0029664334 scopus 로고    scopus 로고
    • Physicochemical characterization of the nisin-membrane interaction with liposomes derived from Listeria monocytogenes
    • Winkowski, K., R. D. Ludescher, and T. J. Montville. 1996. Physicochemical characterization of the nisin-membrane interaction with liposomes derived from Listeria monocytogenes. Appl. Environ. Microbiol. 62:323-327.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 323-327
    • Winkowski, K.1    Ludescher, R.D.2    Montville, T.J.3


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