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Volumn 72, Issue 4, 2006, Pages 2809-2814

Lipid II-based antimicrobial activity of the lantibiotic plantaricin C

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BACTERIA; CELLS; LIPIDS; THIN LAYER CHROMATOGRAPHY;

EID: 33646080127     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.72.4.2809-2814.2006     Document Type: Article
Times cited : (75)

References (35)
  • 1
    • 0021905348 scopus 로고
    • Induction of autolysis of staphylococci by the basic peptide antibiotic Pep5 and nisin and their influence on the activity of autolytic enzymes
    • Bierbaum, G., and H. G. Sahl. 1985. Induction of autolysis of staphylococci by the basic peptide antibiotic Pep5 and nisin and their influence on the activity of autolytic enzymes. Arch. Microbiol. 141:249-254.
    • (1985) Arch. Microbiol. , vol.141 , pp. 249-254
    • Bierbaum, G.1    Sahl, H.G.2
  • 3
    • 33645779735 scopus 로고    scopus 로고
    • Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode of action studies
    • Bonelli, R. R., T. Schneider, H. G. Sahl, and I. Wiedemann. 2006. Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode of action studies. Antimicrob. Agents Chemother. 50:1449-1457.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1449-1457
    • Bonelli, R.R.1    Schneider, T.2    Sahl, H.G.3    Wiedemann, I.4
  • 5
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • Brötz, H., G. Bierbaum, P. E. Reynolds, and H. G. Sahl. 1997. The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation. Eur. J. Biochem. 246:193-199.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 193-199
    • Brötz, H.1    Bierbaum, G.2    Reynolds, P.E.3    Sahl, H.G.4
  • 6
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • Brötz, H., M. Josten, I. Wiedemann, U. Schneider, F. Götz, G. Bierbaum, and H. G. Sahl. 1998. Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 30:317-327.
    • (1998) Mol. Microbiol. , vol.30 , pp. 317-327
    • Brötz, H.1    Josten, M.2    Wiedemann, I.3    Schneider, U.4    Götz, F.5    Bierbaum, G.6    Sahl, H.G.7
  • 8
    • 13844314218 scopus 로고    scopus 로고
    • Bacterial lantibiotics: Strategies to improve therapeutic potential
    • Cotter, P. D., C. Hill, and R. P. Ross. 2005. Bacterial lantibiotics: strategies to improve therapeutic potential. Curr. Protein Pept. Sci. 6:61-75.
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 61-75
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 9
    • 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
  • 10
    • 0036216314 scopus 로고    scopus 로고
    • Ribosomally synthesized antibacterial peptides in Gram positive bacteria
    • Diep, D. B., and I. F. Nes. 2002. Ribosomally synthesized antibacterial peptides in Gram positive bacteria. Curr. Drug Targets 3:107-122.
    • (2002) Curr. Drug Targets , vol.3 , pp. 107-122
    • Diep, D.B.1    Nes, I.F.2
  • 11
    • 0028238737 scopus 로고
    • Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin
    • Gonzalez, B., P. Area, B. Mayo, and J. E. Suárez. 1994. Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin. Appl. Environ. Microbiol. 60:2158-2163.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2158-2163
    • Gonzalez, B.1    Area, P.2    Mayo, B.3    Suárez, J.E.4
  • 13
    • 0033851437 scopus 로고    scopus 로고
    • Posttranslationally modified bacteriocins - The lantibiotics
    • Guder, A., I. Wiedemann, and H. G. Sahl. 2000. Posttranslationally modified bacteriocins-the lantibiotics. Biopolymers 55:62-73.
    • (2000) Biopolymers , vol.55 , pp. 62-73
    • Guder, A.1    Wiedemann, I.2    Sahl, H.G.3
  • 14
    • 0037699956 scopus 로고    scopus 로고
    • NMR study of mersacidin and lipid 11 interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity
    • Hsu, S. T., E. Breukink, G. Bierbaum, H. G. Sahl, B. De Kruijff, R. Kaptein, N. A. van Nuland, and A. M. Bonvin. 2003. NMR study of mersacidin and lipid 11 interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity. J. Biol. Chem. 278:13110-13117.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13110-13117
    • Hsu, S.T.1    Breukink, E.2    Bierbaum, G.3    Sahl, H.G.4    De Kruijff, B.5    Kaptein, R.6    Van Nuland, N.A.7    Bonvin, A.M.8
  • 16
    • 0003148144 scopus 로고
    • Lantibiotics: A survey
    • G. Jung and H. Sahl (ed.). ESCOM Science Publishers, Leiden, The Netherlands
    • Jung, G. 1991. Lantibiotics: a survey, p. 1-34. In G. Jung and H. Sahl (ed.), Nisin and novel lantibiotics. ESCOM Science Publishers, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 1-34
    • Jung, G.1
  • 18
  • 19
    • 0036008798 scopus 로고    scopus 로고
    • Potassium release, a useful tool for studying antimicrobial peptides
    • Orlov, D. S., T. Nguyen, and R. I. Lehrer. 2002. Potassium release, a useful tool for studying antimicrobial peptides. J. Microbiol. Methods 49:325-328.
    • (2002) J. Microbiol. Methods , vol.49 , pp. 325-328
    • Orlov, D.S.1    Nguyen, T.2    Lehrer, R.I.3
  • 20
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dit operon in Staphylococcus aureus confers sensitivity to defensins, protegrins and other antimicrobial peptides
    • Peschel, A., M. Otto, R. W. Jack, H. Kalbacher, G. Jung, and F. Götz. 1999. Inactivation of the dit operon in Staphylococcus aureus confers sensitivity to defensins, protegrins and other antimicrobial peptides. J. Biol. Chem. 274:8405-8410.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Götz, F.6
  • 22
    • 0031841034 scopus 로고    scopus 로고
    • Characterization of the lipid-carrier involved in the synthesis of enterobacterial common antigen (ECA) and identification of a novel phosphoglyceride in a mutant of Salmonella typhimurium defective in ECA synthesis
    • Rick, P. D., G. L. Hubbard, M. Kitaoka, H. Nagaki, T. Kinoshita, S. Dowd, V. Simplaceanu, and C. Ho. 1998. Characterization of the lipid-carrier involved in the synthesis of enterobacterial common antigen (ECA) and identification of a novel phosphoglyceride in a mutant of Salmonella typhimurium defective in ECA synthesis. Glycobiology 8:557-567.
    • (1998) Glycobiology , vol.8 , pp. 557-567
    • Rick, P.D.1    Hubbard, G.L.2    Kitaoka, M.3    Nagaki, H.4    Kinoshita, T.5    Dowd, S.6    Simplaceanu, V.7    Ho, C.8
  • 23
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles
    • Ruhr, E., and H. G. Sahl. 1985. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob. Agents Chemother. 27:841-845.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 24
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl, H. G., and G. Bierbaum. 1998. Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu. Rev. Microbiol. 52:41-79.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-79
    • Sahl, H.G.1    Bierbaum, G.2
  • 25
    • 3242890388 scopus 로고    scopus 로고
    • In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-GIy5) of Staphylococcus aureus
    • Schneider, T., M. M. Senn, B. Berger-Bachi, A. Tossi, H. G. Sahl, and I. Wiedemann. 2004. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-GIy5) of Staphylococcus aureus. Mol. Microbiol. 53:675-685.
    • (2004) Mol. Microbiol. , vol.53 , pp. 675-685
    • Schneider, T.1    Senn, M.M.2    Berger-Bachi, B.3    Tossi, A.4    Sahl, H.G.5    Wiedemann, I.6
  • 26
    • 0038155138 scopus 로고    scopus 로고
    • Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin
    • Szekat, C., R. W. Jack, D. Skutlarek, H. Farber, and G. Bierbaum. 2003. Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin. Appl. Environ. Microbiol. 69:3777-3783.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3777-3783
    • Szekat, C.1    Jack, R.W.2    Skutlarek, D.3    Farber, H.4    Bierbaum, G.5
  • 27
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi, A., L. Sandri, and A. Giangaspero. 2000. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55:4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 29
    • 0035018011 scopus 로고    scopus 로고
    • Formation of the glycan chains in the synthesis of bacterial peptidoglycan
    • van Heijenoort, J. 2001. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11:25R-36R.
    • (2001) Glycobiology , vol.11
    • Van Heijenoort, J.1
  • 30
    • 0034625012 scopus 로고    scopus 로고
    • Correlation between the structure of the bacterial peptidoglycan monomer unit, the specificity of transpeptidation, and susceptibility to β-lactams
    • van Heijenoort, J., and L. Gutmann. 2000. Correlation between the structure of the bacterial peptidoglycan monomer unit, the specificity of transpeptidation, and susceptibility to β-lactams. Proc. Natl. Acad. Sci. USA 97:5028-5030.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5028-5030
    • Van Heijenoort, J.1    Gutmann, L.2
  • 32
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I., E. Breukink, C. van Kraaij, O. P. Kuipers, G. Bierbaum, B. De Kruijff, and H. G. Sahl. 2001. Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. 276:1772-1779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    De Kruijff, B.6    Sahl, H.G.7
  • 33
    • 2342498649 scopus 로고    scopus 로고
    • Lipid II-mediated pore formation by the peptide antibiotic nisin: A black lipid membrane study
    • Wiedemann, I., R. Benz, and H. G. Sahl. 2004. Lipid II-mediated pore formation by the peptide antibiotic nisin: a black lipid membrane study. J. Bacteriol. 186:3259-3261.
    • (2004) J. Bacteriol. , vol.186 , pp. 3259-3261
    • Wiedemann, I.1    Benz, R.2    Sahl, H.G.3
  • 34
    • 4644372683 scopus 로고    scopus 로고
    • Post-translational modifications during lantibiotic biosynthesis
    • Xie, L., and W. A. van der Donk. 2004. Post-translational modifications during lantibiotic biosynthesis. Curr. Opin. Chem. Biol. 8:498-507.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 498-507
    • Xie, L.1    Van Der Donk, W.A.2
  • 35
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


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