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Volumn 51, Issue 2, 2007, Pages 468-474

Activities of antimicrobial peptides and synergy with enrofloxacin against Mycoplasma pulmonis

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; ENROFLOXACIN; GLOBOMYCIN; GRAMICIDIN S; POLYPEPTIDE ANTIBIOTIC AGENT; QUINOLINE DERIVED ANTIINFECTIVE AGENT; SURFACTIN;

EID: 33846618655     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.01030-06     Document Type: Article
Times cited : (48)

References (27)
  • 1
    • 1842454152 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides: Update of clinical development
    • Andres, E., and J. L. Dimarcq. 2004. Cationic antimicrobial peptides: update of clinical development. J. Intern. Med. 255:519-520.
    • (2004) J. Intern. Med , vol.255 , pp. 519-520
    • Andres, E.1    Dimarcq, J.L.2
  • 2
    • 33645119801 scopus 로고    scopus 로고
    • A. Blanchard and G. Browning ed, Mycoplasmas. Molecular biology, pathogenicity, and strategies for control. Horizon Bioscience, Norfolk, United Kingdom
    • Bébéar, C. M., and I. Kempt. 2005. Antimicrobial therapy and antimicrobial resistance, p. 535-568. In A. Blanchard and G. Browning (ed.), Mycoplasmas. Molecular biology, pathogenicity, and strategies for control. Horizon Bioscience, Norfolk, United Kingdom.
    • (2005) Antimicrobial therapy and antimicrobial resistance , pp. 535-568
    • Bébéar, C.M.1    Kempt, I.2
  • 3
    • 0029859561 scopus 로고    scopus 로고
    • Inhibition of spiralin processing by the lipopeptide antibiotic globomycin
    • Béven, L., M. Le Henaff, C. Fontenelle, and H. Wróblewski. 1996. Inhibition of spiralin processing by the lipopeptide antibiotic globomycin. Curr. Microbiol. 33:317-322.
    • (1996) Curr. Microbiol , vol.33 , pp. 317-322
    • Béven, L.1    Le Henaff, M.2    Fontenelle, C.3    Wróblewski, H.4
  • 4
    • 0031060732 scopus 로고    scopus 로고
    • Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes
    • Béven, L., and H. Wróblewski. 1997. Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes. Res. Microbiol. 148:163-175.
    • (1997) Res. Microbiol , vol.148 , pp. 163-175
    • Béven, L.1    Wróblewski, H.2
  • 5
    • 0038526871 scopus 로고    scopus 로고
    • Mycoplasmas of humans
    • S. A. Razin and R. Herrmann ed, Kluwer Academic Plenum, New York, NY
    • Blanchard, A., and C. M. Bébéar. 2002. Mycoplasmas of humans, p. 45-71. In S. A. Razin and R. Herrmann (ed.), Molecular biology and pathogenicity of mycoplasmas. Kluwer Academic Plenum, New York, NY.
    • (2002) Molecular biology and pathogenicity of mycoplasmas , pp. 45-71
    • Blanchard, A.1    Bébéar, C.M.2
  • 6
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman, H. G. 2003. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254:197-215.
    • (2003) J. Intern. Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 7
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. 2005. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3:238-250.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 8
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown, K. L., and R. E. Hancock. 2006. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 18:24-30.
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 9
    • 0033385551 scopus 로고    scopus 로고
    • Interactions between mycoplasma lipoproteins and the host immune system
    • Chambaud, I., H. Wróblewski, and A. Blanchard. 1999. Interactions between mycoplasma lipoproteins and the host immune system. Trends Microbiol. 7:493-499.
    • (1999) Trends Microbiol , vol.7 , pp. 493-499
    • Chambaud, I.1    Wróblewski, H.2    Blanchard, A.3
  • 10
    • 23044472138 scopus 로고    scopus 로고
    • Dartois, V., J. Sanchez-Quesada, E. Cabezas, E. Chi, C. Dubbelde, C. Dunn, J. Granja, C. Gritzen, D. Weinberger, M. R. Ghadiri, and T. R. Parr, Jr. 2005. Systemic antibacterial activity of novel synthetic cyclic peptides. Antimicrob. Agents Chemother. 49:3302-3310.
    • Dartois, V., J. Sanchez-Quesada, E. Cabezas, E. Chi, C. Dubbelde, C. Dunn, J. Granja, C. Gritzen, D. Weinberger, M. R. Ghadiri, and T. R. Parr, Jr. 2005. Systemic antibacterial activity of novel synthetic cyclic peptides. Antimicrob. Agents Chemother. 49:3302-3310.
  • 11
    • 0021800753 scopus 로고
    • Inhibition of prolipoprotein signal peptidase by globomycin
    • Dev, I. K., R. J. Harvey, and P. H. Ray. 1985. Inhibition of prolipoprotein signal peptidase by globomycin. J. Biol. Chem. 260:5891-5894.
    • (1985) J. Biol. Chem , vol.260 , pp. 5891-5894
    • Dev, I.K.1    Harvey, R.J.2    Ray, P.H.3
  • 12
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependant pore formation and antimicrobial activity by alamethicin and analogues
    • Duclohier, H., and H. Wróblewski. 2001. Voltage-dependant pore formation and antimicrobial activity by alamethicin and analogues. J. Membrane Biol. 184:1-12.
    • (2001) J. Membrane Biol , vol.184 , pp. 1-12
    • Duclohier, H.1    Wróblewski, H.2
  • 13
    • 4243213733 scopus 로고    scopus 로고
    • V. Lorian ed, Antibiotics in laboratory medicine. Williams and Wilkins, Baltimore, MD
    • Eliopoulos, G., and J. R. Moellering. 1996. Antimicrobial combinations, p. 330-393. In V. Lorian (ed.), Antibiotics in laboratory medicine. Williams and Wilkins, Baltimore, MD.
    • (1996) Antimicrobial combinations , pp. 330-393
    • Eliopoulos, G.1    Moellering, J.R.2
  • 15
    • 0345338163 scopus 로고    scopus 로고
    • Mycoplasmas of animals
    • S. A. Razin and R. Herrmann ed, Kluwer Academic Plenum, New York, NY
    • Frey, J. 2002. Mycoplasmas of animals, p. 73-90. In S. A. Razin and R. Herrmann (ed.), Molecular biology and pathogenicity of mycoplasmas. Kluwer Academic Plenum, New York, NY.
    • (2002) Molecular biology and pathogenicity of mycoplasmas , pp. 73-90
    • Frey, J.1
  • 16
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E., and R. Lehrer. 1998. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:82-88.
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 17
    • 0037099371 scopus 로고    scopus 로고
    • Role of upper and lower respiratory tract immunity in resistance to Mycoplasma respiratory disease
    • Hodge, L. M., and J. W. Simecka. 2002. Role of upper and lower respiratory tract immunity in resistance to Mycoplasma respiratory disease. J. Infect. Dis. 186:290-294.
    • (2002) J. Infect. Dis , vol.186 , pp. 290-294
    • Hodge, L.M.1    Simecka, J.W.2
  • 18
    • 0019458461 scopus 로고
    • Voltage-dependent channels in planar lipid bilayer membranes
    • Latorre, R., and O. Alvarez. 1981. Voltage-dependent channels in planar lipid bilayer membranes. Physiol. Rev. 61:77-150.
    • (1981) Physiol. Rev , vol.61 , pp. 77-150
    • Latorre, R.1    Alvarez, O.2
  • 19
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: Obstacles and realistic outlook
    • Marr, A. K., W. J. Gooderham, and R. E. W. Hancock. 2006. Antibacterial peptides for therapeutic use: obstacles and realistic outlook. Curr. Opin. Pharmacol. 6:468-472.
    • (2006) Curr. Opin. Pharmacol , vol.6 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.W.3
  • 20
    • 0036241412 scopus 로고    scopus 로고
    • Susceptibilities of Mycoplasma fermentans and Mycoplasma hyorhinis to membrane-active peptides and enrofloxacin in human tissue cell cultures
    • Nir-Paz, R., M. C. Prevost, P. Nicolas, A. Blanchard, and H. Wróblewski. 2002. Susceptibilities of Mycoplasma fermentans and Mycoplasma hyorhinis to membrane-active peptides and enrofloxacin in human tissue cell cultures. Antimicrob. Agents Chemother. 46:1218-1225.
    • (2002) Antimicrob. Agents Chemother , vol.46 , pp. 1218-1225
    • Nir-Paz, R.1    Prevost, M.C.2    Nicolas, P.3    Blanchard, A.4    Wróblewski, H.5
  • 21
    • 0038601510 scopus 로고    scopus 로고
    • Synergy, antagonism, and what the chequerboard puts between them
    • Odds, F. C. 2003. Synergy, antagonism, and what the chequerboard puts between them. J. Antimicrob. Chemother. 52:1.
    • (2003) J. Antimicrob. Chemother , vol.52 , pp. 1
    • Odds, F.C.1
  • 24
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner, E. J., R. N. Lewis, and R. N. McElhaney. 1999. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim. Biophys. Acta 1462:201-221.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.2    McElhaney, R.N.3
  • 25
    • 0002082310 scopus 로고    scopus 로고
    • The peptaibol antibiotics from Trichoderma soil fungi; structural diversity and membrane properties
    • Rebuffat, S., C. Goulard, B. Bodo, and M.-F. Roquebert. 1999. The peptaibol antibiotics from Trichoderma soil fungi; structural diversity and membrane properties. Recent Res. Dev. Org. Bioorg. Chem. 3:65-91.
    • (1999) Recent Res. Dev. Org. Bioorg. Chem , vol.3 , pp. 65-91
    • Rebuffat, S.1    Goulard, C.2    Bodo, B.3    Roquebert, M.-F.4
  • 27
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of muticellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of muticellular organisms. Nature 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


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